ID A0A3E2H2F4_SCYLI Unreviewed; 1595 AA.
AC A0A3E2H2F4;
DT 16-JAN-2019, integrated into UniProtKB/TrEMBL.
DT 16-JAN-2019, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE RecName: Full=Rieske domain-containing protein {ECO:0008006|Google:ProtNLM};
DE Flags: Fragment;
GN ORFNames=B7463_g8754 {ECO:0000313|EMBL:RFU27586.1};
OS Scytalidium lignicola (Hyphomycete).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Leotiomycetes incertae sedis; Scytalidium.
OX NCBI_TaxID=5539 {ECO:0000313|EMBL:RFU27586.1, ECO:0000313|Proteomes:UP000258309};
RN [1] {ECO:0000313|EMBL:RFU27586.1, ECO:0000313|Proteomes:UP000258309}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 105466 {ECO:0000313|EMBL:RFU27586.1,
RC ECO:0000313|Proteomes:UP000258309};
RA Buettner E., Gebauer A.M., Hofrichter M., Liers C., Kellner H.;
RT "Draft genome sequence of Scytalidium lignicola DSM 105466, a ubiquitous
RT saprotrophic fungus.";
RL Submitted (MAY-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974};
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000256|ARBA:ARBA00001966};
CC -!- COFACTOR:
CC Name=siroheme; Xref=ChEBI:CHEBI:60052;
CC Evidence={ECO:0000256|ARBA:ARBA00001929};
CC -!- PATHWAY: Nitrogen metabolism; nitrate reduction (assimilation).
CC {ECO:0000256|ARBA:ARBA00005096}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: Belongs to the nitrite and sulfite reductase 4Fe-4S domain
CC family. {ECO:0000256|ARBA:ARBA00010429}.
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:RFU27586.1}.
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DR EMBL; NCSJ02000199; RFU27586.1; -; Genomic_DNA.
DR STRING; 5539.A0A3E2H2F4; -.
DR OMA; PHKIKFA; -.
DR UniPathway; UPA00653; -.
DR Proteomes; UP000258309; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IEA:InterPro.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR GO; GO:0020037; F:heme binding; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0050661; F:NADP binding; IEA:InterPro.
DR GO; GO:0008942; F:nitrite reductase [NAD(P)H] activity; IEA:InterPro.
DR GO; GO:0022857; F:transmembrane transporter activity; IEA:InterPro.
DR GO; GO:0042128; P:nitrate assimilation; IEA:UniProtKB-UniPathway.
DR CDD; cd17325; MFS_MdtG_SLC18_like; 1.
DR CDD; cd03529; Rieske_NirD; 1.
DR Gene3D; 3.90.480.20; -; 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; 1.20.1250.20; MFS general substrate transporter like domains; 1.
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; IPR011701; MFS.
DR InterPro; IPR020846; MFS_dom.
DR InterPro; IPR036259; MFS_trans_sf.
DR InterPro; IPR005117; NiRdtase/SiRdtase_haem-b_fer.
DR InterPro; IPR036136; Nit/Sulf_reduc_fer-like_dom_sf.
DR InterPro; IPR012744; Nitri_red_NirB.
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 NCBIfam; TIGR02374; nitri_red_nirB; 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; PF07690; MFS_1; 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; 2.
DR SUPFAM; SSF50022; ISP domain; 1.
