DEHA2E20130p_blastp.html 
BLASTP 2.2.18 [Mar-02-2008]


Reference: Altschul, Stephen F., Thomas L. Madden, Alejandro A. Schaffer, 
Jinghui Zhang, Zheng Zhang, Webb Miller, and David J. Lipman (1997), 
"Gapped BLAST and PSI-BLAST: a new generation of protein database search
programs",  Nucleic Acids Res. 25:3389-3402.

Reference for compositional score matrix adjustment: Altschul, Stephen F., 
John C. Wootton, E. Michael Gertz, Richa Agarwala, Aleksandr Morgulis,
Alejandro A. Schaffer, and Yi-Kuo Yu (2005) "Protein database searches
using compositionally adjusted substitution matrices", FEBS J. 272:5101-5109.

Query= DEHA2E20130p (infer) YLR100W ERG27 3-keto sterol reductase
catalyzes the last of three steps required to remove two C-4 methyl
groups from an intermediate in ergosterol biosynthesis : similar to
uniprot|Q12452 Saccharomyces cerevisiae [Debaryomyces hansenii CBS767]
         (346 letters)

Database: Genolevures3.aa 
           48,939 sequences; 23,992,848 total letters

Searching..................................................done



                                                                 Score    E
Sequences producing significant alignments:                      (bits) Value

|DEHA2E20130p (infer) YLR100W ERG27 3-keto sterol reductase catal...   715   0.0  
|SAKL0H16368p (infer) YLR100W ERG27 3-keto sterol reductase catal...   437   e-123
|KLTH0G13046p (infer) YLR100W ERG273-keto sterol reductase cataly...   431   e-121
|SACE0L03674p 3-keto sterol reductase, catalyzes the last of thre...   418   e-117
|ZYRO0D06534p (infer) YLR100W ERG27 3-keto sterol reductase catal...   417   e-116
|KLLA0F19756p (infer) YLR100W ERG27 3-keto sterol reductase catal...   417   e-116
|CAGL0M11506p (infer) YLR100w ERG27 3-keto sterol reductase : hig...   414   e-116
|ERGO0G09878p Syntenic homolog of Saccharomyces cerevisiae YLR100...   396   e-110
|YALI0B17644p (infer) ORF YLR100W ERG27 3-keto sterol reductase s...   254   1e-67


>|DEHA2E20130p (infer) YLR100W ERG27 3-keto sterol reductase catalyzes the last of
           three steps required to remove two C-4 methyl groups
           from an intermediate in ergosterol biosynthesis :
           similar to uniprot|Q12452 Saccharomyces cerevisiae
           [Debaryomyces hansenii CBS767]
          Length = 346

 Score =  715 bits (1846), Expect = 0.0,   Method: Compositional matrix adjust.
 Identities = 346/346 (100%), Positives = 346/346 (100%)

Query: 1   MIKDNDNSKVALITGTSSNLGINIAYRLLEQLPSSTNVTLIVTSRTLPKVKEVITNINQY 60
           MIKDNDNSKVALITGTSSNLGINIAYRLLEQLPSSTNVTLIVTSRTLPKVKEVITNINQY
Sbjct: 1   MIKDNDNSKVALITGTSSNLGINIAYRLLEQLPSSTNVTLIVTSRTLPKVKEVITNINQY 60

Query: 61  SKTKLNRTGQLEFDYLLVDFTDMVSVLSAYYDLNKKFKKIDYLFVNAAQGVYSGIDWVAA 120
           SKTKLNRTGQLEFDYLLVDFTDMVSVLSAYYDLNKKFKKIDYLFVNAAQGVYSGIDWVAA
Sbjct: 61  SKTKLNRTGQLEFDYLLVDFTDMVSVLSAYYDLNKKFKKIDYLFVNAAQGVYSGIDWVAA 120

