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Database: UniProt
Entry: A0A084QPC3_STAC4
LinkDB: A0A084QPC3_STAC4
Original site: A0A084QPC3_STAC4 
ID   A0A084QPC3_STAC4        Unreviewed;      1160 AA.
AC   A0A084QPC3;
DT   29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   29-OCT-2014, sequence version 1.
DT   24-JAN-2024, entry version 41.
DE   RecName: Full=Rieske domain-containing protein {ECO:0000259|PROSITE:PS51296};
GN   ORFNames=S40285_05369 {ECO:0000313|EMBL:KFA65808.1};
OS   Stachybotrys chlorohalonata (strain IBT 40285).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Stachybotryaceae; Stachybotrys.
OX   NCBI_TaxID=1283841 {ECO:0000313|EMBL:KFA65808.1, ECO:0000313|Proteomes:UP000028524};
RN   [1] {ECO:0000313|EMBL:KFA65808.1, ECO:0000313|Proteomes:UP000028524}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IBT 40285 {ECO:0000313|EMBL:KFA65808.1,
RC   ECO:0000313|Proteomes:UP000028524};
RX   PubMed=25015739; DOI=10.1186/1471-2164-15-590;
RA   Semeiks J., Borek D., Otwinowski Z., Grishin N.V.;
RT   "Comparative genome sequencing reveals chemotype-specific gene clusters in
RT   the toxigenic black mold Stachybotrys.";
RL   BMC Genomics 15:590-590(2014).
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000256|ARBA:ARBA00001974};
CC   -!- COFACTOR:
CC       Name=siroheme; Xref=ChEBI:CHEBI:60052;
CC         Evidence={ECO:0000256|ARBA:ARBA00001929};
CC   -!- SIMILARITY: Belongs to the nitrite and sulfite reductase 4Fe-4S domain
CC       family. {ECO:0000256|ARBA:ARBA00010429}.
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DR   EMBL; KL660551; KFA65808.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A084QPC3; -.
DR   STRING; 1283841.A0A084QPC3; -.
DR   HOGENOM; CLU_003291_0_0_1; -.
DR   InParanoid; A0A084QPC3; -.
DR   OMA; FAQVDPW; -.
DR   OrthoDB; 275583at2759; -.
DR   UniPathway; UPA00653; -.
DR   Proteomes; UP000028524; Unassembled WGS sequence.
DR   GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IEA:InterPro.
DR   GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR   GO; GO:0020037; F:heme binding; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0008942; F:nitrite reductase [NAD(P)H] activity; IEA:InterPro.
DR   GO; GO:0009058; P:biosynthetic process; IEA:UniProt.
DR   GO; GO:0042128; P:nitrate assimilation; IEA:UniProtKB-UniPathway.
DR   CDD; cd19944; NirB_Fer2_BFD-like_2; 1.
DR   CDD; cd03529; Rieske_NirD; 1.
DR   Gene3D; 1.10.10.1100; BFD-like [2Fe-2S]-binding domain; 1.
DR   Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 2.
DR   Gene3D; 2.102.10.10; Rieske [2Fe-2S] iron-sulphur domain; 1.
DR   Gene3D; 3.30.413.10; Sulfite Reductase Hemoprotein, domain 1; 1.
DR   InterPro; IPR007419; BFD-like_2Fe2S-bd_dom.
DR   InterPro; IPR041854; BFD-like_2Fe2S-bd_dom_sf.
DR   InterPro; IPR036188; FAD/NAD-bd_sf.
DR   InterPro; IPR023753; FAD/NAD-binding_dom.
DR   InterPro; IPR005117; NiRdtase/SiRdtase_haem-b_fer.
DR   InterPro; IPR036136; Nit/Sulf_reduc_fer-like_dom_sf.
DR   InterPro; IPR006067; NO2/SO3_Rdtase_4Fe4S_dom.
DR   InterPro; IPR045854; NO2/SO3_Rdtase_4Fe4S_sf.
DR   InterPro; IPR006066; NO2/SO3_Rdtase_FeS/sirohaem_BS.
DR   InterPro; IPR012748; Rieske-like_NirD.
DR   InterPro; IPR017941; Rieske_2Fe-2S.
DR   InterPro; IPR036922; Rieske_2Fe-2S_sf.
DR   NCBIfam; TIGR02378; nirD_assim_sml; 1.
DR   PANTHER; PTHR43809; NITRITE REDUCTASE (NADH) LARGE SUBUNIT; 1.
DR   PANTHER; PTHR43809:SF1; NITRITE REDUCTASE (NADH) LARGE SUBUNIT; 1.
