ID A0A1F8S3B5_9CHLR Unreviewed; 888 AA.
AC A0A1F8S3B5;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:OGO54358.1};
GN ORFNames=A2V85_14305 {ECO:0000313|EMBL:OGO54358.1};
OS Chloroflexi bacterium RBG_16_72_14.
OC Bacteria; Chloroflexota.
OX NCBI_TaxID=1797663 {ECO:0000313|EMBL:OGO54358.1, ECO:0000313|Proteomes:UP000176218};
RN [1] {ECO:0000313|EMBL:OGO54358.1, ECO:0000313|Proteomes:UP000176218}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=27774985; DOI=10.1038/ncomms13219;
RA Anantharaman K., Brown C.T., Hug L.A., Sharon I., Castelle C.J.,
RA Probst A.J., Thomas B.C., Singh A., Wilkins M.J., Karaoz U., Brodie E.L.,
RA Williams K.H., Hubbard S.S., Banfield J.F.;
RT "Thousands of microbial genomes shed light on interconnected biogeochemical
RT processes in an aquifer system.";
RL Nat. Commun. 7:13219-13219(2016).
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:OGO54358.1}.
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DR EMBL; MGOE01000134; OGO54358.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1F8S3B5; -.
DR STRING; 1797663.A2V85_14305; -.
DR Proteomes; UP000176218; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:InterPro.
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:0008137; F:NADH dehydrogenase (ubiquinone) activity; IEA:InterPro.
DR GO; GO:0042773; P:ATP synthesis coupled electron transport; IEA:InterPro.
DR CDD; cd00207; fer2; 1.
DR Gene3D; 3.10.20.740; -; 1.
DR Gene3D; 3.30.70.20; -; 2.
DR Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 2.
DR InterPro; IPR036010; 2Fe-2S_ferredoxin-like_sf.
DR InterPro; IPR001041; 2Fe-2S_ferredoxin-type.
DR InterPro; IPR017896; 4Fe4S_Fe-S-bd.
DR InterPro; IPR017900; 4Fe4S_Fe_S_CS.
DR InterPro; IPR028261; DPD_II.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR023753; FAD/NAD-binding_dom.
DR InterPro; IPR000283; NADH_UbQ_OxRdtase_75kDa_su_CS.
DR PANTHER; PTHR43100:SF2; FERREDOXIN-DEPENDENT GLUTAMATE SYNTHASE, CHLOROPLASTIC-LIKE; 1.
DR PANTHER; PTHR43100; GLUTAMATE SYNTHASE [NADPH] SMALL CHAIN; 1.
DR Pfam; PF13510; Fer2_4; 1.
DR Pfam; PF14691; Fer4_20; 1.
DR Pfam; PF12838; Fer4_7; 1.
DR Pfam; PF07992; Pyr_redox_2; 1.
DR PRINTS; PR00419; ADXRDTASE.
DR SUPFAM; SSF54292; 2Fe-2S ferredoxin-like; 1.
DR SUPFAM; SSF54862; 4Fe-4S ferredoxins; 2.
DR SUPFAM; SSF46548; alpha-helical ferredoxin; 1.
DR SUPFAM; SSF51971; Nucleotide-binding domain; 1.
DR PROSITE; PS51085; 2FE2S_FER_2; 1.
DR PROSITE; PS00198; 4FE4S_FER_1; 1.
DR PROSITE; PS51379; 4FE4S_FER_2; 3.
DR PROSITE; PS00641; COMPLEX1_75K_1; 1.
PE 4: Predicted;
KW Iron {ECO:0000256|ARBA:ARBA00023004};
KW Iron-sulfur {ECO:0000256|ARBA:ARBA00023014};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723}.
FT DOMAIN 53..131
FT /note="2Fe-2S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51085"
FT DOMAIN 693..712
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51379"
FT DOMAIN 736..765
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51379"
FT DOMAIN 768..797
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51379"
FT REGION 1..27
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 858..888
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 860..888
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 888 AA; 97744 MW; E837003BFD0297EC CRC64;
MADLITRPDP TLERPREVRP DAPMVYDTVT PREDSLAERL ITTQSPQRPQ STPRIRIEVD
GRVVEGFEGQ TILEVCRDNG IEIPTLCYEP KLPGFGACRM CVVEVEGEET PPISCSRSAE
AGMVVQTQTE ELRRLRRTNL ELIFSDHNAY CLPPCQNKCP SHIDIPGFLK ANAEANWRES
ARIFKRTIPF PSILGRVCPA PCEEHCRRDE VDEAIAIRDS HRYAGDQVLR AMLDDGEDPP
LPFERQAPTG RRAAVIGSGP AGMAAAYYLL LNGHEVTVFE RDPAPGGMLR YGIPQYRLPK
VEVLEAEYEA VWRLGAKLQC NMALGRDFTL DDLQNQGFDA VVVAIGCYDT NKLGIANEDA
DGVIDGLEYL RTATLGLPYP GHEGTRAVVI GGGFTAMDCV RTSVRQGAGE VTLVYRRDMK
DMPAASEVHE AIEEGVTTIF QAGPTRVITD ERTGKVTGVE FIRMQLGEPD ASGRRRPEPA
PGTEFTIDCD RVLLAIGQGP DLRWIGPGSE GPLATRQRRL GADAVTFETA RPGVFGTGDV
RIGAATVVQA IAEGRRAAYA VDAYLRGQDL AAIRTRQTLA EPQPEFLSIV PFTGEVKEPR
YRLKALEAEV RNRSYIEYEI PYTRDEAVAE STRCLQCTCE AIGFCDLRRL GIEYGTTLRT
LEPAFHQGAG YRSVTENRFT GINHDYIRDD SHAFILREPS RCIDCGRCAN VCAEVVGAAC
YDFMRIGFDT LVTTPLDMSL NDTPCVSCGR CAETCPTGAL MPKPRVLQQY EVDESRCILC
GICVDACPYD AVRDSDQFEL SHTSREEPMI DLLALASIER ETEMSYIRRE RDWADRARAE
GRLLDPARNL PVLPASLVHG NGNGNGSGNG HAARQLGSGT GSGHAQDH
//
