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Streptomyces avermitilis MA-4680 (save0)
Gene : BAC68002.1
DDBJ      :             putative oxidoreductase
Swiss-Prot:             

Homologs  Archaea  3/68 : Bacteria  190/915 : Eukaryota  3/199 : Viruses  0/175   --->[See Alignment]
b.43.4c.25.1
:449 amino acids
:SECSTR
:PSIPRED
:BLT:PDB   253->446 1tvcA PDBj 3e-09 26.6 %
:RPS:PDB   257->447 1amoA PDBj 2e-26 15.3 %
:RPS:SCOP  253->321 1qfjA1  b.43.4.2 * 2e-06 20.0 %
:RPS:SCOP  317->447 1ep1B2  c.25.1.3 * 6e-19 10.5 %
:HMM:SCOP  228->323 1qfjA1 b.43.4.2 * 7.5e-16 28.7 %
:HMM:SCOP  311->444 1i7pA2 c.25.1.1 * 4.1e-30 34.3 %
:RPS:PFM   262->319 PF08022 * FAD_binding_8 6e-07 43.1 %
:RPS:PFM   333->425 PF00175 * NAD_binding_1 2e-07 41.3 %
:HMM:PFM   63->184 PF01794 * Ferric_reduct 6.7e-16 30.0 120/125  
:HMM:PFM   333->426 PF00175 * NAD_binding_1 4.4e-12 29.8 94/109  
:HMM:PFM   233->321 PF00970 * FAD_binding_6 6.5e-09 25.0 88/99  
:BLT:SWISS 253->447 YEAX_ECOLI 2e-16 32.4 %
:PROS 42->56|PS00024|HEMOPEXIN
:TM
:SEG

SeqInfo AminoSeq See neighboring genes
Links GIB DAD Abbreviations Back to title page
GT:ID BAC68002.1 GT:GENE BAC68002.1 GT:PRODUCT putative oxidoreductase GT:DATABASE GIB00135CH01 GT:ORG save0 GB:ACCESSION GIB00135CH01 GB:LOCATION complement(343805..345154) GB:FROM 343805 GB:TO 345154 GB:DIRECTION - GB:PRODUCT putative oxidoreductase GB:NOTE PF00175: Oxidoreductase NAD-binding domain GB:PROTEIN_ID BAC68002.1 LENGTH 449 SQ:AASEQ MPVLIVIAIYAVRIARAPLDPRLKKRHVGPLSVTTGAVMLYLAWDWLRPEGLSAVYFVGEFAGVLSAYLMSCTLVLATRLMWLEQWFGGLDRMYRQHKRYAVWSILLLTPHLLLHFFSGFDGSQYGYAHRTASVGMGHLLGAVSAIGLLLLVLISLGQVGRILRLPYERWLFLHRLTGLLLLSALLHGWFLDLIINGSTPLLAIYVTMATVGMTAYAYDELVLRHREPRADYTIHRVERPTPDILDLTLTPTGKTALPVTGGQFVYLRVGGWHEHPFSVAGTQADGSVRLTIRALGRGTRGLYTDVSEGHPATLKGPYGMFDHTLGGPRQIWIAGGIGIAPFLGWLTHPGAEPAQTDLFYCAATAEDAPFLSELTAAAAHRPEFRLHPTFSRSHGRLTAERIQAEAGPITPDTHVFLCGPASMIENLTRGLHRQGVPRQHLHAEHFAFR GT:EXON 1|1-449:0| BL:SWS:NREP 1 BL:SWS:REP 253->447|YEAX_ECOLI|2e-16|32.4|188/321| PROS 42->56|PS00024|HEMOPEXIN|PDOC00023| TM:NTM 6 TM:REGION 1->22| TM:REGION 27->49| TM:REGION 57->79| TM:REGION 100->122| TM:REGION 133->155| TM:REGION 173->195| SEG 5->17|iviaiyavriara| SEG 106->115|llltphlllh| SEG 139->156|llgavsaigllllvlisl| SEG 169->191|rwlflhrltgllllsallhgwfl| SEG 240->252|ptpdildltltpt| BL:PDB:NREP 1 BL:PDB:REP 253->446|1tvcA|3e-09|26.6|192/250| RP:PDB:NREP 1 RP:PDB:REP 257->447|1amoA|2e-26|15.3|189/601| RP:PFM:NREP 2 RP:PFM:REP 262->319|PF08022|6e-07|43.1|58/101|FAD_binding_8| RP:PFM:REP 333->425|PF00175|2e-07|41.3|92/107|NAD_binding_1| HM:PFM:NREP 3 HM:PFM:REP 63->184|PF01794|6.7e-16|30.0|120/125|Ferric_reduct| HM:PFM:REP 333->426|PF00175|4.4e-12|29.8|94/109|NAD_binding_1| HM:PFM:REP 233->321|PF00970|6.5e-09|25.0|88/99|FAD_binding_6| GO:PFM:NREP 2 GO:PFM