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Database: UniProt
Entry: A0A507ASH0_9PEZI
LinkDB: A0A507ASH0_9PEZI
Original site: A0A507ASH0_9PEZI 
ID   A0A507ASH0_9PEZI        Unreviewed;      1207 AA.
AC   A0A507ASH0;
DT   18-SEP-2019, integrated into UniProtKB/TrEMBL.
DT   18-SEP-2019, sequence version 1.
DT   13-SEP-2023, entry version 15.
DE   RecName: Full=Urea carboxylase {ECO:0008006|Google:ProtNLM};
GN   ORFNames=E0L32_006587 {ECO:0000313|EMBL:TPX12942.1};
OS   Thyridium curvatum.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Sordariomycetes incertae sedis; Thyridiaceae; Thyridium.
OX   NCBI_TaxID=1093900 {ECO:0000313|EMBL:TPX12942.1, ECO:0000313|Proteomes:UP000319257};
RN   [1] {ECO:0000313|EMBL:TPX12942.1, ECO:0000313|Proteomes:UP000319257}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=D216 {ECO:0000313|EMBL:TPX12942.1,
RC   ECO:0000313|Proteomes:UP000319257};
RA   Varaljay V.A., Lyon W.J., Crouch A.L., Drake C.E., Hollomon J.M.,
RA   Nadeau L.J., Nunn H.S., Stevenson B.S., Bojanowski C.L.,
RA   Crookes-Goodson W.J.;
RT   "Draft genome sequence of the filamentous fungus Phialemoniopsis curvata
RT   isolated from diesel fuel.";
RL   Submitted (JUN-2019) 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:TPX12942.1}.
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DR   EMBL; SKBQ01000038; TPX12942.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A507ASH0; -.
DR   STRING; 1093900.A0A507ASH0; -.
DR   InParanoid; A0A507ASH0; -.
DR   OrthoDB; 313213at2759; -.
DR   Proteomes; UP000319257; 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   NCBIfam; TIGR00724; urea_amlyse_rel; 1.
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; 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   Coiled coil {ECO:0000256|SAM:Coils};
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:UP000319257}.
FT   DOMAIN          2..443
FT                   /note="Biotin carboxylation"
FT                   /evidence="ECO:0000259|PROSITE:PS50979"
FT   DOMAIN          115..314
FT                   /note="ATP-grasp"
FT                   /evidence="ECO:0000259|PROSITE:PS50975"
FT   COILED          1096..1123
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   1207 AA;  131874 MW;  35DE9832D07B7303 CRC64;
     MEIKRLLIAN RGEIAYRILR TAKRLGYFVV AIYTQTDVSS PHVLDADLPC LVKSYVDIDE
     IVAIVRQQAI HLVIPGYGFL SENEAFAAAV VKAGAAFVGP DPEHIAAFGI KHRARDLAEK
     VGVPICPGSG ILNSEDEAVL AATKIGYPVM LKATAGGGGM GLQICENEAE VRSSFTSVVS
     RGSTLFSNPG VFLERYYAVS RHVEVQIFGD GQGRCVVFGE RECSIQRRHQ KVIEESPSPF
     VEMRPALRKR LFEVSELLGQ SIKYRSAGTI EFLVDDATAD FFFLEMNTRL QVEHGITELR
     FDIDLVELML RLAEGTLNIS EYMLLEPRGT AIEARVYAEN PLKNHMPSPG VLQHAYFAEG
     PGVRVDTWVR TGTNVSLAYD PLLAKVMGYG ATREEATTTI VGALRDTKLQ GIVTNLSLLF
     RILTSQDFRD GNTTTGFLTD FDHTPRSMEI LTAGSYTTIQ SWPGRVGVGF GIPEGGPMDP
     LHAQLANCIV GNDRGCELLE ITFTGPKIRF HSRAIVCLTG AGAHGMELDG VPIPMCTSLE
     APAGSVLAVG SLSGGSRAYL AIRGGLPSIP YYLGSKATSP VADIGGLQGR ALVAGDLLEL
     PEAGSFRAFS LPSSLIPEWD PHVIHCLSGP HDSPDIILSE ALPALCESEW TVSHQASRVG
     IRLHGPQPQW ARTTGGEGGS HPSNYLDYPY SIGALNWTGD SAVIFPADAP SLGGFISSHV
     VARAEMFKVA QLRPGDKFRL SPISVDAAMD LRRRQEAFLE TIRKLVASGN STFSAISPLS
     LAVPNSLSCS KSTAILERCE DITIRQAGDS YILVEFHQSL DLDTRCRVQS VLEAIEEAHI
     NGVRLATPIG CSLLIDYEGF EISQMELVLK VKDILVAQFA TQISQSTMLN SRLIKLPMVF
     DDKVNKAAIE RYMATQRKYA SYLPDPVEFI ARSNGLDSKD DVRKKVLNTR ILVVGVGFFN
     GTPIGIPLDP RSRLIVPKFN PSRTFSPEGG LGFGGSFFTC DPIDAPGGYV NFGRTLPGWD
     KYCLNKDFGQ RPWLFNNFDQ LEFYEVTEDE LDKIYARFKA GRFDFDISPA TFDVEAYSRF
     CESVAVETQT FKAKQQLATE REIERENKLL AQWQEDQNGE KDEVQGLDDI DDSLKVQAET
     HASVYKIPAQ KGTKVKAGDV LLVLEAMKME INLLASAEHE GSVIRSIVVG PNDVVKPGDT
     LIVLAQA
//
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