ID A0A3D8QFW4_9HELO Unreviewed; 1244 AA.
AC A0A3D8QFW4;
DT 16-JAN-2019, integrated into UniProtKB/TrEMBL.
DT 16-JAN-2019, sequence version 1.
DT 13-SEP-2023, entry version 13.
DE RecName: Full=Urea carboxylase {ECO:0008006|Google:ProtNLM};
GN ORFNames=BP6252_12062 {ECO:0000313|EMBL:RDW60679.1};
OS Coleophoma cylindrospora.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Helotiales; Dermateaceae; Coleophoma.
OX NCBI_TaxID=1849047 {ECO:0000313|EMBL:RDW60679.1, ECO:0000313|Proteomes:UP000256645};
RN [1] {ECO:0000313|EMBL:RDW60679.1, ECO:0000313|Proteomes:UP000256645}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BP6252 {ECO:0000313|EMBL:RDW60679.1,
RC ECO:0000313|Proteomes:UP000256645};
RX PubMed=30018880; DOI=10.5598/imafungus.2018.09.01.13;
RA Wingfield B.D., Bills G.F., Dong Y., Huang W., Nel W.J.,
RA Swalarsk-Parry B.S., Vaghefi N., Wilken P.M., An Z., de Beer Z.W.,
RA De Vos L., Chen L., Duong T.A., Gao Y., Hammerbacher A., Kikkert J.R.,
RA Li Y., Li H., Li K., Li Q., Liu X., Ma X., Naidoo K., Pethybridge S.J.,
RA Sun J., Steenkamp E.T., van der Nest M.A., van Wyk S., Wingfield M.J.,
RA Xiong C., Yue Q., Zhang X.;
RT "IMA Genome-F 9: Draft genome sequence of Annulohypoxylon stygium,
RT Aspergillus mulundensis, Berkeleyomyces basicola (syn. Thielaviopsis
RT basicola), Ceratocystis smalleyi, two Cercospora beticola strains,
RT Coleophoma cylindrospora, Fusarium fracticaudum, Phialophora cf. hyalina,
RT and Morchella septimelata.";
RL IMA Fungus 9:199-223(2018).
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:RDW60679.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; PDLM01000015; RDW60679.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3D8QFW4; -.
DR STRING; 1849047.A0A3D8QFW4; -.
DR Proteomes; UP000256645; Unassembled WGS sequence.
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; IPR001882; Biotin_BS.
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; SSF160467; PH0987 N-terminal 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; PS00188; BIOTIN; 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};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU00409}; Reference proteome {ECO:0000313|Proteomes:UP000256645}.
FT DOMAIN 8..462
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 1163..1235
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
SQ SEQUENCE 1244 AA; 135624 MW; C12801C7421D5809 CRC64;
MAAYTFSHVK KVLVANRGEI AVRCIKACAA AGIKSVSVYT ESDSTSDHVS LADEAVLLSG
QNVNGYLNVE NLLQICKSHQ VDAVIPGYGF LSENVDFAKE VQDAGMIFVG PSSESILEMG
QKHRARALAV EADVPVVPGS ELLTSEADAI AAATKLGYPI MLKATGGGGG MGLEVCNAEE
DIKSAFTKVK GRGDSLFGNN GVFMEKYYPS SRHVEVQVFG NGEEVIHFGE RECSIQRRHQ
KVIEECPSPY VHSHPEMRQR LTNCAVAYAS KLKYKSAGTV EFLVDDISGD FFFLEMNTRL
QVEHGITELC YDVDLVALML RQADYEKSGA IGIPTADLRS FQKDGPNGAA IEVRVYAEVP
YRNFAPSPGL LQAVDWPQGD GIRVDTWVRT GQRIAPYYDP LLAKVMVHAV DRATAMPKML
KTLSDCLLQG PATNLHYLSA VIASDGFQKG ETLTNYLSTK FQYKPCAFDV LAAGAFTTVQ
DYPARATSGH GIPMGGPMDN ISSRIANVLV GNSPGMETLE ITISGPELLF TASAVFAVCG
APMPVTIDGI EKPMWSRLVI KAGQKLKIGA AKNGGCRNYL AIKGGFPDVP VYLGSKAATP
SLKYGGTQGR QLQTSDYIAL AEETEIWAAE ATEYTLPASC IPNFDISEVY VLHGPHDDDT
FMTAKDREML YSTKWKIGHN SNRTGIRLIG PVPEWSRKDG GDGGAHPSNC FDYGYPLGGI
NWGGDSSVVF SMDSPNLGGL ICSSTVISAD LWRMGQLKPG ESVRLKPTTY DNSLQLTDRV
EKYVSQMQEL VEGKTIHVPV LDVALPEGET GAVLKKVEGD GGVRPEVKYR QGGDSYLIVE
FGQQKADITI TCRIRLLIQK IEALQIPGIV MNPSIIGVTI QFDSRVITQH ELLRKVDELE
SAIEPTLDVT IPVRTVKLPV VLDHPSLTEC LERYMATIRS TAGYLPDNVD YLRKANGFST
RREVFEILLQ SRFLIVSVGF LVGNPILFPL NPMSHITGQK FNPTRIATPG GTVGIGGSLF
SLYPVEQPGG YMMLARTLET WDTFGTKPGF SPTNPWLWEP FDMVTFYEVS VDEYNSIEAD
FIAGRYQWNV SEDIFNLHEI YNVLESAKTD PKYVAFKEGQ RKGVAEQLAI ENKMYSDWTA
GLAATAASEA ERLKEIMLLN PNPINIDSPI DANVWKVEVN IGDVLKKDQV VVILEAMKME
INILVPEDAI GSTVQAIASK PGSTVAPGSL LVVAKGKEPD PKTE
//
