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Database: UniProt
Entry: Q3AS08_CHLCH
LinkDB: Q3AS08_CHLCH
Original site: Q3AS08_CHLCH 
ID   Q3AS08_CHLCH            Unreviewed;       927 AA.
AC   Q3AS08;
DT   22-NOV-2005, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2005, sequence version 1.
DT   27-MAR-2024, entry version 113.
DE   SubName: Full=Twin-arginine translocation pathway signal {ECO:0000313|EMBL:ABB28217.1};
DE            EC=1.2.1.2 {ECO:0000313|EMBL:ABB28217.1};
DE            EC=1.7.2.3 {ECO:0000313|EMBL:ABB28217.1};
GN   OrderedLocusNames=Cag_0954 {ECO:0000313|EMBL:ABB28217.1};
OS   Chlorobium chlorochromatii (strain CaD3).
OC   Bacteria; Chlorobiota; Chlorobiia; Chlorobiales; Chlorobiaceae;
OC   Chlorobium/Pelodictyon group; Chlorobium.
OX   NCBI_TaxID=340177 {ECO:0000313|EMBL:ABB28217.1};
RN   [1] {ECO:0000313|EMBL:ABB28217.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CaD3 {ECO:0000313|EMBL:ABB28217.1};
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA   Hammon N., Israni S., Pitluck S., Bryant D., Schmutz J., Larimer F.,
RA   Land M., Kyrpides N., Ivanova N., Richardson P.;
RT   "Complete sequence of Chlorobium chlorochromatii CaD3.";
RL   Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC         Evidence={ECO:0000256|ARBA:ARBA00001966};
CC   -!- SIMILARITY: Belongs to the prokaryotic molybdopterin-containing
CC       oxidoreductase family. {ECO:0000256|ARBA:ARBA00010312}.
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DR   EMBL; CP000108; ABB28217.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q3AS08; -.
DR   STRING; 340177.Cag_0954; -.
DR   KEGG; cch:Cag_0954; -.
DR   eggNOG; COG0243; Bacteria.
DR   HOGENOM; CLU_000422_13_3_10; -.
DR   OrthoDB; 9792592at2; -.
DR   GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0043546; F:molybdopterin cofactor binding; IEA:InterPro.
DR   GO; GO:0050626; F:trimethylamine-N-oxide reductase (cytochrome c) activity; IEA:UniProtKB-EC.
DR   GO; GO:0009033; F:trimethylamine-N-oxide reductase activity; IEA:UniProtKB-EC.
DR   CDD; cd02778; MopB_CT_Thiosulfate-R-like; 1.
DR   CDD; cd02755; MopB_Thiosulfate-R-like; 1.
DR   Gene3D; 2.40.40.20; -; 1.
DR   Gene3D; 3.30.200.210; -; 1.
DR   Gene3D; 3.40.50.740; -; 1.
DR   Gene3D; 3.40.228.10; Dimethylsulfoxide Reductase, domain 2; 1.
DR   InterPro; IPR009010; Asp_de-COase-like_dom_sf.
DR   InterPro; IPR006657; MoPterin_dinucl-bd_dom.
DR   InterPro; IPR006656; Mopterin_OxRdtase.
DR   InterPro; IPR006963; Mopterin_OxRdtase_4Fe-4S_dom.
DR   InterPro; IPR027467; MopterinOxRdtase_cofactor_BS.
DR   InterPro; IPR006311; TAT_signal.
DR   PANTHER; PTHR43742:SF9; TETRATHIONATE REDUCTASE SUBUNIT A; 1.
DR   PANTHER; PTHR43742; TRIMETHYLAMINE-N-OXIDE REDUCTASE; 1.
DR   Pfam; PF04879; Molybdop_Fe4S4; 1.
DR   Pfam; PF00384; Molybdopterin; 1.
DR   Pfam; PF01568; Molydop_binding; 1.
DR   SMART; SM00926; Molybdop_Fe4S4; 1.
DR   SUPFAM; SSF50692; ADC-like; 1.
DR   SUPFAM; SSF53706; Formate dehydrogenase/DMSO reductase, domains 1-3; 1.
DR   PROSITE; PS51669; 4FE4S_MOW_BIS_MGD; 1.
DR   PROSITE; PS00551; MOLYBDOPTERIN_PROK_1; 1.
DR   PROSITE; PS51318; TAT; 1.
PE   3: Inferred from homology;
KW   Iron {ECO:0000256|ARBA:ARBA00023004};
KW   Iron-sulfur {ECO:0000256|ARBA:ARBA00023014};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW   ECO:0000313|EMBL:ABB28217.1}; Signal {ECO:0000256|ARBA:ARBA00022729}.
FT   DOMAIN          49..109
FT                   /note="4Fe-4S Mo/W bis-MGD-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51669"
SQ   SEQUENCE   927 AA;  101337 MW;  2A3AD2910E190920 CRC64;
     MSKKITRRDF LKVASLLGGA TLLRPLWGSN SAVPQGGANA VASQVAHANT WVPSICNFCS
     SFCNIMVATE ESEGVKRIVK IEGNANSPLN RGKICARGQA GLRQTYDPDR LKQPLIRVQG
     SKRGEWRFRA ATWDEAYNYI AAKLMKVNPW EIAMVGGWTA CVSYMHFSLP FTRTLQIPNI
     IASPLQHCVT AGHLGTDLVT GNFNVHDEIL ADFEHARYIL FSMNNASVAA ISTARAVRFG
     EAKKNGAKVV CLDPRMSELA SKADEWIPIK PGTDHAFFLA FLHLLLREKL YDETFVQKHT
     NAPFLAWKDE QGLVHLAGES SNGKPSSYTL FDLNSQRVVT VAGHTNSNER SSGGARLLPA
     LHAPEGTVWN GHSVKTVFDF FIEESATFTP EWAAAITDVP ATTIRRIARE FGQARPALVD
     PGWMGARYHH VIGQRRLQAI IQTLVGGIDV PGGWLMSGEY HHKAEKMAHG SHSGDVPPVE
     KPGMGFAFGL LDIFGNPAAW EHGKPAVSFA WAMEQQKQGK PSVFIPAMAD VGLLESVKGE
     LQFNGEPYMT KAFIMNAANP IRHYFPASRW KEMLSHENVE LVVAIDVLPS DTTLYADVIL
     PNHTYLERNE PLLYPLGPST DLGYTTRLRS IKPLYNSRDT ADILCEIARR MGKLEPFLDG
     VAEYAGLDKA MLQSEINTAT QAGTPLNDAF LKTAYAAMST FAEQVNGTPI SAQEVEATIR
     TKGMLLLKSA DAVLEESAMP GKLALPTMSG RLELFSPILA SFAQAAGMQP IFNPVLGYVP
     RMMQQSGDKT TLSSNEFYFT YGKTPLVSHA STNTNNTLLV SITAQKEGAL RGLWMNSRKA
     TALGLENGQT VKVKNLRYGA SVTATLFTTE MIRPDTVFLP SSHGSSNKLL RVAAGKGTPL
     NELMPYSIEP IAASFMSQEF TVSVQAV
//
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