CAGL0M11506p_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= CAGL0M11506p (infer) YLR100w ERG27 3-keto sterol reductase :
highly similar to uniprot|Q12452 Saccharomyces cerevisiae [Candida
glabrata CBS 138]
(348 letters)
Database: Genolevures3.aa
48,939 sequences; 23,992,848 total letters
Searching..................................................done
Score E
Sequences producing significant alignments: (bits) Value
|CAGL0M11506p (infer) YLR100w ERG27 3-keto sterol reductase : hig... 718 0.0
|SACE0L03674p 3-keto sterol reductase, catalyzes the last of thre... 543 e-154
|SAKL0H16368p (infer) YLR100W ERG27 3-keto sterol reductase catal... 532 e-151
|KLTH0G13046p (infer) YLR100W ERG273-keto sterol reductase cataly... 526 e-149
|KLLA0F19756p (infer) YLR100W ERG27 3-keto sterol reductase catal... 514 e-146
|ZYRO0D06534p (infer) YLR100W ERG27 3-keto sterol reductase catal... 504 e-143
|ERGO0G09878p Syntenic homolog of Saccharomyces cerevisiae YLR100... 479 e-135
|DEHA2E20130p (infer) YLR100W ERG27 3-keto sterol reductase catal... 414 e-116
|YALI0B17644p (infer) ORF YLR100W ERG27 3-keto sterol reductase s... 269 4e-72
>|CAGL0M11506p (infer) YLR100w ERG27 3-keto sterol reductase : highly similar to
uniprot|Q12452 Saccharomyces cerevisiae [Candida
glabrata CBS 138]
Length = 348
Score = 718 bits (1854), Expect = 0.0, Method: Compositional matrix adjust.
Identities = 348/348 (100%), Positives = 348/348 (100%)
Query: 1 MTSKTRKVAVITGANSNLGLNIAYRLIERQSADVRLTLVVTSRTLPRVREVVELIKKFVA 60
MTSKTRKVAVITGANSNLGLNIAYRLIERQSADVRLTLVVTSRTLPRVREVVELIKKFVA
Sbjct: 1 MTSKTRKVAVITGANSNLGLNIAYRLIERQSADVRLTLVVTSRTLPRVREVVELIKKFVA 60
Query: 61 TQEDPCSVDFDYLLVDFTNMVSVLNAYYDLNQKYESINYFFVNAAQGVYDGIDWIGAVKQ 120
TQEDPCSVDFDYLLVDFTNMVSVLNAYYDLNQKYESINYFFVNAAQGVYDGIDWIGAVKQ
Sbjct: 61 TQEDPCSVDFDYLLVDFTNMVSVLNAYYDLNQKYESINYFFVNAAQGVYDGIDWIGAVKQ 120
Query: 121 VLSDPLEAVTNPTYRKQLVGVKSKDEMGLVFQANVFGPYYLIQKILPQLSKGKATVVWIS 180
VLSDPLEAVTNPTYRKQLVGVKSKDEMGLVFQANVFGPYYLIQKILPQLSKGKATVVWIS
Sbjct: 121 VLSDPLEAVTNPTYRKQLVGVKSKDEMGLVFQANVFGPYYLIQKILPQLSKGKATVVWIS 180
Query: 181 SIMADPKHLSLQDIEMIKSDVTYEGSKRVVDLLHLATYKQMKSQGIHQYVVQPGIFTSYS 240
SIMADPKHLSLQDIEMIKSDVTYEGSKRVVDLLHLATYKQMKSQGIHQYVVQPGIFTSYS
Sbjct: 181 SIMADPKHLSLQDIEMIKSDVTYEGSKRVVDLLHLATYKQMKSQGIHQYVVQPGIFTSYS 240
Query: 241 FAKYLNFFTTFGMLFLFYLARLLGSKWHNIDGYKAANAPVYVATLINPHFEHQEVKYGSA 300
FAKYLNFFTTFGMLFLFYLARLLGSKWHNIDGYKAANAPVYVATLINPHFEHQEVKYGSA
Sbjct: 241 FAKYLNFFTTFGMLFLFYLARLLGSKWHNIDGYKAANAPVYVATLINPHFEHQEVKYGSA 300
Query: 301 SSRDGMEYIETTDIDKTGSSDVLAYIEKKKLEWDDKLKDQITNSRIPI 348
SSRDGMEYIETTDIDKTGSSDVLAYIEKKKLEWDDKLKDQITNSRIPI
Sbjct: 301 SSRDGMEYIETTDIDKTGSSDVLAYIEKKKLEWDDKLKDQITNSRIPI 348
>|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 = 543 bits (1399), Expect = e-154, Method: Compositional matrix adjust.