DR   Pfam; PF04324; Fer2_BFD; 1.
DR   Pfam; PF01077; NIR_SIR; 1.
DR   Pfam; PF03460; NIR_SIR_ferr; 1.
DR   Pfam; PF07992; Pyr_redox_2; 1.
DR   Pfam; PF13806; Rieske_2; 1.
DR   PRINTS; PR00368; FADPNR.
DR   PRINTS; PR00397; SIROHAEM.
DR   SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
DR   SUPFAM; SSF50022; ISP domain; 1.
DR   SUPFAM; SSF56014; Nitrite and sulphite reductase 4Fe-4S domain-like; 1.
DR   SUPFAM; SSF55124; Nitrite/Sulfite reductase N-terminal domain-like; 1.
DR   PROSITE; PS00365; NIR_SIR; 1.
DR   PROSITE; PS51296; RIESKE; 1.
PE   3: Inferred from homology;
KW   FAD {ECO:0000256|ARBA:ARBA00022827};
KW   Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW   Heme {ECO:0000256|ARBA:ARBA00022617}; Iron {ECO:0000256|ARBA:ARBA00023004};
KW   Iron-sulfur {ECO:0000256|ARBA:ARBA00023014};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Nitrate assimilation {ECO:0000256|ARBA:ARBA00023063};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Reference proteome {ECO:0000313|Proteomes:UP000028524}.
FT   DOMAIN          970..1082
FT                   /note="Rieske"
FT                   /evidence="ECO:0000259|PROSITE:PS51296"
FT   REGION          1..59
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1107..1160
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        14..34
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1123..1138
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1145..1160
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1160 AA;  127532 MW;  F9B415F733099DC8 CRC64;
     MPGLVETPAP AVVPASTDLQ SNMPEPSERS TSPSDAGPEV PPMTRATTPE SDTSDPPRKR
     AAVVGLGMVG IAFIEKLLKY DLEGGRDEWE VTVFGEEPHI AYNRVGLTQY FTNRSIDELY
     LNPLEWYASH AKGKLTYHLS DPVVSIDAEA KTLKTEKGLD FGYDECILAT GSDAALPPYL
     SRERFWKTKG SFLYRTIKDL DDIIGYAVDA PKTLGRRIRR AAVIGGGLLG LEAAKALLDL
     EEVEQVVLVE RNRWVLSRQL DQEGGTLVLE KVKSLGVEVL LQARVRNVIW NDEDRLTGLM
     LEGQNGKEDE PYDVDMLVFA VGIKPRDDLA KVTPLTVAKR GGGFVVDPQL RTNLPNVYAI
     GECANFLDQT FGLIAPGIEM ADVLAFNLTE GPHHQLRNLK APDVSTKLKL MGVDVASFGD
     FFADQGKISK PLPGTTRGRK GDVSSLSPEE IRSKVKSLTY RDPFSDVYKK YIFTADGKYI
     LGGMMVGDVK DFVKLVALCN KGAAIDKPPA EFIIGAKKEG EEEGDDLPDD AQICSCHNVS
     KGDVVKCVKS GGIRSFGEMK SSTKCGTGCG GCIPLATSIF NRALKDAGVE VSNHICKDFA
     YSRQELFQVI KFKKLKDFSS TMRAVGKKSD SLGCEVCRPA VGSILSSLYN EWIMEPSLRQ
     TQDTNDRYLA NMQRDGTYSV VPRLAGGEVT PAGLKVLGEI GTEFGLYTKI TGGQRIDLFG
     AKKQDLPQIW EKLVDAGFES GHAYGKALRT VKSCVGSTWC RYGLGDSVGL AVELEQRYKG
     LRAPHKFKGG VSGCVRECAE AQSKDFGLIA TPKGWNVFVG GNGGAKPRHA EIIAEDVTKR
     EAIRILDRFL IFYIRSADKL ERTARWIEKY PGGIKGIKDV VVKDSLGICA ELEKEMETLV
     GLYHCEWTNV VNSKERRKAF KQFANTDETQ NVSELISERT QNRPADWPAD SSPLHFSVLD
     VAKDAQWEWR SVCKLSNLDR QEDSPTSVTI KYGDSQLAVW NIPGRGLRAS QNMCPHRRAF
     VLADGLVGED EKGREYVSCP LHKRNYLLES NQKEGGGSCS DTDYSIMTFE AKADEENDAI
     LLKLPPTDAL DAVLSTTKWM LKKAQEETDK LGGSGNVEIA EPLPADKMEE RKNRFHAKMG
     QQPEPASTPK ASCGDSSLDW
//
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