ID A0A0G4KGD1_9PEZI Unreviewed; 1269 AA.
AC A0A0G4KGD1;
DT 16-SEP-2015, integrated into UniProtKB/TrEMBL.
DT 16-SEP-2015, sequence version 1.
DT 13-SEP-2023, entry version 28.
DE RecName: Full=RING-type domain-containing protein {ECO:0000259|PROSITE:PS50089};
GN ORFNames=BN1708_009389 {ECO:0000313|EMBL:CRJ93486.1};
OS Verticillium longisporum.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Glomerellales; Plectosphaerellaceae; Verticillium.
OX NCBI_TaxID=100787 {ECO:0000313|EMBL:CRJ93486.1, ECO:0000313|Proteomes:UP000044602};
RN [1] {ECO:0000313|EMBL:CRJ93486.1, ECO:0000313|Proteomes:UP000044602}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=VL1 {ECO:0000313|EMBL:CRJ93486.1};
RA Wang D.B., Wang M.;
RL Submitted (MAY-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- PATHWAY: Cofactor biosynthesis; molybdopterin biosynthesis.
CC {ECO:0000256|ARBA:ARBA00005046}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the MoeA family.
CC {ECO:0000256|ARBA:ARBA00008339}.
CC -!- SIMILARITY: In the N-terminal section; belongs to the MoaB/Mog family.
CC {ECO:0000256|ARBA:ARBA00007589}.
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DR EMBL; CVQH01001002; CRJ93486.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0G4KGD1; -.
DR STRING; 100787.A0A0G4KGD1; -.
DR OrthoDB; 275356at2759; -.
DR UniPathway; UPA00344; -.
DR Proteomes; UP000044602; Unassembled WGS sequence.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0061598; F:molybdopterin adenylyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0061599; F:molybdopterin molybdotransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0006777; P:Mo-molybdopterin cofactor biosynthetic process; IEA:UniProtKB-KW.
DR CDD; cd00887; MoeA; 1.
DR CDD; cd00886; MogA_MoaB; 1.
DR Gene3D; 3.40.980.10; MoaB/Mog-like domain; 2.
DR Gene3D; 2.40.340.10; MoeA, C-terminal, domain IV; 1.
DR Gene3D; 3.90.105.10; Molybdopterin biosynthesis moea protein, domain 2; 1.
DR Gene3D; 2.170.190.11; Molybdopterin biosynthesis moea protein, domain 3; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR036425; MoaB/Mog-like_dom_sf.
DR InterPro; IPR001453; MoaB/Mog_dom.
DR InterPro; IPR008284; MoCF_biosynth_CS.
DR InterPro; IPR038987; MoeA-like.
DR InterPro; IPR005111; MoeA_C_domain_IV.
DR InterPro; IPR036688; MoeA_C_domain_IV_sf.
DR InterPro; IPR005110; MoeA_linker/N.
DR InterPro; IPR036135; MoeA_linker/N_sf.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR InterPro; IPR017907; Znf_RING_CS.
DR NCBIfam; TIGR00177; molyb_syn; 2.
DR PANTHER; PTHR10192:SF5; GEPHYRIN; 1.
DR PANTHER; PTHR10192; MOLYBDOPTERIN BIOSYNTHESIS PROTEIN; 1.
DR Pfam; PF00994; MoCF_biosynth; 2.
DR Pfam; PF03454; MoeA_C; 1.
DR Pfam; PF03453; MoeA_N; 1.
DR Pfam; PF14634; zf-RING_5; 1.
DR SMART; SM00852; MoCF_biosynth; 2.
DR SUPFAM; SSF63867; MoeA C-terminal domain-like; 1.
DR SUPFAM; SSF63882; MoeA N-terminal region -like; 1.
DR SUPFAM; SSF53218; Molybdenum cofactor biosynthesis proteins; 2.
DR SUPFAM; SSF57850; RING/U-box; 1.
DR PROSITE; PS01078; MOCF_BIOSYNTHESIS_1; 1.
DR PROSITE; PS01079; MOCF_BIOSYNTHESIS_2; 1.
DR PROSITE; PS00518; ZF_RING_1; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 3: Inferred from homology;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Molybdenum cofactor biosynthesis {ECO:0000256|ARBA:ARBA00023150};
KW Reference proteome {ECO:0000313|Proteomes:UP000044602};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00175}.
FT DOMAIN 12..53
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT REGION 247..267
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 772..835
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 147..181
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 407..434
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 794..810
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1269 AA; 137388 MW; C3DB8C68E20ACC89 CRC64;
MEHSLKCNVL KCRQEITDRA LVTTCSHIFC IDCAGRSGLA GQSERRSSCP ACNSNLGNPD
DAVIAILSPS DEYKTSVLSG LSPNIIMECA GRALSFWAYQ TTQEMWVDAG VRAFLHLLTI
ASVYQKYLEK TLTDKYKALD MHLDKTVNEA NAEIESIQGQ LRDLALQNDS MRRKYDELGQ
AFKDKSRKLL QTQELYDRVK RKAEMGQMQA AACDAVDSHL QMNVFSDTRE RGSPRQGLYE
QQADFSQFHK SRGSDRTEMP PPQNRGASQF VVNDELWARQ NTLSGIDMQK APMITPVRQR
TRNTANIGLS AIPGLVAGSP VPLNGPTRMQ EFTIREQSAI AGNRESGVGD PSIDAAHLHH
PMSSSATPVP RDMSATSTAP GAVFDEADPP SNLQECRIPS EAEDQSLNSL AGEVESLKQQ
LAEVMHLRER EREQERCRRG DEQIQKEQLH KEQLVHERKL NAQRLIEMAQ LHDEALLQAS
RDHADSLAEA VSRVTRKLEM ERQALHAEDL LSVEAYRKLW NAEIGRRTKQ EKQLAMVRKE
LMATNSRLRV LGSVERADLL QSKVNKCKSI SQTVSLTPSS PDASATSVMA TSPLKVAILI
VSTTASKNPA SDKSELVLRD VIETEGGRQW EVVETKIVSD HVPQIQRQIM LWADLGADAV
NLIVTTGGTG FAVTDHTPEA VGALLHRQAP GIVHGMLATS LAVTPFAMMS RPVAGVRHST
VIVTLPGSPK GAKENLQAIL RTLPHACLQA AGVDSRALHS GGVKKLEADA GISAGQSASS
QSHGNDHSHT HGHGHSHDHN HGHSHNHGHG GLVRHTGNQQ VVSNDPSLGP TRRYRESPYP
MLAVEDALGI IEQHTPEADI VSRKVDADLI NAVLAEDVTA NENVPAFRAS IVDGYAVIVP
KDGNMKGVYP VTAVSHAAPS EIGTFKEGEI ARITTGAPLP PGATSVIMVE DTLLKTKTDD
GKEEKEVEIL ADGVKPGENV REVGSDIKKS DTILRKGEQI SGIGGEIGLL AAVGVASIKT
YRRPVVGVLS TGDEIVEHDR EGELRLGEVR DTNRVTLLAA AKERGFEAID LGIARDRPGA
LEETLREALR KVDLLVTTGG VSMGELDLLK PTIERSLGGT IHFGRVDMKP GKPTTFATVP
VKTNAGERVS KPVFALPGNP ASALVTFNLF VLPALHKLAG VEPRSLSKVP VVLAHDFALD
KGRPEYHRAV VTVGKDGILH ANSTGGQRSS RVGSLRSANA LLCLPKGNGP LKKGTQVHAL
LMGGVQAEI
//