Identities = 255/345 (73%), Positives = 302/345 (87%), Gaps = 2/345 (0%)
Query: 6 RKVAVITGANSNLGLNIAYRLIERQSADVRLTLVVTSRTLPRVREVVELIKKFV--ATQE 63
RKVA++TG NSNLGLNI +RLIE + +VRLT+VVTSRTLPRV+EV+ IK F + +
Sbjct: 3 RKVAIVTGTNSNLGLNIVFRLIETEDTNVRLTIVVTSRTLPRVQEVINQIKDFYNKSGRV 62
Query: 64 DPCSVDFDYLLVDFTNMVSVLNAYYDLNQKYESINYFFVNAAQGVYDGIDWIGAVKQVLS 123
+ +DFDYLLVDFTNMVSVLNAYYD+N+KY +INY FVNAAQG++DGIDWIGAVK+V +
Sbjct: 63 EDLEIDFDYLLVDFTNMVSVLNAYYDINKKYRAINYLFVNAAQGIFDGIDWIGAVKEVFT 122
Query: 124 DPLEAVTNPTYRKQLVGVKSKDEMGLVFQANVFGPYYLIQKILPQLSKGKATVVWISSIM 183
+PLEAVTNPTY+ QLVGVKSKD+MGL+FQANVFGPYY I KILPQL++GKA +VWISSIM
Sbjct: 123 NPLEAVTNPTYKIQLVGVKSKDDMGLIFQANVFGPYYFISKILPQLTRGKAYIVWISSIM 182
Query: 184 ADPKHLSLQDIEMIKSDVTYEGSKRVVDLLHLATYKQMKSQGIHQYVVQPGIFTSYSFAK 243
+DPK+LSL DIE++K++ +YEGSKR+VDLLHLATYK +K GI+QYVVQPGIFTS+SF++
Sbjct: 183 SDPKYLSLNDIELLKTNASYEGSKRLVDLLHLATYKDLKKLGINQYVVQPGIFTSHSFSE 242
Query: 244 YLNFFTTFGMLFLFYLARLLGSKWHNIDGYKAANAPVYVATLINPHFEHQEVKYGSASSR 303
YLNFFT FGML LFYLARLLGS WHNIDGYKAANAPVYV L NP+FE Q+VKYGSA+SR
Sbjct: 243 YLNFFTYFGMLCLFYLARLLGSPWHNIDGYKAANAPVYVTRLANPNFEKQDVKYGSATSR 302
Query: 304 DGMEYIETTDIDKTGSSDVLAYIEKKKLEWDDKLKDQITNSRIPI 348
DGM YI+T +ID TG SDV AYI+KKKLEWD+KLKDQI +R PI
Sbjct: 303 DGMPYIKTQEIDPTGMSDVFAYIQKKKLEWDEKLKDQIVETRTPI 347
>|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 = 532 bits (1370), Expect = e-151, Method: Compositional matrix adjust.