DR SUPFAM; SSF103473; MFS general substrate transporter; 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; PS50850; MFS; 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 Membrane {ECO:0000256|SAM:Phobius};
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:UP000258309};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 1172..1193
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1200..1219
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1225..1244
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1265..1285
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1305..1323
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1378..1404
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1416..1435
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1447..1464
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1522..1543
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 918..1020
FT /note="Rieske"
FT /evidence="ECO:0000259|PROSITE:PS51296"
FT DOMAIN 1121..1559
FT /note="Major facilitator superfamily (MFS) profile"
FT /evidence="ECO:0000259|PROSITE:PS50850"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1563..1595
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1569..1587
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:RFU27586.1"
FT NON_TER 1595
FT /evidence="ECO:0000313|EMBL:RFU27586.1"
SQ SEQUENCE 1595 AA; 174872 MW; 985144569834AC08 CRC64;
MKTAVDMEAG SSLGVSTDGD DSEKIERKKV VVVGLGMVGI SFIEKLIKLD AKRREYDIVV
IGEESHLAYN RVGLTSFFQH RKVEDLYLNP KEWYQSVPAG SLNYHINTKV ISIDTSQKNV
ACSSGEIVAY DILVLATGSD ALLPRHTPGH DAKGVFVYRT IEDLESLINY SATKKGTVGT
VVGGGLLGLE AAKAMMDLEA FEKVKLVERN RWVLSRQLDS DAGGLVVEQV QALGLEVMLS
KRVGKIEVDE NNAVKGVVFE DGERTDCSTL CFAIGIKPRD ELAKSANIEC AERGGGIVVK
DDLSTSAKDV YAIGECASWE NQTFGLIAPG VEMADVLAFN LTQAKVHTYR KFKRPDLSTK
LKLLGVEVAS FGDFFADQDG PKYLPARAGR KKEGDQPVPV KALTYKDPFQ AVYKKYLFTL
DGKYLLGGMM IGDTKDYVKL VPMAKNQKML EVPPSQLILG ASKGDDDGAD DLDDDTQICS
CHNVAKGDVI KVVKDGTCKS IGDVKSCTKA GTGCGGCMPL VTTIFNNQMK AMGNEVKNHV
CPHLNYSRAD LYNIISVKQL KTLQEVMKDC GNDPESLGCE ACKPVLGSIF ASLYNQHVMD
KPTRGLQDTN DRYLGNIQRN GTYSVVPRVS AGEITPDKLI VIGNVAKKYN LYTKITGGQR
IDMFGAKKQD LIPIWEELIA GGMESGHAYA KSLRTVKSCV GSTWCRYGVG DSVGMAVRLE
ERYKSIRSPH KLKGGVSGCV RECAEAQSKD FGLIATDKGF NIFVGGNGGA KPKHTELLAK
DVFPDDVVPI IDRYLMFYIR TADKLQRTAR WLENLPGGIK YLREVILEDR LGICASLEAQ
MEELVGSFFD EWAETIKDVS KKAQFTQFNN TTETLETMES ITDRGQMRPV YWATESVKED
FRNTKWTSLT WQPIIEASHF AGADDAPNGI SATIKRGDTQ LAIFRVRGKY LASQQMCPHK
RAFVLSDGLI GDSGDKLWVS CPYHKRNYTL TGEQAGRCQN DEEVSIATFP VEERDDGWVY
LKLPPVHELD GVLGTKKWMV KQGESGPEPF EKLDKKMAIN RLKMKGRKPF EAKKEVVSQA
SNPLAPQRGI KLAGDNVIAN GMSSVTQTTD PMAVKYLHTI LEELGLISLY NSSIDVKLLC
LQRFVRLFAY GGSTLVLVAY QNALGISEAR TGLFMTLTLV GDVLISFFLT LTADALGRRA
ILALGAALMC GSGVIFALFD NYWVLLLAAI VGVISPSGNE IGPFRAIEES SVAHLTPTAN
RGDIYAWYSL VGTAGTAFGM MTTGWTVHYL RATKNWSSIE AYRAVFWGYA VFGFIKFLLS
ITLSSKIEAE KKQPPASTAQ DPEAAPLLGN NANGNAAAKQ KKRTFLSLLP EVSKESRLIV
VDLCLLFALD SFASGLAPLS WVTWFFKQKF DLQEGFLGSL FFITSIIAAC SMLIASSIAK
RFGNVKTMVF THLPSAISLA LIPIPNDLHF AMLFLILRSC TQSMDVAPRS AFLSAVVLPH
ERTAVLGLIN VVKTSASSLG PYITGILAGR GLFWVAFVVA GCLKATYDLG MLAVFAGHKT
REEREQEGLD EQAAEEEREA EQEELLRESE DPNER
//
