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Clostridium perfringens str. 13 (cper0)
Gene : asrB.1
DDBJ      :asrB         anaerobic sulfite reductase subunit B
Swiss-Prot:             

Homologs  Archaea  35/68 : Bacteria  230/915 : Eukaryota  87/199 : Viruses  0/175   --->[See Alignment]
b.43.4c.25.1
:263 amino acids
:SECSTR
:PSIPRED
:BLT:PDB   9->253 1ep1B PDBj 9e-15 29.7 %
:RPS:PDB   11->221 1amoA PDBj 6e-28 14.4 %
:RPS:SCOP  6->94 1qfjA1  b.43.4.2 * 2e-12 22.1 %
:RPS:SCOP  89->257 1ep1B2  c.25.1.3 * 2e-21 21.3 %
:HMM:SCOP  4->94 1ep3B1 b.43.4.2 * 1.3e-17 27.5 %
:HMM:SCOP  89->260 1ep3B2 c.25.1.3 * 1.7e-32 35.3 %
:RPS:PFM   10->92 PF00970 * FAD_binding_6 4e-05 34.9 %
:RPS:PFM   106->205 PF00175 * NAD_binding_1 1e-09 31.6 %
:RPS:PFM   226->254 PF10418 * DHODB_Fe-S_bind 4e-06 58.6 %
:HMM:PFM   107->207 PF00175 * NAD_binding_1 1.1e-19 29.0 100/109  
:HMM:PFM   226->257 PF10418 * DHODB_Fe-S_bind 9.7e-15 43.8 32/40  
:HMM:PFM   32->92 PF00970 * FAD_binding_6 3.3e-07 31.7 60/99  
:BLT:SWISS 7->263 ASRB_SALTY 1e-68 43.6 %

SeqInfo AminoSeq See neighboring genes
Links GIB DAD Abbreviations Back to title page
GT:ID BAB81145.1 GT:GENE asrB.1 GT:PRODUCT anaerobic sulfite reductase subunit B GT:DATABASE GIB00075CH01 GT:ORG cper0 GB:ACCESSION GIB00075CH01 GB:LOCATION complement(1697171..1697962) GB:FROM 1697171 GB:TO 1697962 GB:DIRECTION - GB:GENE asrB GB:PRODUCT anaerobic sulfite reductase subunit B GB:NOTE 263 aa, similar to sp:ASRB_SALTY ANAEROBIC SULFITE REDUCTASE SUBUNIT B (EC 1.8.2.-) from Salmonella typhimurium (272 aa); 43.9% identity in 253 aa overlap. 1 putative transmembrane region was found by PSORT CPE1439 GB:PROTEIN_ID BAB81145.1 LENGTH 263 SQ:AASEQ MHNEYTPFISKILNVKKHTDIEYTFRMEFKGDVKPGQFFEVSLPKFGEAPISVSGIGEDYVELTIRRVGVVTNEIFEKYEGDKLFLRGPYGNGFDVNNYKGKEVIVVAGGTGLSPVKGIVDYFSQNPKDAESFTLISGFKGPKDILFKDDMKEWEKNMNMIITVDSAEEGYEGNTGLVTKYIPELEIKDMDNVQVIVVGPPMMMKFTVLEFLKRGIKEENIWISQERKMCCGLGKCGHCKIDDTYICLDGPVFNYTKGKLLID GT:EXON 1|1-263:0| BL:SWS:NREP 1 BL:SWS:REP 7->263|ASRB_SALTY|1e-68|43.6|257/272| BL:PDB:NREP 1 BL:PDB:REP 9->253|1ep1B|9e-15|29.7|232/261| RP:PDB:NREP 1 RP:PDB:REP 11->221|1amoA|6e-28|14.4|209/601| RP:PFM:NREP 3 RP:PFM:REP 10->92|PF00970|4e-05|34.9|83/99|FAD_binding_6| RP:PFM:REP 106->205|PF00175|1e-09|31.6|95/107|NAD_binding_1| RP:PFM:REP 226->254|PF10418|4e-06|58.6|29/38|DHODB_Fe-S_bind| HM:PFM:NREP 3 HM:PFM:REP 107->207|PF00175|1.1e-19|29.0|100/109|NAD_binding_1| HM:PFM:REP 226->257|PF10418|9.7e-15|43.8|32/40|DHODB_Fe-S_bind| HM:PFM:REP 32->92|PF00970|3.3e-07|31.7|60/99|FAD_binding_6| GO:PFM:NREP 4 GO:PFM GO:0016491|"GO:oxidoreductase activity"|PF00970|IPR008333| GO:PFM GO:0055114|"GO:oxidation reduction"|PF00970|IPR008333| 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 6->94|1qfjA1|2e-12|22.1|86/91|b.43.4.2| RP:SCP:REP 89->257|1ep1B2|2e-21|21.3|150/160|c.25.1.3| HM:SCP:REP 4->94|1ep3B1|1.3e-17|27.5|91/0|b.43.4.2|1/1|Riboflavin synthase domain-like| HM:SCP:REP 89->260|1ep3B2|1.7e-32|35.3|153/0|c.25.1.3|1/1|Ferredoxin reductase-like, C-terminal NADP-linked domain| OP:NHOMO 539 OP:NHOMOORG 352 OP:PATTERN -----------------------1-----1--11111111111-211222111-33212331221-11 -1----------------------11-------111-11-1-1----------------------------1--------22--1221111-31-1-----------------------------22232111222-----222-1---1-----------------1--------------------111--1--------------1--1111-------1--111111---------------------------------------------111-------211------------------------1---------21-2544444447462222344313112-1111--4211-2122211111-2-1--------1-1-----2-111----------2--------------11---1-----------------------------------------------------------------------1111--------1111111-111111----21-1-23-1-----2----11-2111----------1---2-1212212121111-2322224-2-----111-------------------------221--11--1--1-------1--------------1-12---------------------------1------------------1----1111111111111111-------------------------------1111-1----------------------------1------------------2-------------------------------------1-1111------------211------------------1------322-11211-2-- -----1--21-----12222--111---1-1-11-11111111---22111222--1112212-2221-3-113311111111111-1-1--2152----111211-----1---1--------------------1-----------------------------------------18-----1-13221-133321 ------------------------------------------------------------------------------------------------------------------------------------------------------------------------------- STR:NPRED 252 STR:RPRED 95.8 SQ:SECSTR #TccEEEEEEHHHHTTTTTccHHHHHHHcTTccccHHHHHHHccccccEEEEcTTTcTTEEEEEEEccEEEcTTccEEEcccEEEEEEEccccccccccTTccEEEEEEGGGGHHHHHHHHHHHHHHHTTcEEEEEEEccTTTccTTHHHHHHHHHEEEEEETTcccccccHHHHHHHTHHHHHHHHHHcTccEEEEEEETTTHHHHHHHHHHHHHHHTTcHHHHHHHHHHccccccTTccTTccTTTTccEE########## PSIPRED ccccccEEEEEEEEEEEccccEEEEEEEcccccccccEEEEEEccccEEEEEEccccccEEEEEEEEcccHHHHHHHcccccEEEEEccccccEEcccccccEEEEEEccHHHHHHHHHHHHHHHccccccEEEEEEEEccHHHHccHHHHHHHHHcccEEEEEcccccccccccccHHHHHHHHccccccccEEEEEccHHHHHHHHHHHHHccccHHHEEEEccccccccccEEcEEEEccEEEcccccEEEHHHHHHHcc //