Identities = 248/343 (72%), Positives = 296/343 (86%)
Query: 6 RKVAVITGANSNLGLNIAYRLIERQSADVRLTLVVTSRTLPRVREVVELIKKFVATQEDP 65
RK+AVITG NSNLGLNIAYRLI++ + R+T+VVTSRTLPR REV++ I +V
Sbjct: 4 RKIAVITGTNSNLGLNIAYRLIKKLDPETRITIVVTSRTLPRAREVIDQINAYVERSGRT 63
Query: 66 CSVDFDYLLVDFTNMVSVLNAYYDLNQKYESINYFFVNAAQGVYDGIDWIGAVKQVLSDP 125
VDFDYLLVDFTNMVSVL+AYYDLN++Y+ INYFFVNAAQGVY+GIDW GA+K+V ++P
Sbjct: 64 GIVDFDYLLVDFTNMVSVLSAYYDLNKRYKEINYFFVNAAQGVYEGIDWFGAIKEVCANP 123
Query: 126 LEAVTNPTYRKQLVGVKSKDEMGLVFQANVFGPYYLIQKILPQLSKGKATVVWISSIMAD 185
LEAVTNPTY+ Q VGV SKD MGLVFQANVFGPYYLIQK++PQLS GKA +VWISSIM++
Sbjct: 124 LEAVTNPTYKIQRVGVTSKDGMGLVFQANVFGPYYLIQKLIPQLSAGKANIVWISSIMSN 183
Query: 186 PKHLSLQDIEMIKSDVTYEGSKRVVDLLHLATYKQMKSQGIHQYVVQPGIFTSYSFAKYL 245
PK+LSLQDIE++K++ +YEGSKR+VDLLHLATYK MK GIHQYV QPGIFTS+SF KYL
Sbjct: 184 PKYLSLQDIELLKTNASYEGSKRLVDLLHLATYKDMKLHGIHQYVTQPGIFTSHSFFKYL 243
Query: 246 NFFTTFGMLFLFYLARLLGSKWHNIDGYKAANAPVYVATLINPHFEHQEVKYGSASSRDG 305
NFFT +GML LFY AR +GS+WHNIDGYKAANAPVY ATL NP+FE Q++KYGSA+ RDG
Sbjct: 244 NFFTYYGMLLLFYFARWIGSEWHNIDGYKAANAPVYAATLANPNFEGQQLKYGSATYRDG 303
Query: 306 MEYIETTDIDKTGSSDVLAYIEKKKLEWDDKLKDQITNSRIPI 348
MEYI+T +ID TGS D+ A+I+ + EWD+KLKDQITN+RIP+
Sbjct: 304 MEYIKTQEIDPTGSHDIYAHIKHLEKEWDEKLKDQITNTRIPM 346
>|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 = 526 bits (1354), Expect = e-149, Method: Compositional matrix adjust.
Identities = 251/340 (73%), Positives = 286/340 (84%)
Query: 6 RKVAVITGANSNLGLNIAYRLIERQSADVRLTLVVTSRTLPRVREVVELIKKFVATQEDP 65
RKVAVITG NSNLGLN AYRLI+ DVRLT+VVTSRTLPR REV++ IK FV P
Sbjct: 5 RKVAVITGTNSNLGLNTAYRLIQELDQDVRLTIVVTSRTLPRAREVIDNIKDFVGKSSRP 64
Query: 66 CSVDFDYLLVDFTNMVSVLNAYYDLNQKYESINYFFVNAAQGVYDGIDWIGAVKQVLSDP 125
VD+DYLLVDFT+MVS LNAYY+LN+ Y+ INYFFVNAAQGVY GIDW+GAVK+V ++P
Sbjct: 65 GLVDYDYLLVDFTDMVSTLNAYYELNKHYKEINYFFVNAAQGVYSGIDWLGAVKEVFTNP 124
Query: 126 LEAVTNPTYRKQLVGVKSKDEMGLVFQANVFGPYYLIQKILPQLSKGKATVVWISSIMAD 185
+EAVTNPTY+ Q VGVKS+D MGLVFQANVFGPYYLIQKILPQL GKA VVWISSIM+D
Sbjct: 125 IEAVTNPTYKIQRVGVKSQDGMGLVFQANVFGPYYLIQKILPQLQAGKAVVVWISSIMSD 184