Query: 121 TKEICRNPMEGVTNPTYKTQRVGVKSNDNMGLVFQANVFGPYYLIHKIKHLLQKGGRIIW 180
           TKEICRNPMEGVTNPTYKTQRVGVKSNDNMGLVFQANVFGPYYLIHKIKHLLQKGGRIIW
Sbjct: 121 TKEICRNPMEGVTNPTYKTQRVGVKSNDNMGLVFQANVFGPYYLIHKIKHLLQKGGRIIW 180

Query: 181 ISSLMSNPKYLSFNDLQLLKSPESYEGSKRLVDLMHFGTFKQLQSEYGIEQYLVQPGIFT 240
           ISSLMSNPKYLSFNDLQLLKSPESYEGSKRLVDLMHFGTFKQLQSEYGIEQYLVQPGIFT
Sbjct: 181 ISSLMSNPKYLSFNDLQLLKSPESYEGSKRLVDLMHFGTFKQLQSEYGIEQYLVQPGIFT 240

Query: 241 SFSFFKFLNVFTYYSMLMLFYLARLFGSPSHNISGFIAANAPVTCALGNESQSVKVCSVS 300
           SFSFFKFLNVFTYYSMLMLFYLARLFGSPSHNISGFIAANAPVTCALGNESQSVKVCSVS
Sbjct: 241 SFSFFKFLNVFTYYSMLMLFYLARLFGSPSHNISGFIAANAPVTCALGNESQSVKVCSVS 300

Query: 301 NRTGKEYLSYQEVDTTGSADISAYLEKLCHEWDLTLKDQIVNTRQP 346
           NRTGKEYLSYQEVDTTGSADISAYLEKLCHEWDLTLKDQIVNTRQP
Sbjct: 301 NRTGKEYLSYQEVDTTGSADISAYLEKLCHEWDLTLKDQIVNTRQP 346


>|SAKL0H16368p (infer) YLR100W ERG27 3-keto sterol reductase catalyzes the last of
           three steps required to remove two C-4 methyl groups
           from an intermediate in ergosterol biosynthesis mutants
           are sterol auxotrophs : highly similar to uniprot|Q12452
           Saccharomyces cerevisiae [Lachancea kluyveri]
          Length = 346

 Score =  437 bits (1125), Expect = e-123,   Method: Compositional matrix adjust.
 Identities = 217/343 (63%), Positives = 262/343 (76%), Gaps = 7/343 (2%)

Query: 9   KVALITGTSSNLGINIAYRLLEQLPSSTNVTLIVTSRTLPKVKEVITNINQYSKTKLNRT 68
           K+A+ITGT+SNLG+NIAYRL+++L   T +T++VTSRTLP+ +EVI  IN Y + +  RT
Sbjct: 5   KIAVITGTNSNLGLNIAYRLIKKLDPETRITIVVTSRTLPRAREVIDQINAYVE-RSGRT 63

Query: 69  GQLEFDYLLVDFTDMVSVLSAYYDLNKKFKKIDYLFVNAAQGVYSGIDWVAATKEICRNP 128
           G ++FDYLLVDFT+MVSVLSAYYDLNK++K+I+Y FVNAAQGVY GIDW  A KE+C NP
Sbjct: 64  GIVDFDYLLVDFTNMVSVLSAYYDLNKRYKEINYFFVNAAQGVYEGIDWFGAIKEVCANP 123

Query: 129 MEGVTNPTYKTQRVGVKSNDNMGLVFQANVFGPYYLIHKIKHLLQKG-GRIIWISSLMSN 187
           +E VTNPTYK QRVGV S D MGLVFQANVFGPYYLI K+   L  G   I+WISS+MSN
Sbjct: 124 LEAVTNPTYKIQRVGVTSKDGMGLVFQANVFGPYYLIQKLIPQLSAGKANIVWISSIMSN 183

Query: 188 PKYLSFNDLQLLKSPESYEGSKRLVDLMHFGTFKQLQSEYGIEQYLVQPGIFTSFSFFKF 247
           PKYLS  D++LLK+  SYEGSKRLVDL+H  T+K ++  +GI QY+ QPGIFTS SFFK+
Sbjct: 184 PKYLSLQDIELLKTNASYEGSKRLVDLLHLATYKDMKL-HGIHQYVTQPGIFTSHSFFKY 242

