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Database: UniProt
Entry: S5DQN8_9ACTN
LinkDB: S5DQN8_9ACTN
Original site: S5DQN8_9ACTN 
ID   S5DQN8_9ACTN            Unreviewed;       719 AA.
AC   S5DQN8;
DT   16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT   16-OCT-2013, sequence version 1.
DT   27-MAR-2024, entry version 22.
DE   SubName: Full=MedDCM-OCT-S27-C38-cds7 {ECO:0000313|EMBL:AGQ18809.1};
DE   SubName: Full=MedDCM-OCT-S31-C40-cds7 {ECO:0000313|EMBL:AGQ19200.1};
OS   Candidatus Actinomarina minuta.
OC   Bacteria; Actinomycetota; Actinomycetes; Candidatus Actinomarinidae;
OC   Candidatus Actinomarinales; Candidatus Actinomarineae;
OC   Candidatus Actinomarinaceae; Actinomarina.
OX   NCBI_TaxID=1389454 {ECO:0000313|EMBL:AGQ19200.1};
RN   [1] {ECO:0000313|EMBL:AGQ19200.1}
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=23959135; DOI=10.1038/srep02471;
RA   Ghai R., Mizuno C.M., Picazo A., Camacho A., Rodriguez-Valera F.;
RT   "Metagenomics uncovers a new group of low GC and ultra-small marine
RT   Actinobacteria.";
RL   Sci. Rep. 3:2471-2471(2013).
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC       pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
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DR   EMBL; KC811113; AGQ18809.1; -; Genomic_DNA.
DR   EMBL; KC811125; AGQ19200.1; -; Genomic_DNA.
DR   AlphaFoldDB; S5DQN8; -.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-KW.
DR   GO; GO:0051536; F:iron-sulfur cluster binding; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR   Gene3D; 1.10.1060.10; Alpha-helical ferredoxin; 1.
DR   Gene3D; 1.20.950.20; Transmembrane di-heme cytochromes, Chain C; 1.
DR   InterPro; IPR017896; 4Fe4S_Fe-S-bd.
DR   InterPro; IPR017900; 4Fe4S_Fe_S_CS.
DR   InterPro; IPR004017; Cys_rich_dom.
DR   InterPro; IPR009051; Helical_ferredxn.
DR   InterPro; IPR023234; NarG-like_domain.
DR   InterPro; IPR036197; NarG-like_sf.
DR   PANTHER; PTHR43255:SF6; IRON-SULFUR-BINDING OXIDOREDUCTASE FADF-RELATED; 1.
DR   PANTHER; PTHR43255; IRON-SULFUR-BINDING OXIDOREDUCTASE FADF-RELATED-RELATED; 1.
DR   Pfam; PF02754; CCG; 2.
DR   Pfam; PF13237; Fer4_10; 1.
DR   Pfam; PF02665; Nitrate_red_gam; 1.
DR   SUPFAM; SSF46548; alpha-helical ferredoxin; 1.
DR   SUPFAM; SSF103501; Respiratory nitrate reductase 1 gamma chain; 1.
DR   PROSITE; PS00198; 4FE4S_FER_1; 1.
DR   PROSITE; PS51379; 4FE4S_FER_2; 2.
PE   4: Predicted;
KW   Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW   Iron {ECO:0000256|ARBA:ARBA00023004};
KW   Iron-sulfur {ECO:0000256|ARBA:ARBA00023014};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        12..34
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        54..73
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        120..141
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        153..176
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        196..218
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        245..265
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          317..346
FT                   /note="4Fe-4S ferredoxin-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51379"
FT   DOMAIN          385..415
FT                   /note="4Fe-4S ferredoxin-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51379"
SQ   SEQUENCE   719 AA;  80606 MW;  AF1B23D860D24D13 CRC64;
     MNKQKPTRQV NDYVLLFSAG AALSVVFLWI ASYIFPEGEI IGGRRVFENI PKSIQYIFYI
     LSAASVFICG YLFSLRAKNW SRGTEEKRKV KLSKRILSFF DGILMRTTLR FKAAGVMHSM
     IYLGFLGLFA GTITLEIHHL MPPSLKFLQG TTYIVYSFSL ELASLLYLGG LGWAFYRRIF
     GTEDRIKTKT KMDDYLTLSL LAFMGISGLT TEAGRILVEG FPNYEKWSFV GYYIATLLPF
     DDGILFHRVS WILHTVSFFV FLLVLPQSKL RHIVTSPSNM FLSPKDRPKG AMRDIGNLME
     AEDIETVGAE LIENFTWKQL LDLDACTVCG RCTSVCPANL TGKPLDPREI ILKVGQVMSE
     SGDPAVPATV STPIDLKVKS SSVFDRITPE ELWACTSCKA CDEICPVNIE ILDKILDMRR
     YLALMASDFP SELGKAYVAM ENSSNPWGAS QEDRMKWSED LEFDVPLLDE TNKEEVEYLY
     WIGCAGAFDD RNVPVTKAVA TLLKRANVSY AVLGTKEVCT GDSARRTGNE FVFQQLAIQN
     IETMNNLDVK KVITQCPHCF NTISNEYPQL GGNFEVIHHS QLLTELVQSG KIEVGTSEEP
     HVITYHDSCY LGRHNDIYTA PREIVGSIGG IEIREMKRQG TNSFCCGAGG GRMWMEEATG
     KKVNIERVEE AIETGANEVA VACPFCYIMM DDGMKELGQG DNVRVRDVSL ILLDNLRKD
//
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