ID A0A0G4MZA9_9PEZI Unreviewed; 726 AA.
AC A0A0G4MZA9;
DT 16-SEP-2015, integrated into UniProtKB/TrEMBL.
DT 16-SEP-2015, sequence version 1.
DT 22-FEB-2023, entry version 24.
DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:CRK39459.1};
GN ORFNames=BN1708_001666 {ECO:0000313|EMBL:CRK39459.1};
OS Verticillium longisporum.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Glomerellales; Plectosphaerellaceae; Verticillium.
OX NCBI_TaxID=100787 {ECO:0000313|EMBL:CRK39459.1, ECO:0000313|Proteomes:UP000044602};
RN [1] {ECO:0000313|EMBL:CRK39459.1, ECO:0000313|Proteomes:UP000044602}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=VL1 {ECO:0000313|EMBL:CRK39459.1};
RA Wang D.B., Wang M.;
RL Submitted (MAY-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=biotin; Xref=ChEBI:CHEBI:57586;
CC Evidence={ECO:0000256|ARBA:ARBA00001953};
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DR EMBL; CVQH01025860; CRK39459.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0G4MZA9; -.
DR STRING; 100787.A0A0G4MZA9; -.
DR OrthoDB; 1459320at2759; -.
DR Proteomes; UP000044602; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0016874; F:ligase activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR CDD; cd06850; biotinyl_domain; 1.
DR Gene3D; 2.40.50.100; -; 1.
DR Gene3D; 3.30.470.20; ATP-grasp fold, B domain; 1.
DR InterPro; IPR011761; ATP-grasp.
DR InterPro; IPR005481; BC-like_N.
DR InterPro; IPR011764; Biotin_carboxylation_dom.
DR InterPro; IPR005482; Biotin_COase_C.
DR InterPro; IPR000089; Biotin_lipoyl.
DR InterPro; IPR005479; CbamoylP_synth_lsu-like_ATP-bd.
DR InterPro; IPR016185; PreATP-grasp_dom_sf.
DR InterPro; IPR011054; Rudment_hybrid_motif.
DR InterPro; IPR011053; Single_hybrid_motif.
DR PANTHER; PTHR18866; CARBOXYLASE:PYRUVATE/ACETYL-COA/PROPIONYL-COA CARBOXYLASE; 1.
DR PANTHER; PTHR18866:SF33; METHYLCROTONOYL-COA CARBOXYLASE SUBUNIT ALPHA, MITOCHONDRIAL-RELATED; 1.
DR Pfam; PF02785; Biotin_carb_C; 1.
DR Pfam; PF00289; Biotin_carb_N; 1.
DR Pfam; PF00364; Biotin_lipoyl; 1.
DR Pfam; PF02786; CPSase_L_D2; 1.
DR SMART; SM00878; Biotin_carb_C; 1.
DR SUPFAM; SSF56059; Glutathione synthetase ATP-binding domain-like; 1.
DR SUPFAM; SSF52440; PreATP-grasp domain; 1.
DR SUPFAM; SSF51246; Rudiment single hybrid motif; 1.
DR SUPFAM; SSF51230; Single hybrid motif; 1.
DR PROSITE; PS50975; ATP_GRASP; 1.
DR PROSITE; PS50979; BC; 1.
DR PROSITE; PS50968; BIOTINYL_LIPOYL; 1.
DR PROSITE; PS00867; CPSASE_2; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU00409}; Biotin {ECO:0000256|ARBA:ARBA00023267};
KW Ligase {ECO:0000256|ARBA:ARBA00022598};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU00409}; Reference proteome {ECO:0000313|Proteomes:UP000044602}.
FT DOMAIN 35..485
FT /note="Biotin carboxylation"
FT /evidence="ECO:0000259|PROSITE:PS50979"
FT DOMAIN 151..351
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT DOMAIN 643..718
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
SQ SEQUENCE 726 AA; 78722 MW; 7C5CFCBD045894C3 CRC64;
MRSMKAKHRL ARPLPRLLST AATGVSASAA PQITPITSLL IANRGEIALR IHKTAGRLGI
RTTTLYTDPD ASSQHAACSP HSLSLGNPKA YLDGDRIISL AKQHGIQALH PGYGFLSENP
AFASRCEKEG IVFVGPPAKA MHDMGDKARS KEIMTAAGVP CVPGYHGADQ EEAQLLQHAR
EVRFPVLLKS VKGGGGKGMR IVLTEDEFPA QLRSARLEAK ASFGDGGEVM LVEKYIVRPR
HVEVQVFADK HGNCVALGER DCSVQRRHQK ILEESPAPCL DEATRLDLWD KARKAASAVD
YVGAGTVEFI LDRDTGEFYF MEMNTRLQVE HPVSEMVTGT DLVEWQLNIA AGEKLPMTQE
EISEAISQRG AAIEARIYAE SPEKGFMPDS GKLVHLTTPA TDPDVRIDAG FVQGDTVSEA
YDGMIAKLIV RGRDRETAIR RLELALRDYE VVGLSTNIEF LKRMCRSPAF IEGDVETGFI
EKWKDELFAP RVITDEVFVQ AALGSLTAQL ASEAPHGGSL GFGAPNTASE RSFALKVLDA
YSKQDGEVVQ VTVSQTSPGM FSATVTRKGA EPVVIEKIAC TSSTPKSLAT KLTTFFPGER
IHSTVVRTTP NATETQDSKV VVFQHGVRTE LALLPPKWFE KALGLKEIAA SVVAPMPCKV
LRNEVAEGEV VKKGAPLVVI ESMKMETVIR SPQDGVVKKL AHKEGDICKA GTVLVLFEEE
AANEAS
//