Query: 248 LNVFTYYSMLMLFYLARLFGSPSHNISGFIAANAPVTCA-LGN---ESQSVKVCSVSNRT 303
           LN FTYY ML+LFY AR  GS  HNI G+ AANAPV  A L N   E Q +K  S + R 
Sbjct: 243 LNFFTYYGMLLLFYFARWIGSEWHNIDGYKAANAPVYAATLANPNFEGQQLKYGSATYRD 302

Query: 304 GKEYLSYQEVDTTGSADISAYLEKLCHEWDLTLKDQIVNTRQP 346
           G EY+  QE+D TGS DI A+++ L  EWD  LKDQI NTR P
Sbjct: 303 GMEYIKTQEIDPTGSHDIYAHIKHLEKEWDEKLKDQITNTRIP 345


>|KLTH0G13046p (infer) YLR100W ERG273-keto sterol reductase catalyzes the last of
           three steps required to remove two C-4 methyl groups
           from an intermediate in ergosterol biosynthesis mutants
           are sterol auxotrophs : similar to uniprot|Q12452
           Saccharomyces cerevisiae [Kluyveromyces thermotolerans]
          Length = 347

 Score =  431 bits (1107), Expect = e-121,   Method: Compositional matrix adjust.
 Identities = 212/344 (61%), Positives = 263/344 (76%), Gaps = 7/344 (2%)

Query: 7   NSKVALITGTSSNLGINIAYRLLEQLPSSTNVTLIVTSRTLPKVKEVITNINQYSKTKLN 66
           + KVA+ITGT+SNLG+N AYRL+++L     +T++VTSRTLP+ +EVI NI  +   K +
Sbjct: 4   DRKVAVITGTNSNLGLNTAYRLIQELDQDVRLTIVVTSRTLPRAREVIDNIKDFV-GKSS 62

Query: 67  RTGQLEFDYLLVDFTDMVSVLSAYYDLNKKFKKIDYLFVNAAQGVYSGIDWVAATKEICR 126
           R G +++DYLLVDFTDMVS L+AYY+LNK +K+I+Y FVNAAQGVYSGIDW+ A KE+  
Sbjct: 63  RPGLVDYDYLLVDFTDMVSTLNAYYELNKHYKEINYFFVNAAQGVYSGIDWLGAVKEVFT 122

Query: 127 NPMEGVTNPTYKTQRVGVKSNDNMGLVFQANVFGPYYLIHKIKHLLQKG-GRIIWISSLM 185
           NP+E VTNPTYK QRVGVKS D MGLVFQANVFGPYYLI KI   LQ G   ++WISS+M
Sbjct: 123 NPIEAVTNPTYKIQRVGVKSQDGMGLVFQANVFGPYYLIQKILPQLQAGKAVVVWISSIM 182

Query: 186 SNPKYLSFNDLQLLKSPESYEGSKRLVDLMHFGTFKQLQSEYGIEQYLVQPGIFTSFSFF 245
           S+PKYLS  D++L+KSP SYEGSKRLVDL+H  T+K+L+ + GI QY+VQPGIF S SFF
Sbjct: 183 SDPKYLSLEDIELVKSPASYEGSKRLVDLLHLATYKELKGQ-GIHQYVVQPGIFISHSFF 241

Query: 246 KFLNVFTYYSMLMLFYLARLFGSPSHNISGFIAANAPVTCA-LGN---ESQSVKVCSVSN 301
           K+LNV +YY ML+LFY AR  GSP HNI G+ AANAPV  A L N   E Q+VK  S + 
Sbjct: 242 KYLNVLSYYGMLLLFYFARFLGSPWHNIDGYRAANAPVYVATLANPTFEQQNVKYGSATY 301

