ID A0A0G2ERS8_9EURO Unreviewed; 1238 AA.
AC A0A0G2ERS8;
DT 22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2015, sequence version 1.
DT 22-FEB-2023, entry version 29.
DE SubName: Full=Putative urea carboxylase {ECO:0000313|EMBL:KKY24949.1};
GN ORFNames=UCRPC4_g02250 {ECO:0000313|EMBL:KKY24949.1};
OS Phaeomoniella chlamydospora.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Chaetothyriomycetidae; Phaeomoniellales; Phaeomoniellaceae; Phaeomoniella.
OX NCBI_TaxID=158046 {ECO:0000313|EMBL:KKY24949.1, ECO:0000313|Proteomes:UP000053317};
RN [1] {ECO:0000313|EMBL:KKY24949.1, ECO:0000313|Proteomes:UP000053317}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UCRPC4 {ECO:0000313|EMBL:KKY24949.1};
RA Lawrence D.P., Travadon R., Rolshausen P.E., Baumgartner K.;
RT "Distinctive expansion of gene families associated with plant cell wall
RT degradation and secondary metabolism in the genomes of grapevine trunk
RT pathogens.";
RL Submitted (MAY-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KKY24949.1, ECO:0000313|Proteomes:UP000053317}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UCRPC4 {ECO:0000313|EMBL:KKY24949.1};
RA Morales-Cruz A., Amrine K.C., Cantu D.;
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};
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:KKY24949.1}.
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DR EMBL; LCWF01000054; KKY24949.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0G2ERS8; -.
DR OrthoDB; 313213at2759; -.
DR Proteomes; UP000053317; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
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; 3.30.1360.40; -; 1.
DR Gene3D; 3.30.470.20; ATP-grasp fold, B domain; 1.
DR Gene3D; 2.40.100.10; Cyclophilin-like; 2.
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; IPR003778; CT_A_B.
DR InterPro; IPR003833; CT_C_D.
DR InterPro; IPR029000; Cyclophilin-like_dom_sf.
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 Pfam; PF02626; CT_A_B; 1.
DR Pfam; PF02682; CT_C_D; 1.
DR SMART; SM00796; AHS1; 1.
DR SMART; SM00797; AHS2; 1.
DR SMART; SM00878; Biotin_carb_C; 1.
DR SUPFAM; SSF50891; Cyclophilin-like; 2.
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; PS00866; CPSASE_1; 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 Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Ligase {ECO:0000256|ARBA:ARBA00022598}; Membrane {ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU00409}; Reference proteome {ECO:0000313|Proteomes:UP000053317};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 969..992
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 8..463
FT /note="Biotin carboxylation"
FT /evidence="ECO:0000259|PROSITE:PS50979"
FT DOMAIN 126..324
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT DOMAIN 1157..1236
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
SQ SEQUENCE 1238 AA; 134815 MW; 697DA30F33EC2012 CRC64;
MTSRSLSHIK KVLIANRGEI AVRCIKACAA AGVKSVAIYT EADATSLHVS LADESAHLPG
SNSTAYTNGD DIIEICKQHH VDAVLPGYGF LSENTDFAAS VYAAGMVFCG PSSESISAMG
LKHEAREIAL KANVPIVPGS PLLSSAEDAV ATAKKLGFPI MLKATGGGGG MGLQVCNTSD
EVATAFQRVE SRGAALFKNS GVFLERYYPN SRHVEVQVAG NGEKVIHFGE RECSLQRRHQ
KVIEECPSPF VEAHSGLREK LTASAVSYAS QLNYKSVGTV EFLVDDETGD YFFLEMNTRL
QVEHPVTEKC YDVDLVQLML RQADYEKGGL KGIPTEELLA LQKSGPKGAA IEARIYAEIP
SRDFAPSPGL LQHVEWPEGQ GIRVDTWVKT GQRIPPYYDP LIAKLIVHSS EGRESVRQEM
LRALSKTSLQ GPPTNLEYLS KVIGTENFKT GDTLTNFLSS KFVYEPCAID VISPGAFTTV
QDFPARPGQA HGVPSGGPMD SVSSRVANLL VGNSAGAELL EVTVSGPELL FHASAVVSVC
GAKMSEVSVD GETQPMWSRF VVRKGQKLKV GKVETSGCRC YIAVKGGFPS VASYLGSKGA
TPSLAFGGTQ GRQVQLGDLL ALSEESEAWA AETETYSLPS DILPSFDFEQ VYCMHGPHDS
DDIMTQEDRD MIYSTSWKIG HNSNRTGVRL VGPAPKWARK DGGEGGAHPS NVFDYGYPSP
GGINWTGDDP VVFVADSPDL GGLVCSTTVC SGEMWKIGQL KPGDFVKLTP TTYENALNLL
NRNERYIEDI QRFVSGDVTH KPALHYGVSD GATPAILKVV KRSDGRPDVT YRQGGDRFLI
VKYGIETADL MIVSRVRLLT QALEEQKIEN LVLNPNVGTV TMQFDSKIIS QSKLLDLICQ
LDDQLGDPIK AHIPCRELHV PACLDHPDLQ EAIQRYMDTA RPTAVYLPDN VEYLRKNNAL
AKRRDAFEVL LNTPFLAVAV GFLVGTPILF PLDPRYTIVG QKYNPSRVFT PGGTIGIGGS
LFAIYPIDAP GGYMILARTL EAWDAFGTRP GFNPSKPWLY EPFDVVRFHE VTLEEYNQAH
RDFIAGKYQF DIRDTVFDVE HYYNLFASRK ADPSYQEYRD RQRAAAKEQL AIENKMLSEW
MESKASAAQS EAQQLQSILE SDSGLMISSP IDANVWKVLV EPGDVLKEGQ LVVILEAMKM
EINVNCGADL AGAVVKGIAS RPGSIVSPGK PLIVAAKE
//