Query: 186 PKHLSLQDIEMIKSDVTYEGSKRVVDLLHLATYKQMKSQGIHQYVVQPGIFTSYSFAKYL 245
PK+LSL+DIE++KS +YEGSKR+VDLLHLATYK++K QGIHQYVVQPGIF S+SF KYL
Sbjct: 185 PKYLSLEDIELVKSPASYEGSKRLVDLLHLATYKELKGQGIHQYVVQPGIFISHSFFKYL 244
Query: 246 NFFTTFGMLFLFYLARLLGSKWHNIDGYKAANAPVYVATLINPHFEHQEVKYGSASSRDG 305
N + +GML LFY AR LGS WHNIDGY+AANAPVYVATL NP FE Q VKYGSA+ +DG
Sbjct: 245 NVLSYYGMLLLFYFARFLGSPWHNIDGYRAANAPVYVATLANPTFEQQNVKYGSATYKDG 304
Query: 306 MEYIETTDIDKTGSSDVLAYIEKKKLEWDDKLKDQITNSR 345
MEYI T +I+ TG DV Y++K K WDDKLKDQITNSR
Sbjct: 305 MEYIRTQEIEATGVHDVYVYLKKLKDVWDDKLKDQITNSR 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 = 514 bits (1323), Expect = e-146, Method: Compositional matrix adjust.
Identities = 241/344 (70%), Positives = 288/344 (83%)
Query: 5 TRKVAVITGANSNLGLNIAYRLIERQSADVRLTLVVTSRTLPRVREVVELIKKFVATQED 64
+ KVAV+TG NSNLGLNI YRLIER + LT+VVTSRTLPRVRE ++LIK FV T
Sbjct: 3 SSKVAVVTGTNSNLGLNIVYRLIERSEPEDNLTIVVTSRTLPRVRECIDLIKAFVNTINR 62
Query: 65 PCSVDFDYLLVDFTNMVSVLNAYYDLNQKYESINYFFVNAAQGVYDGIDWIGAVKQVLSD 124
SVD+DYLLVDFTNM+S+L+A+Y L+++Y+ INYFFVNAAQGVY GIDW+GAVK+V S
Sbjct: 63 TGSVDYDYLLVDFTNMISILDAHYSLSKRYDHINYFFVNAAQGVYSGIDWLGAVKEVFSS 122
Query: 125 PLEAVTNPTYRKQLVGVKSKDEMGLVFQANVFGPYYLIQKILPQLSKGKATVVWISSIMA 184
PLEAVTNPTY+ Q VGVKSKD MGLVFQANVFGPYYLIQK+LP L G+ TVVW+SSIM+
Sbjct: 123 PLEAVTNPTYKIQRVGVKSKDGMGLVFQANVFGPYYLIQKLLPLLQAGQGTVVWVSSIMS 182
Query: 185 DPKHLSLQDIEMIKSDVTYEGSKRVVDLLHLATYKQMKSQGIHQYVVQPGIFTSYSFAKY 244
PK+LSLQDI++++SDV+YEGSKR+VDLLH ATYK+MK GI QY+ PGIFTS SF +Y
Sbjct: 183 APKYLSLQDIQLLESDVSYEGSKRLVDLLHSATYKEMKKLGIRQYLTHPGIFTSLSFFQY 242
Query: 245 LNFFTTFGMLFLFYLARLLGSKWHNIDGYKAANAPVYVATLINPHFEHQEVKYGSASSRD 304
LN FT +GMLFLFYLAR +GS WHNI GYKAANAPVYVAT+ NPHFE +++KYGSA+ RD
Sbjct: 243 LNVFTYYGMLFLFYLARWIGSPWHNIQGYKAANAPVYVATMANPHFEKEQMKYGSATFRD 302
Query: 305 GMEYIETTDIDKTGSSDVLAYIEKKKLEWDDKLKDQITNSRIPI 348
G+EYI+T ++D TG DV YI KL+WD+KLKDQI +RIP+
Sbjct: 303 GLEYIKTDEVDTTGCEDVYKYISNLKLQWDEKLKDQIKPTRIPL 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 = 504 bits (1299), Expect = e-143, Method: Compositional matrix adjust.