Query: 302 RTGKEYLSYQEVDTTGSADISAYLEKLCHEWDLTLKDQIVNTRQ 345
           + G EY+  QE++ TG  D+  YL+KL   WD  LKDQI N+RQ
Sbjct: 302 KDGMEYIRTQEIEATGVHDVYVYLKKLKDVWDDKLKDQITNSRQ 345


>|SACE0L03674p 3-keto sterol reductase, catalyzes the last of three steps required
           to remove two C-4 methyl groups from an intermediate in
           ergosterol biosynthesis; mutants are sterol auxotrophs
           [Saccharomyces cerevisiae]
          Length = 347

 Score =  418 bits (1075), Expect = e-117,   Method: Compositional matrix adjust.
 Identities = 208/346 (60%), Positives = 263/346 (76%), Gaps = 7/346 (2%)

Query: 7   NSKVALITGTSSNLGINIAYRLLEQLPSSTNVTLIVTSRTLPKVKEVITNINQ-YSKTKL 65
           N KVA++TGT+SNLG+NI +RL+E   ++  +T++VTSRTLP+V+EVI  I   Y+K+  
Sbjct: 2   NRKVAIVTGTNSNLGLNIVFRLIETEDTNVRLTIVVTSRTLPRVQEVINQIKDFYNKSGR 61

Query: 66  NRTGQLEFDYLLVDFTDMVSVLSAYYDLNKKFKKIDYLFVNAAQGVYSGIDWVAATKEIC 125
               +++FDYLLVDFT+MVSVL+AYYD+NKK++ I+YLFVNAAQG++ GIDW+ A KE+ 
Sbjct: 62  VEDLEIDFDYLLVDFTNMVSVLNAYYDINKKYRAINYLFVNAAQGIFDGIDWIGAVKEVF 121

Query: 126 RNPMEGVTNPTYKTQRVGVKSNDNMGLVFQANVFGPYYLIHKIKHLLQKG-GRIIWISSL 184
            NP+E VTNPTYK Q VGVKS D+MGL+FQANVFGPYY I KI   L +G   I+WISS+
Sbjct: 122 TNPLEAVTNPTYKIQLVGVKSKDDMGLIFQANVFGPYYFISKILPQLTRGKAYIVWISSI 181

Query: 185 MSNPKYLSFNDLQLLKSPESYEGSKRLVDLMHFGTFKQLQSEYGIEQYLVQPGIFTSFSF 244
           MS+PKYLS ND++LLK+  SYEGSKRLVDL+H  T+K L+ + GI QY+VQPGIFTS SF
Sbjct: 182 MSDPKYLSLNDIELLKTNASYEGSKRLVDLLHLATYKDLK-KLGINQYVVQPGIFTSHSF 240

Query: 245 FKFLNVFTYYSMLMLFYLARLFGSPSHNISGFIAANAPV-TCALGN---ESQSVKVCSVS 300
            ++LN FTY+ ML LFYLARL GSP HNI G+ AANAPV    L N   E Q VK  S +
Sbjct: 241 SEYLNFFTYFGMLCLFYLARLLGSPWHNIDGYKAANAPVYVTRLANPNFEKQDVKYGSAT 300

Query: 301 NRTGKEYLSYQEVDTTGSADISAYLEKLCHEWDLTLKDQIVNTRQP 346
           +R G  Y+  QE+D TG +D+ AY++K   EWD  LKDQIV TR P
Sbjct: 301 SRDGMPYIKTQEIDPTGMSDVFAYIQKKKLEWDEKLKDQIVETRTP 346


>|ZYRO0D06534p (infer) YLR100W ERG27 3-keto sterol reductase catalyzes the last of
           three steps required to remove two C-4 methyl groups
           from an intermediate in ergosterol biosynthesis mutants
           are sterol auxotrophs : similar to uniprot|Q12452
           Saccharomyces cerevisiae [Zygosaccharomyces rouxii]
          Length = 346

 Score =  417 bits (1072), Expect = e-116,   Method: Compositional matrix adjust.
 Identities = 209/342 (61%), Positives = 257/342 (75%), Gaps = 7/342 (2%)

