ID A0A3M2RXX5_9HYPO Unreviewed; 1534 AA.
AC A0A3M2RXX5;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 24-JAN-2024, entry version 25.
DE RecName: Full=Flavodoxin-like domain-containing protein {ECO:0000259|PROSITE:PS50902};
GN ORFNames=CDV36_010209 {ECO:0000313|EMBL:RMJ10148.1};
OS Fusarium kuroshium.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium;
OC Fusarium solani species complex.
OX NCBI_TaxID=2010991 {ECO:0000313|EMBL:RMJ10148.1, ECO:0000313|Proteomes:UP000277212};
RN [1] {ECO:0000313|EMBL:RMJ10148.1, ECO:0000313|Proteomes:UP000277212}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UCR3666 {ECO:0000313|EMBL:RMJ10148.1};
RA Stajich J.E., Carrillo J., Kijimoto T., Eskalen A., O'Donnell K.,
RA Kasson M.;
RT "Comparative genomic analysis of Ambrosia Fusariam Clade fungi.";
RL Submitted (JUN-2017) to the EMBL/GenBank/DDBJ databases.
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 -!- 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:RMJ10148.1}.
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DR EMBL; NKUJ01000213; RMJ10148.1; -; Genomic_DNA.
DR STRING; 2010991.A0A3M2RXX5; -.
DR Proteomes; UP000277212; Unassembled WGS sequence.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0010181; F:FMN 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:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR CDD; cd07034; TPP_PYR_PFOR_IOR-alpha_like; 1.
DR Gene3D; 3.40.50.360; -; 1.
DR Gene3D; 3.40.50.920; -; 1.
DR Gene3D; 3.40.50.970; -; 2.
DR Gene3D; 3.90.480.20; -; 1.
DR Gene3D; 3.30.413.10; Sulfite Reductase Hemoprotein, domain 1; 2.
DR Gene3D; 3.90.480.10; Sulfite Reductase Hemoprotein;Domain 2; 1.
DR InterPro; IPR001094; Flavdoxin-like.
DR InterPro; IPR008254; Flavodoxin/NO_synth.
DR InterPro; IPR029039; Flavoprotein-like_sf.
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; IPR045169; NO2/SO3_Rdtase_4Fe4S_prot.
DR InterPro; IPR045854; NO2/SO3_Rdtase_4Fe4S_sf.
DR InterPro; IPR006066; NO2/SO3_Rdtase_FeS/sirohaem_BS.
DR InterPro; IPR002880; Pyrv_Fd/Flavodoxin_OxRdtase_N.
DR InterPro; IPR029061; THDP-binding.
DR InterPro; IPR009014; Transketo_C/PFOR_II.
DR PANTHER; PTHR11493:SF47; SULFITE REDUCTASE [NADPH] SUBUNIT BETA; 1.
DR PANTHER; PTHR11493; SULFITE REDUCTASE [NADPH] SUBUNIT BETA-RELATED; 1.
DR Pfam; PF00258; Flavodoxin_1; 1.
DR Pfam; PF01077; NIR_SIR; 1.
DR Pfam; PF03460; NIR_SIR_ferr; 2.
DR Pfam; PF01855; POR_N; 1.
DR PRINTS; PR00369; FLAVODOXIN.
DR PRINTS; PR00397; SIROHAEM.
DR SUPFAM; SSF52218; Flavoproteins; 1.
DR SUPFAM; SSF56014; Nitrite and sulphite reductase 4Fe-4S domain-like; 2.
DR SUPFAM; SSF55124; Nitrite/Sulfite reductase N-terminal domain-like; 2.
DR SUPFAM; SSF52518; Thiamin diphosphate-binding fold (THDP-binding); 2.
DR SUPFAM; SSF52922; TK C-terminal domain-like; 1.
DR PROSITE; PS50902; FLAVODOXIN_LIKE; 1.
DR PROSITE; PS00365; NIR_SIR; 1.
PE 3: Inferred from homology;
KW 4Fe-4S {ECO:0000256|ARBA:ARBA00022485};
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 Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000277212}.