Identities = 238/340 (70%), Positives = 287/340 (84%)
Query: 6 RKVAVITGANSNLGLNIAYRLIERQSADVRLTLVVTSRTLPRVREVVELIKKFVATQEDP 65
RKVAVITG NSNLGLNIAYRLIE++ RLT+VVTSRTLPR E + LI+KF
Sbjct: 4 RKVAVITGTNSNLGLNIAYRLIEQEDPTNRLTIVVTSRTLPRATEAINLIQKFAKKCPRV 63
Query: 66 CSVDFDYLLVDFTNMVSVLNAYYDLNQKYESINYFFVNAAQGVYDGIDWIGAVKQVLSDP 125
VD+DYLL+DFT+MVSVL AYY+L +KY+ I+YFFVNAAQGVY GIDWIGAVK+V ++
Sbjct: 64 GIVDYDYLLIDFTDMVSVLGAYYELTKKYKEIHYFFVNAAQGVYGGIDWIGAVKEVCTNL 123
Query: 126 LEAVTNPTYRKQLVGVKSKDEMGLVFQANVFGPYYLIQKILPQLSKGKATVVWISSIMAD 185
+++VT P+Y+ Q +GVKS D++GLVFQANVFGPYYLIQKILPQL+ GKA+VVWISS+M++
Sbjct: 124 IKSVTYPSYKIQRIGVKSDDDLGLVFQANVFGPYYLIQKILPQLTAGKASVVWISSLMSE 183
Query: 186 PKHLSLQDIEMIKSDVTYEGSKRVVDLLHLATYKQMKSQGIHQYVVQPGIFTSYSFAKYL 245
PK+ S+ DI+++KSD +YEGSKR+VDLLH+ATYK MK+ GIHQY+VQPGIF S SF+ YL
Sbjct: 184 PKYFSINDIQLLKSDASYEGSKRLVDLLHMATYKDMKNHGIHQYLVQPGIFISNSFSIYL 243
Query: 246 NFFTTFGMLFLFYLARLLGSKWHNIDGYKAANAPVYVATLINPHFEHQEVKYGSASSRDG 305
N FT +GML LFYLAR LGS WHN+DGYKAANAPVY ATL NP+FE Q +KYGSAS RDG
Sbjct: 244 NIFTYYGMLALFYLARWLGSVWHNVDGYKAANAPVYAATLANPNFEEQYLKYGSASGRDG 303
Query: 306 MEYIETTDIDKTGSSDVLAYIEKKKLEWDDKLKDQITNSR 345
MEYI+T ++D TG+SDV Y+ K KLEWD+KLKDQITNSR
Sbjct: 304 MEYIQTQEVDPTGASDVQEYLSKLKLEWDEKLKDQITNSR 343
>|ERGO0G09878p Syntenic homolog of Saccharomyces cerevisiae YLR100W (ERG27)
[Eremothecium gossypii]
Length = 348
Score = 479 bits (1233), Expect = e-135, Method: Compositional matrix adjust.