Query: 9   KVALITGTSSNLGINIAYRLLEQLPSSTNVTLIVTSRTLPKVKEVITNINQYSKTKLNRT 68
           KVA+ITGT+SNLG+NIAYRL+EQ   +  +T++VTSRTLP+  E I  I +++K K  R 
Sbjct: 5   KVAVITGTNSNLGLNIAYRLIEQEDPTNRLTIVVTSRTLPRATEAINLIQKFAK-KCPRV 63

Query: 69  GQLEFDYLLVDFTDMVSVLSAYYDLNKKFKKIDYLFVNAAQGVYSGIDWVAATKEICRNP 128
           G +++DYLL+DFTDMVSVL AYY+L KK+K+I Y FVNAAQGVY GIDW+ A KE+C N 
Sbjct: 64  GIVDYDYLLIDFTDMVSVLGAYYELTKKYKEIHYFFVNAAQGVYGGIDWIGAVKEVCTNL 123

Query: 129 MEGVTNPTYKTQRVGVKSNDNMGLVFQANVFGPYYLIHKIKHLLQKG-GRIIWISSLMSN 187
           ++ VT P+YK QR+GVKS+D++GLVFQANVFGPYYLI KI   L  G   ++WISSLMS 
Sbjct: 124 IKSVTYPSYKIQRIGVKSDDDLGLVFQANVFGPYYLIQKILPQLTAGKASVVWISSLMSE 183

Query: 188 PKYLSFNDLQLLKSPESYEGSKRLVDLMHFGTFKQLQSEYGIEQYLVQPGIFTSFSFFKF 247
           PKY S ND+QLLKS  SYEGSKRLVDL+H  T+K +++ +GI QYLVQPGIF S SF  +
Sbjct: 184 PKYFSINDIQLLKSDASYEGSKRLVDLLHMATYKDMKN-HGIHQYLVQPGIFISNSFSIY 242

Query: 248 LNVFTYYSMLMLFYLARLFGSPSHNISGFIAANAPVTCA-LGN---ESQSVKVCSVSNRT 303
           LN+FTYY ML LFYLAR  GS  HN+ G+ AANAPV  A L N   E Q +K  S S R 
Sbjct: 243 LNIFTYYGMLALFYLARWLGSVWHNVDGYKAANAPVYAATLANPNFEEQYLKYGSASGRD 302

Query: 304 GKEYLSYQEVDTTGSADISAYLEKLCHEWDLTLKDQIVNTRQ 345
           G EY+  QEVD TG++D+  YL KL  EWD  LKDQI N+R+
Sbjct: 303 GMEYIQTQEVDPTGASDVQEYLSKLKLEWDEKLKDQITNSRE 344


>|KLLA0F19756p (infer) YLR100W ERG27 3-keto sterol reductase catalyzes the last of
           three steps required to remove two C-4 methyl groups
           from an intermediate in ergosterol biosynthesis mutants
           are sterol auxotrophs : highly similar to uniprot|Q12452
           Saccharomyces cerevisiae [Kluyveromyces lactis NRRL
           Y-1140]
          Length = 346

 Score =  417 bits (1071), Expect = e-116,   Method: Compositional matrix adjust.
 Identities = 207/345 (60%), Positives = 260/345 (75%), Gaps = 7/345 (2%)

Query: 7   NSKVALITGTSSNLGINIAYRLLEQLPSSTNVTLIVTSRTLPKVKEVITNINQYSKTKLN 66
           +SKVA++TGT+SNLG+NI YRL+E+     N+T++VTSRTLP+V+E I  I  +  T +N
Sbjct: 3   SSKVAVVTGTNSNLGLNIVYRLIERSEPEDNLTIVVTSRTLPRVRECIDLIKAFVNT-IN 61