GO:0016491|"GO:oxidoreductase activity"|PF00175|IPR001433| GO:PFM GO:0055114|"GO:oxidation reduction"|PF00175|IPR001433| RP:SCP:NREP 2 RP:SCP:REP 253->321|1qfjA1|2e-06|20.0|65/91|b.43.4.2| RP:SCP:REP 317->447|1ep1B2|6e-19|10.5|124/160|c.25.1.3| HM:SCP:REP 228->323|1qfjA1|7.5e-16|28.7|94/97|b.43.4.2|1/1|Riboflavin synthase domain-like| HM:SCP:REP 311->444|1i7pA2|4.1e-30|34.3|134/0|c.25.1.1|1/1|Ferredoxin reductase-like, C-terminal NADP-linked domain| OP:NHOMO 247 OP:NHOMOORG 196 OP:PATTERN -----------------------------1--------------1---------------------1- -1--1---------1----------2-------12112421111---------11-----1-1-22141---111--------------------------------------------------------------------------------------------1-----------------------------------------------------1---------------------------------------------------------111----1--1111111111--------------1------------11------------------------------1---------------------------11-----22222-------------1-----1--1-1---1--111111-----1-----1-1-------------1--------------------------------------11111-12-21----1112------31-1-11--11-31-2112-11--21-1---1----------312-------1---111----------------------------------------------22-4----------------------------------------1----111-1---11-11112--1111-211111-111----------------------1111111---11111111111--------------1-11-----1----------11111---13-1122-2--223331111-----------11111111-1-11------------------------------------------------------------------------- -----------------------------------------------------------1---1----------------------------------------------------------------------------------------------------------------------------1---------- ------------------------------------------------------------------------------------------------------------------------------------------------------------------------------- STR:NPRED 244 STR:RPRED 54.3 SQ:SECSTR ############################################################################################################################################################################################################GGGGGGEEHHHHHTTccHHHHHHHHTcTTTGGGTTcTHHHHHHHHHccTEEETccccHHHHHHHccccccEEEEccccTTTTEEEEEEEccEEEcTTHHHHHccccEEEEEEEcccccccccTTccEEEEEGGGGHHHHHHHHHHHHHHHTTcEEEEccTTTccTTHHHHHHHHHTTcccEEEEEETTHHHHHTHHHHHHHHHHccTccEEEEEEETTTHHHHHHHHHHHHHHHTTccHHHHHE# PSIPRED ccEEEEEHHHHHHHHHHcccHHHHHccccHHHHHHHHHHHHHHHHHHcccccHHHHHHHHHHHHHHHHHHHHHHHHHcccHHHHHHcccHHHHHHHHHHHHHHHHHHHHHHHHHHHHHHHHHcccccccccccccccccHHHHHHHHHHHHHHHHHHHHHHHHHccHHHHHHHHHHHHHHHHHHHHHHHHHHHHHHHHccHHHHHHHHHHHHHHHccHHHHHHcccccEEEEEEEEEEEccccEEEEEEEcccccccccccccEEEEEcccccEEEEEEcccccccEEEEEEEEcccHHHHHHHHcccccEEEEEcccccccccccccEEEEEEccHHHHHHHHHHHHHHHccccEEEEEEEccHHHcccHHHHHHHHHccccEEEEEEEccccccccHHHHHHHccccccccEEEEEccHHHHHHHHHHHHHccccHHHEEccccccc //