Identities = 227/330 (68%), Positives = 272/330 (82%)
Query: 16 SNLGLNIAYRLIERQSADVRLTLVVTSRTLPRVREVVELIKKFVATQEDPCSVDFDYLLV 75
SNLGLNIAYRLIE+ + D +L +VVTSRTLPRVREVV+LIK + +VDFDYLLV
Sbjct: 16 SNLGLNIAYRLIEQFTDDSKLVIVVTSRTLPRVREVVDLIKTYAEKCGKSGAVDFDYLLV 75
Query: 76 DFTNMVSVLNAYYDLNQKYESINYFFVNAAQGVYDGIDWIGAVKQVLSDPLEAVTNPTYR 135
DFT+MVSVL A Y+L ++Y++I+YF+ NAAQGVY GIDW+GA K VL DPL+AVTNPTY+
Sbjct: 76 DFTDMVSVLGAAYELEKRYDAIHYFYANAAQGVYSGIDWLGATKAVLRDPLDAVTNPTYK 135
Query: 136 KQLVGVKSKDEMGLVFQANVFGPYYLIQKILPQLSKGKATVVWISSIMADPKHLSLQDIE 195
Q VGVKS+D +GLVFQANVFGPYYLI++I+P L+KGKA VVW+SS+M+D K+LSL+D+E
Sbjct: 136 IQRVGVKSRDGLGLVFQANVFGPYYLIRRIIPLLAKGKAKVVWLSSLMSDVKYLSLEDVE 195
Query: 196 MIKSDVTYEGSKRVVDLLHLATYKQMKSQGIHQYVVQPGIFTSYSFAKYLNFFTTFGMLF 255
++++D +YEGSKR+VDLLHLATYK++KS GIHQYV PGIFTS+SF +YLNFFT +GMLF
Sbjct: 196 LLRTDSSYEGSKRLVDLLHLATYKELKSLGIHQYVTHPGIFTSHSFYQYLNFFTYYGMLF 255
Query: 256 LFYLARLLGSKWHNIDGYKAANAPVYVATLINPHFEHQEVKYGSASSRDGMEYIETTDID 315
LFYLAR LGS WHNI GYK ANAP+YVATL NP FEHQ +KYGSA+ RDGMEYI +ID
Sbjct: 256 LFYLARWLGSPWHNIQGYKGANAPIYVATLANPTFEHQALKYGSATYRDGMEYIAKHEID 315
Query: 316 KTGSSDVLAYIEKKKLEWDDKLKDQITNSR 345
TG D YI EWD KLKDQIT R
Sbjct: 316 PTGMHDAYKYIRDLAEEWDIKLKDQITIGR 345
>|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 = 414 bits (1064), Expect = e-116, Method: Compositional matrix adjust.
Identities = 204/343 (59%), Positives = 263/343 (76%), Gaps = 7/343 (2%)
Query: 7 KVAVITGANSNLGLNIAYRLIERQSADVRLTLVVTSRTLPRVREVVELIKKFVATQEDPC 66
KVA+ITG +SNLG+NIAYRL+E+ + +TL+VTSRTLP+V+EV+ I ++ T+ +
Sbjct: 9 KVALITGTSSNLGINIAYRLLEQLPSSTNVTLIVTSRTLPKVKEVITNINQYSKTKLNRT 68
Query: 67 S-VDFDYLLVDFTNMVSVLNAYYDLNQKYESINYFFVNAAQGVYDGIDWIGAVKQVLSDP 125
++FDYLLVDFT+MVSVL+AYYDLN+K++ I+Y FVNAAQGVY GIDW+ A K++ +P
Sbjct: 69 GQLEFDYLLVDFTDMVSVLSAYYDLNKKFKKIDYLFVNAAQGVYSGIDWVAATKEICRNP 128
Query: 126 LEAVTNPTYRKQLVGVKSKDEMGLVFQANVFGPYYLIQKILPQLSKGKATVVWISSIMAD 185
+E VTNPTY+ Q VGVKS D MGLVFQANVFGPYYLI KI L KG ++WISS+M++
Sbjct: 129 MEGVTNPTYKTQRVGVKSNDNMGLVFQANVFGPYYLIHKIKHLLQKG-GRIIWISSLMSN 187