Query: 67  RTGQLEFDYLLVDFTDMVSVLSAYYDLNKKFKKIDYLFVNAAQGVYSGIDWVAATKEICR 126
           RTG +++DYLLVDFT+M+S+L A+Y L+K++  I+Y FVNAAQGVYSGIDW+ A KE+  
Sbjct: 62  RTGSVDYDYLLVDFTNMISILDAHYSLSKRYDHINYFFVNAAQGVYSGIDWLGAVKEVFS 121

Query: 127 NPMEGVTNPTYKTQRVGVKSNDNMGLVFQANVFGPYYLIHKIKHLLQKG-GRIIWISSLM 185
           +P+E VTNPTYK QRVGVKS D MGLVFQANVFGPYYLI K+  LLQ G G ++W+SS+M
Sbjct: 122 SPLEAVTNPTYKIQRVGVKSKDGMGLVFQANVFGPYYLIQKLLPLLQAGQGTVVWVSSIM 181

Query: 186 SNPKYLSFNDLQLLKSPESYEGSKRLVDLMHFGTFKQLQSEYGIEQYLVQPGIFTSFSFF 245
           S PKYLS  D+QLL+S  SYEGSKRLVDL+H  T+K+++ + GI QYL  PGIFTS SFF
Sbjct: 182 SAPKYLSLQDIQLLESDVSYEGSKRLVDLLHSATYKEMK-KLGIRQYLTHPGIFTSLSFF 240

Query: 246 KFLNVFTYYSMLMLFYLARLFGSPSHNISGFIAANAPVTCA-LGN---ESQSVKVCSVSN 301
           ++LNVFTYY ML LFYLAR  GSP HNI G+ AANAPV  A + N   E + +K  S + 
Sbjct: 241 QYLNVFTYYGMLFLFYLARWIGSPWHNIQGYKAANAPVYVATMANPHFEKEQMKYGSATF 300

Query: 302 RTGKEYLSYQEVDTTGSADISAYLEKLCHEWDLTLKDQIVNTRQP 346
           R G EY+   EVDTTG  D+  Y+  L  +WD  LKDQI  TR P
Sbjct: 301 RDGLEYIKTDEVDTTGCEDVYKYISNLKLQWDEKLKDQIKPTRIP 345


>|CAGL0M11506p (infer) YLR100w ERG27 3-keto sterol reductase : highly similar to
           uniprot|Q12452 Saccharomyces cerevisiae [Candida
           glabrata CBS 138]
          Length = 348

 Score =  414 bits (1064), Expect = e-116,   Method: Compositional matrix adjust.
 Identities = 204/343 (59%), Positives = 263/343 (76%), Gaps = 7/343 (2%)

Query: 9   KVALITGTSSNLGINIAYRLLEQLPSSTNVTLIVTSRTLPKVKEVITNINQYSKTKLNRT 68
           KVA+ITG +SNLG+NIAYRL+E+  +   +TL+VTSRTLP+V+EV+  I ++  T+ +  
Sbjct: 7   KVAVITGANSNLGLNIAYRLIERQSADVRLTLVVTSRTLPRVREVVELIKKFVATQEDPC 66

Query: 69  GQLEFDYLLVDFTDMVSVLSAYYDLNKKFKKIDYLFVNAAQGVYSGIDWVAATKEICRNP 128
             ++FDYLLVDFT+MVSVL+AYYDLN+K++ I+Y FVNAAQGVY GIDW+ A K++  +P
Sbjct: 67  S-VDFDYLLVDFTNMVSVLNAYYDLNQKYESINYFFVNAAQGVYDGIDWIGAVKQVLSDP 125

Query: 129 MEGVTNPTYKTQRVGVKSNDNMGLVFQANVFGPYYLIHKIKHLLQKG-GRIIWISSLMSN 187
           +E VTNPTY+ Q VGVKS D MGLVFQANVFGPYYLI KI   L KG   ++WISS+M++
Sbjct: 126 LEAVTNPTYRKQLVGVKSKDEMGLVFQANVFGPYYLIQKILPQLSKGKATVVWISSIMAD 185

