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
//