ID B2WHV4_PYRTR Unreviewed; 552 AA.
AC B2WHV4;
DT 01-JUL-2008, integrated into UniProtKB/TrEMBL.
DT 01-JUL-2008, sequence version 1.
DT 27-MAR-2024, entry version 59.
DE SubName: Full=Sulfite oxidase, mitochondrial {ECO:0000313|EMBL:EDU42614.1};
GN ORFNames=PTRG_09563 {ECO:0000313|EMBL:EDU42614.1};
OS Pyrenophora tritici-repentis (strain Pt-1C-BFP) (Wheat tan spot fungus)
OS (Drechslera tritici-repentis).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Pleosporales; Pleosporineae; Pleosporaceae;
OC Pyrenophora.
OX NCBI_TaxID=426418 {ECO:0000313|EMBL:EDU42614.1, ECO:0000313|Proteomes:UP000001471};
RN [1] {ECO:0000313|Proteomes:UP000001471}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Pt-1C-BFP {ECO:0000313|Proteomes:UP000001471};
RX PubMed=23316438; DOI=10.1534/g3.112.004044;
RA Manning V.A., Pandelova I., Dhillon B., Wilhelm L.J., Goodwin S.B.,
RA Berlin A.M., Figueroa M., Freitag M., Hane J.K., Henrissat B., Holman W.H.,
RA Kodira C.D., Martin J., Oliver R.P., Robbertse B., Schackwitz W.,
RA Schwartz D.C., Spatafora J.W., Turgeon B.G., Yandava C., Young S., Zhou S.,
RA Zeng Q., Grigoriev I.V., Ma L.-J., Ciuffetti L.M.;
RT "Comparative genomics of a plant-pathogenic fungus, Pyrenophora tritici-
RT repentis, reveals transduplication and the impact of repeat elements on
RT pathogenicity and population divergence.";
RL G3 (Bethesda) 3:41-63(2013).
CC -!- COFACTOR:
CC Name=Mo-molybdopterin; Xref=ChEBI:CHEBI:71302;
CC Evidence={ECO:0000256|ARBA:ARBA00001924};
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DR EMBL; DS231625; EDU42614.1; -; Genomic_DNA.
DR RefSeq; XP_001939895.1; XM_001939860.1.
DR AlphaFoldDB; B2WHV4; -.
DR STRING; 426418.B2WHV4; -.
DR EnsemblFungi; EDU42614; EDU42614; PTRG_09563.
DR GeneID; 6347853; -.
DR eggNOG; KOG0535; Eukaryota.
DR HOGENOM; CLU_003827_5_2_1; -.
DR InParanoid; B2WHV4; -.
DR OMA; CESYAAN; -.
DR OrthoDB; 1239at2759; -.
DR Proteomes; UP000001471; Unassembled WGS sequence.
DR GO; GO:0030151; F:molybdenum ion binding; IEA:InterPro.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR Gene3D; 2.60.40.650; -; 1.
DR Gene3D; 3.90.420.10; Oxidoreductase, molybdopterin-binding domain; 1.
DR InterPro; IPR014756; Ig_E-set.
DR InterPro; IPR005066; MoCF_OxRdtse_dimer.
DR InterPro; IPR008335; Mopterin_OxRdtase_euk.
DR InterPro; IPR000572; OxRdtase_Mopterin-bd_dom.
DR InterPro; IPR036374; OxRdtase_Mopterin-bd_sf.
DR PANTHER; PTHR19372:SF7; SULFITE OXIDASE, MITOCHONDRIAL; 1.
DR PANTHER; PTHR19372; SULFITE REDUCTASE; 1.
DR Pfam; PF03404; Mo-co_dimer; 1.
DR Pfam; PF00174; Oxidored_molyb; 1.
DR PRINTS; PR00407; EUMOPTERIN.
DR SUPFAM; SSF81296; E set domains; 1.
DR SUPFAM; SSF56524; Oxidoreductase molybdopterin-binding domain; 1.
PE 4: Predicted;
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Molybdenum {ECO:0000256|ARBA:ARBA00022505};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000001471}.
FT DOMAIN 213..393
FT /note="Oxidoreductase molybdopterin-binding"
FT /evidence="ECO:0000259|Pfam:PF00174"
FT DOMAIN 420..543
FT /note="Moybdenum cofactor oxidoreductase dimerisation"
FT /evidence="ECO:0000259|Pfam:PF03404"
FT REGION 1..30
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 552 AA; 61778 MW; 86936D674AF64CA4 CRC64;
MTGKSTQFKK SQELPAEGAV QPIRSDLSED EEYPGFRRFL RQRPYIIRHG TYFQPSEEPT
WDFEKPLFPI IMPNGKTGPY YLIDPPTPPM SPHLPIMLPY DHWRARRVTT ASADSRDYPQ
LQPRTCSIPT RDKTEYCRVQ RSAGAPDLSL KPACPAASRR LTLPSLNHAI AAKPQSTTMV
QLVHSVEEPL NREPQLEKLI QSFITEDGYD RNHGPIPQIN PNTHKVSVIG LVDNELSLSV
ADLQALPQHT VICALQCAGN RRHTMRTKLK EVHGIDWFDG AVMNCKWKGP LLKDVLEKAG
IKIEESKLKD AHVAFSCFQT PCQDDKFYGA SLPLSRIMDP KRSIMLALEM NDKPLPPNHG
APVRVVTPGI AGARSVKWLD QISVQMTESD SYYQQHDYKI LPPEADCKEK AEEYWGKVDA
LHDMPVNSVI AVPKSESTVR QEEDGTIEVK GYALPSGADG PIVKVEVSTD GGNSWADAEL
INTYDDEDAK DVELKWAWAL WKAKVKVEKG KEATVVSRAT DKSGNTQEKC PLWNFRGVAY
NGYGEVTGLK VV
//