Query: 188 PKYLSFNDLQLLKSPESYEGSKRLVDLMHFGTFKQLQSEYGIEQYLVQPGIFTSFSFFKF 247
           PK+LS  D++++KS  +YEGSKR+VDL+H  T+KQ++S+ GI QY+VQPGIFTS+SF K+
Sbjct: 186 PKHLSLQDIEMIKSDVTYEGSKRVVDLLHLATYKQMKSQ-GIHQYVVQPGIFTSYSFAKY 244

Query: 248 LNVFTYYSMLMLFYLARLFGSPSHNISGFIAANAPVTCA-LGN---ESQSVKVCSVSNRT 303
           LN FT + ML LFYLARL GS  HNI G+ AANAPV  A L N   E Q VK  S S+R 
Sbjct: 245 LNFFTTFGMLFLFYLARLLGSKWHNIDGYKAANAPVYVATLINPHFEHQEVKYGSASSRD 304

Query: 304 GKEYLSYQEVDTTGSADISAYLEKLCHEWDLTLKDQIVNTRQP 346
           G EY+   ++D TGS+D+ AY+EK   EWD  LKDQI N+R P
Sbjct: 305 GMEYIETTDIDKTGSSDVLAYIEKKKLEWDDKLKDQITNSRIP 347


>|ERGO0G09878p Syntenic homolog of Saccharomyces cerevisiae YLR100W (ERG27)
           [Eremothecium gossypii]
          Length = 348

 Score =  396 bits (1018), Expect = e-110,   Method: Compositional matrix adjust.
 Identities = 192/332 (57%), Positives = 245/332 (73%), Gaps = 7/332 (2%)

Query: 18  SNLGINIAYRLLEQLPSSTNVTLIVTSRTLPKVKEVITNINQYSKTKLNRTGQLEFDYLL 77
           SNLG+NIAYRL+EQ    + + ++VTSRTLP+V+EV+  I  Y++ K  ++G ++FDYLL
Sbjct: 16  SNLGLNIAYRLIEQFTDDSKLVIVVTSRTLPRVREVVDLIKTYAE-KCGKSGAVDFDYLL 74

Query: 78  VDFTDMVSVLSAYYDLNKKFKKIDYLFVNAAQGVYSGIDWVAATKEICRNPMEGVTNPTY 137
           VDFTDMVSVL A Y+L K++  I Y + NAAQGVYSGIDW+ ATK + R+P++ VTNPTY
Sbjct: 75  VDFTDMVSVLGAAYELEKRYDAIHYFYANAAQGVYSGIDWLGATKAVLRDPLDAVTNPTY 134

Query: 138 KTQRVGVKSNDNMGLVFQANVFGPYYLIHKIKHLLQKG-GRIIWISSLMSNPKYLSFNDL 196
           K QRVGVKS D +GLVFQANVFGPYYLI +I  LL KG  +++W+SSLMS+ KYLS  D+
Sbjct: 135 KIQRVGVKSRDGLGLVFQANVFGPYYLIRRIIPLLAKGKAKVVWLSSLMSDVKYLSLEDV 194

Query: 197 QLLKSPESYEGSKRLVDLMHFGTFKQLQSEYGIEQYLVQPGIFTSFSFFKFLNVFTYYSM 256
           +LL++  SYEGSKRLVDL+H  T+K+L+S  GI QY+  PGIFTS SF+++LN FTYY M
Sbjct: 195 ELLRTDSSYEGSKRLVDLLHLATYKELKS-LGIHQYVTHPGIFTSHSFYQYLNFFTYYGM 253

Query: 257 LMLFYLARLFGSPSHNISGFIAANAPVTCA-LGN---ESQSVKVCSVSNRTGKEYLSYQE 312
           L LFYLAR  GSP HNI G+  ANAP+  A L N   E Q++K  S + R G EY++  E
Sbjct: 254 LFLFYLARWLGSPWHNIQGYKGANAPIYVATLANPTFEHQALKYGSATYRDGMEYIAKHE 313

