ID A0A423XCE6_9PEZI Unreviewed; 726 AA.
AC A0A423XCE6;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 28-JUN-2023, entry version 13.
DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:ROW13688.1};
GN ORFNames=VPNG_04572 {ECO:0000313|EMBL:ROW13688.1};
OS Cytospora leucostoma.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Diaporthales; Valsaceae; Cytospora.
OX NCBI_TaxID=1230097 {ECO:0000313|EMBL:ROW13688.1, ECO:0000313|Proteomes:UP000285146};
RN [1] {ECO:0000313|EMBL:ROW13688.1, ECO:0000313|Proteomes:UP000285146}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SXYLt {ECO:0000313|EMBL:ROW13688.1,
RC ECO:0000313|Proteomes:UP000285146};
RA Yin Z., Huang L.;
RT "Host preference determinants of Valsa canker pathogens revealed by
RT comparative genomics.";
RL Submitted (SEP-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=biotin; Xref=ChEBI:CHEBI:57586;
CC Evidence={ECO:0000256|ARBA:ARBA00001953};
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:ROW13688.1}.
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DR EMBL; LKEB01000018; ROW13688.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A423XCE6; -.
DR STRING; 1230097.A0A423XCE6; -.
DR InParanoid; A0A423XCE6; -.
DR Proteomes; UP000285146; 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:UP000285146}.
FT DOMAIN 37..484
FT /note="Biotin carboxylation"
FT /evidence="ECO:0000259|PROSITE:PS50979"
FT DOMAIN 150..350
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT DOMAIN 648..721
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
FT REGION 15..35
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 19..35
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 726 AA; 79191 MW; 04F0201B1603D1D9 CRC64;
MRSIKDAHRR LPIRPASRAL LSTTGSSSPS NTPSITPITS VIIANRGEIA LRVQRTAAKL
GIRTTTLYTD VDREAQHTTA TPYSLSLPNY LDGDRIISLA KQHNIQALHP GYGFLSENAT
FAQKCEDAGI VFVGPPASAM ADMGDKARSK EIMTAAGVPC VPGYHGSEQS VGALQAHARE
VGFPVLLKSV KGGGGKGMRI VNSEDEFPAQ LGSARAEARA SFGEGGEVML VEKYVVRPRH
VEVQVFADKH GGCVALGERD CSVQRRHQKI LEESPAPLLD EATRKDLWEK AKTAALTVGY
VGAGTVEFIL DRDSGKFYFM EMNTRLQVEH PVSEMVTGTD LVEWQLRVAA GEKLPLTQEE
IEKNIAKRGA AIEARIYAEN PEKEFMPDSG KLVHLVTPKT DDDVRIDAGF IEGDTVSSAY
DGMIAKLIVR GKDRETALRK LELALREYEV VGLSTNIEFL KRLCRSQAFI DGDVETGFIK
KHGEDLFRPT RVDNEVFIQA SLGLLTSQLQ IDASRSGPHG ESLGFGEGSA TSSERNFAFK
VIDGYSSQEG EIVEASITQL GNNLFSASVS RKDQDAPQIF ENLICEPTTT AARPQAKTGV
RTFFPLERID TTVVQDPTHE HKISVFQHGH KTELLLQRPS WYDEALGLKE VAASAVAPMP
CKILRNEVKE GETVEKGAPL VVIESMKMET VIRSPQSGVV KKLAHKEGDI CKAGTVLVIF
EEGEST
//