Query: 186 PKHLSLQDIEMIKSDVTYEGSKRVVDLLHLATYKQMKSQ-GIHQYVVQPGIFTSYSFAKY 244
PK+LS D++++KS +YEGSKR+VDL+H T+KQ++S+ GI QY+VQPGIFTS+SF K+
Sbjct: 188 PKYLSFNDLQLLKSPESYEGSKRLVDLMHFGTFKQLQSEYGIEQYLVQPGIFTSFSFFKF 247
Query: 245 LNFFTTFGMLFLFYLARLLGSKWHNIDGYKAANAPVYVATLINPHFEHQEVKYGSASSRD 304
LN FT + ML LFYLARL GS HNI G+ AANAPV A L N E Q VK S S+R
Sbjct: 248 LNVFTYYSMLMLFYLARLFGSPSHNISGFIAANAPVTCA-LGN---ESQSVKVCSVSNRT 303
Query: 305 GMEYIETTDIDKTGSSDVLAYIEKKKLEWDDKLKDQITNSRIP 347
G EY+ ++D TGS+D+ AY+EK EWD LKDQI N+R P
Sbjct: 304 GKEYLSYQEVDTTGSADISAYLEKLCHEWDLTLKDQIVNTRQP 346
>|YALI0B17644p (infer) ORF YLR100W ERG27 3-keto sterol reductase singleton :
similar to uniprot|Q12452 Saccharomyces cerevisiae
[Yarrowia lipolytica CLIB122]
Length = 343
Score = 269 bits (687), Expect = 4e-72, Method: Compositional matrix adjust.
Identities = 146/339 (43%), Positives = 207/339 (61%), Gaps = 3/339 (0%)
Query: 4 KTRKVAVITGANSNLGLNIAYRLIERQSADVRLTLVVTSRTLPRVREVVELIKKFVATQE 63
KT+ V VITGA+SNLG+ I RLI+ + D LT+VVTSRTL VR ++ +K +E
Sbjct: 6 KTQTV-VITGASSNLGIAIGKRLIDEKKEDAHLTIVVTSRTLRNVRVAIKTLKAHAVAKE 64
Query: 64 DPCSVDFDYLLVDFTNMVSVLNAYYDLNQKYESINYFFVNAAQGVYDGIDWIGAVKQVLS 123
VDFDYLL D +M S+ A +L ++ I+ N+ Y GI+W A+ + +
Sbjct: 65 VGPEVDFDYLLFDLADMTSINGALVELKLRFSRIDTLIFNSNAANYIGINWPLAMWRFTT 124
Query: 124 DPLEAVTNPTYRKQLVGVKSKDEMGLVFQANVFGPYYLIQKILPQLSKGKATVVWISSIM 183
+ NP+ Q VGVKS D MG +Q+NVFGP+Y++ ++ QL G V+WISSI
Sbjct: 125 QFKSEIENPSCMIQAVGVKSDDGMGSAYQSNVFGPWYMVLELTEQLKNG-GKVIWISSIT 183
Query: 184 ADPKHLSLQDIEMIKSDVTYEGSKRVVDLLH-LATYKQMKSQGIHQYVVQPGIFTSYSFA 242
+ K++ L+DIE+I + Y+GSKR++D+ H + K + GI+ Y+ PGIFTS S +
Sbjct: 184 SSEKYVDLEDIELIHNKEPYKGSKRLIDVAHNYYSPKLEEEHGIYSYLTDPGIFTSSSAS 243
Query: 243 KYLNFFTTFGMLFLFYLARLLGSKWHNIDGYKAANAPVYVATLINPHFEHQEVKYGSASS 302
+YLN F+ FGM +FY ARL+G NID YK AN PV+V +P +E + GS +
Sbjct: 244 EYLNIFSAFGMYLMFYFARLIGLTTMNIDPYKGANVPVWVTLSEDPSALKREYRLGSRTG 303
Query: 303 RDGMEYIETTDIDKTGSSDVLAYIEKKKLEWDDKLKDQI 341
R G E ++ T + GS +V AYI+K EW +KLKDQI
Sbjct: 304 RWGTEMMDATKLQYEGSEEVGAYIDKGVGEWREKLKDQI 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.