Query: 313 VDTTGSADISAYLEKLCHEWDLTLKDQIVNTR 344
           +D TG  D   Y+  L  EWD+ LKDQI   R
Sbjct: 314 IDPTGMHDAYKYIRDLAEEWDIKLKDQITIGR 345


>|YALI0B17644p (infer) ORF YLR100W ERG27 3-keto sterol reductase singleton :
           similar to uniprot|Q12452 Saccharomyces cerevisiae
           [Yarrowia lipolytica CLIB122]
          Length = 343

 Score =  254 bits (649), Expect = 1e-67,   Method: Compositional matrix adjust.
 Identities = 131/340 (38%), Positives = 201/340 (59%), Gaps = 5/340 (1%)

Query: 5   NDNSKVALITGTSSNLGINIAYRLLEQLPSSTNVTLIVTSRTLPKVKEVITNINQYSKTK 64
           N  ++  +ITG SSNLGI I  RL+++     ++T++VTSRTL  V+  I  +  ++  K
Sbjct: 4   NRKTQTVVITGASSNLGIAIGKRLIDEKKEDAHLTIVVTSRTLRNVRVAIKTLKAHAVAK 63

Query: 65  LNRTGQLEFDYLLVDFTDMVSVLSAYYDLNKKFKKIDYLFVNAAQGVYSGIDWVAATKEI 124
                +++FDYLL D  DM S+  A  +L  +F +ID L  N+    Y GI+W  A    
Sbjct: 64  -EVGPEVDFDYLLFDLADMTSINGALVELKLRFSRIDTLIFNSNAANYIGINWPLAMWRF 122

Query: 125 CRNPMEGVTNPTYKTQRVGVKSNDNMGLVFQANVFGPYYLIHKIKHLLQKGGRIIWISSL 184
                  + NP+   Q VGVKS+D MG  +Q+NVFGP+Y++ ++   L+ GG++IWISS+
Sbjct: 123 TTQFKSEIENPSCMIQAVGVKSDDGMGSAYQSNVFGPWYMVLELTEQLKNGGKVIWISSI 182

Query: 185 MSNPKYLSFNDLQLLKSPESYEGSKRLVDLMHFGTFKQLQSEYGIEQYLVQPGIFTSFSF 244
            S+ KY+   D++L+ + E Y+GSKRL+D+ H     +L+ E+GI  YL  PGIFTS S 
Sbjct: 183 TSSEKYVDLEDIELIHNKEPYKGSKRLIDVAHNYYSPKLEEEHGIYSYLTDPGIFTSSSA 242

Query: 245 FKFLNVFTYYSMLMLFYLARLFGSPSHNISGFIAANAPVTCALGNESQSVK----VCSVS 300
            ++LN+F+ + M ++FY ARL G  + NI  +  AN PV   L  +  ++K    + S +
Sbjct: 243 SEYLNIFSAFGMYLMFYFARLIGLTTMNIDPYKGANVPVWVTLSEDPSALKREYRLGSRT 302

Query: 301 NRTGKEYLSYQEVDTTGSADISAYLEKLCHEWDLTLKDQI 340
            R G E +   ++   GS ++ AY++K   EW   LKDQI
Sbjct: 303 GRWGTEMMDATKLQYEGSEEVGAYIDKGVGEWREKLKDQI 342



BLASTP 2.2.18 [Mar-02-2008]


Reference: Altschul, Stephen F., Thomas L. Madden, Alejandro A. Schaffer, 
Jinghui Zhang, Zheng Zhang, Webb Miller, and David J. Lipman (1997), 
"Gapped BLAST and PSI-BLAST: a new generation of protein database search
programs",  Nucleic Acids Res. 25:3389-3402.

Reference for compositional score matrix adjustment: Altschul, Stephen F., 
John C. Wootton, E. Michael Gertz, Richa Agarwala, Aleksandr Morgulis,
Alejandro A. Schaffer, and Yi-Kuo Yu (2005) "Protein database searches
using compositionally adjusted substitution matrices", FEBS J. 272:5101-5109.