GenomeNet

Database: UniProt
Entry: A0A409XVZ6_PSICY
LinkDB: A0A409XVZ6_PSICY
Original site: A0A409XVZ6_PSICY 
ID   A0A409XVZ6_PSICY        Unreviewed;      1304 AA.
AC   A0A409XVZ6;
DT   08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT   08-MAY-2019, sequence version 1.
DT   13-SEP-2023, entry version 18.
DE   RecName: Full=Urea carboxylase {ECO:0008006|Google:ProtNLM};
GN   ORFNames=CVT25_004411 {ECO:0000313|EMBL:PPQ94925.1};
OS   Psilocybe cyanescens.
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC   Agaricomycetidae; Agaricales; Agaricineae; Strophariaceae; Psilocybe.
OX   NCBI_TaxID=93625 {ECO:0000313|EMBL:PPQ94925.1, ECO:0000313|Proteomes:UP000283269};
RN   [1] {ECO:0000313|EMBL:PPQ94925.1, ECO:0000313|Proteomes:UP000283269}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=2631 {ECO:0000313|EMBL:PPQ94925.1,
RC   ECO:0000313|Proteomes:UP000283269};
RX   PubMed=30283667; DOI=10.1002/evl3.42;
RA   Reynolds H.T., Vijayakumar V., Gluck-Thaler E., Korotkin H.B.,
RA   Matheny P.B., Slot J.C.;
RT   "Horizontal gene cluster transfer increased hallucinogenic mushroom
RT   diversity.";
RL   Evol. Lett. 2:88-101(2018).
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:PPQ94925.1}.
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; NHYD01000192; PPQ94925.1; -; Genomic_DNA.
DR   STRING; 93625.A0A409XVZ6; -.
DR   InParanoid; A0A409XVZ6; -.
DR   OrthoDB; 313213at2759; -.
DR   Proteomes; UP000283269; 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; IPR011764; Biotin_carboxylation_dom.
DR   InterPro; IPR005482; Biotin_COase_C.
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; 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; 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:UP000283269}.
FT   DOMAIN          5..482
FT                   /note="Biotin carboxylation"
FT                   /evidence="ECO:0000259|PROSITE:PS50979"
FT   DOMAIN          131..332
FT                   /note="ATP-grasp"
FT                   /evidence="ECO:0000259|PROSITE:PS50975"
SQ   SEQUENCE   1304 AA;  144027 MW;  F7D9C0F9D93BC198 CRC64;
     MGIYDNHKLL IANRGEIAVR ILRTAKRIGL QTVAIYTPSD ALSPHVLQAN ESVPLKLPES
     TSTASSEAAA YLSISTIIDI CKTHSVTLVH PGYGFLSENA DFAAQVVENG MVWLGPRHEV
     IRWMGMKHEA RKIAQEAGIR VVPGSDGLVA SEQEALEAAS RCGFPVMLKA TAGGGGMGMV
     VCHDGESLVK NFRFTEGRAQ ALFHNNGIYL ERYYEAARHI EIQIFGNGQG SVIHLREREC
     SVQRRHQKVI EESPSPFCVS HPGLRERMCD VAVSLARAIK YNSAGTIEFL VDEETVNFYF
     LEMNTRIQVE HPVTEQIHPG LDLVELMIKQ GLEELSPNKG LLSTSPEMAQ ATYDQLHEQG
     LRQGYAHSIE GRIYAENPYD GFIPSPGLLQ HVSTDIVGHD WLRIDSWVET GMTITPHFDP
     LLAKVIVSGA SREEALSRFL MALGEVKILG PPNNIGYLAS IAENEQFRAG LVTTRFLETF
     KVHPSAFKVL SSGIDTTIQD LPGRHLKLGI PVSGPMDSLA FATANILVGN PKTTEGLEIV
     VVPGVKASFY FFVQTVLAVT GKDVTITVNN ERRLMWSKII VPPFSTVDIE AKPTSVTAGF
     RVYVCIRGGF PDVPPYLGSK STSMGLGGYQ GRSLIKGDLI SIENCSSASD EENAPCIPEL
     LTPSYPSHWV IYVLPGPHGD DEFITADGIQ RFYSTHWRIS PSSNRLGIRL DAPTSTEKIE
     WARDSGGEGG SHPSNILDNG YAPGTINING DTPVILTNEG PDMGGYLCIC TVATAEMWKL
     GQLAPGCTVQ FRRISWIAAL QRLVLNSQWL ETIEKFVSRT IEESPTVNFN LLNTETKDMA
     FFGVLHEQKG HEGYPSRLRI TFRQAGDSAI LVEFGEMHLD IFIRARIHAF QGIVNEKNVL
     GVLSVCPCIR SILVGCPILI DGCKADIINF HYDPDIISQH AFLRILVESA ALIPDNMDEM
     TFSGRRITFP IVLDDRWSKE AIQRYMSTAR DKAVYLPSNV EYLANNNGLA NAKEALQKLI
     ASDWLVLGVG FYLACPFLIP IDPRCRLIGQ KMNPSRTFTP RGAIGIAGPV AAIYPIESPG
     GYQLYGRTLP TWQTWGKGHD FRADKPWLLE AFDQVTPPFT TYHSFHFLSL LQITFKPVSE
     DEYVKIENEF DAGQYVFQIE SAQFSVRNHA QFLQSIGEEL QMFSTRQAEA SKREELKERV
     LLREWEETKT LLNTDNNGKG SIYNDTENGV RITAPLFANI WKLRCSANDI IESESQVLVV
     LEAMKTEIPV CAGEGNKGKS IIGFGKGVQE GHSVCPGDTL IILG
//
DBGET integrated database retrieval system