FT DOMAIN 794..943
FT /note="Flavodoxin-like"
FT /evidence="ECO:0000259|PROSITE:PS50902"
FT REGION 207..287
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 238..287
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1534 AA; 168769 MW; 867B9E69B7E46457 CRC64;
MDAAQPHQIK TPEEAVARIA YLSSDVIVSV QPAIGTESDF SAHLKRYAGR KDSSLVAQSA
DAVPDILPVR HNADPLLSVY TPIRAGKLVS VTTTSSILLP SVSHLYKLAN YPVVLHVSLQ
PRTFADYSVI TAIRNSGWTF VQSETLQEAQ DMALTAHALA IRTGKGVIHF FAPSTSEKDK
PIAIEDAAVI RDILDIESVR RFQAGPTASS QSGIYADDGH TAVSSDHDAP VTGAAHNGSL
TVPPSASASK APSAGTSVKS SQDSEASTPV APSSAATTVE TTPPQVSSED VYKCSARIWG
QIKTAFGREY SAFEYSGPPD AENCLFIFGS DAGAFAQAID DANSDEIFAS AAILTPRLYR
PWIGSRLVEA IPRSVKRIAV LEQIHRKTTK WGPLLIDVLT SVKSGPGGVE TIVGHQLGYL
APEVVVQALR GVLQNLTAEK PIQNLEVGKK SAWKEPTGYD LKTPQLETAY TKILDQLFGK
RAYVANAIKS ATTGLSPTVA ASPEFGFGSL LARKQRRNQF VSQVKDAATN GSFITDAPKS
WLARWAMNAD DATKSTEIAD DVIARLETDG SSLAAELLSA KGLFRKESLW LTGSDAWSYD
LGNSGVHHVL ASGENVNMLI IDSTPYSQRA TADANRRKKD IGLYAMNFGN VYVASTAVYS
SYTQVLQALL EADKFDGPSV VLAYLPYFGE TDSPLTVLQE TKKAVDAGYW PLYRWNPDNE
KKGEPNFSLD SELIKQELKK FLARDNQLTQ LAAKEPKFAA ALAQDFGTEV RAQQKRKAKD
AYNQLLEGLL GAPLTILFAS DNGNAGTVAK RLANRGRARG LKTAVMTMED YPLEDLPAEE
NIVFITSTAG QGEFPQNGLP FWDAIKDNTD LDLATVNYSV FGLGDSHYWP RKEDRIYYNK
PAKDLDRVMT NLGAKHLVPI GLGDDQDPDG FQTGYQEWEP KIWTALGVDN VDGLPEEPPP
ITNEDIKLAS NYLRGTIVEG LNDTSTLAIS AADQQLTKFH GTYMQDDRDI RDERKAQGLE
PAYSFMIRCR LPGGISTPKQ WIQMDDIANE LGNETMKLTT RQTFQFHGIV KSKLKPAMQA
INRALMTTIA ACGDVNRNVM CSSLPTHSKY HRQVFACSQL ISDHLLPSTT AYHEIWLTDE
NNEKTQVAGD AVQDFEPLYG PTYLPRKFKI TIGIPPHNDT DVYAHDIGLI AIKGEDGNLA
GFNVLAGGGM GTTHNNKKTY PQTGRMFGFC KTEDIHIVCE KIMLVQRDNG DRKNRKHARL
KYTIDDMTVP VFRSKVEELW GKKFEPEKPF EFKSNVDTFG WQKDEFGLSH FTFFIENGRI
EDTAEFQMKT GLREIAKVHK GEFRLTGNQH LILSGVADED LPAMKELMKK YKLDNIQFSG
LRLSSSACVA FPTCGLAMAE SERYLPVLIS KLEACLEENG LRQDSIVMRM TGCPNGCARP
WLAEVAFVGK AYGAYNMYLG GGYHGQRLNK LYRQSIKEDE ILAIMKPLLK QYALERQEGE
RFGDFCVRTG VIVATTDGQN FHDNIPEEDE EDEE
//