ID A0A178ZJD6_9EURO Unreviewed; 1241 AA.
AC A0A178ZJD6;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 22-FEB-2023, entry version 22.
DE SubName: Full=Urea carboxylase {ECO:0000313|EMBL:OAP59303.1};
GN ORFNames=AYL99_06601 {ECO:0000313|EMBL:OAP59303.1};
OS Fonsecaea erecta.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae; Fonsecaea.
OX NCBI_TaxID=1367422 {ECO:0000313|EMBL:OAP59303.1, ECO:0000313|Proteomes:UP000078343};
RN [1] {ECO:0000313|EMBL:OAP59303.1, ECO:0000313|Proteomes:UP000078343}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 125763 {ECO:0000313|EMBL:OAP59303.1,
RC ECO:0000313|Proteomes:UP000078343};
RA Weiss V.A., Vicente V.A., Raittz R.T., Moreno L.F., De Souza E.M.,
RA Pedrosa F.O., Steffens M.B., Faoro H., Tadra-Sfeir M.Z., Najafzadeh M.J.,
RA Felipe M.S., Teixeira M., Sun J., Xi L., Gomes R., De Azevedo C.M.,
RA Salgado C.G., Da Silva M.B., Nascimento M.F., Queiroz-Telles F.,
RA Attili D.S., Gorbushina A.;
RT "Draft genome of Fonsecaea erecta CBS 125763.";
RL Submitted (APR-2016) 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:OAP59303.1}.
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DR EMBL; LVYI01000005; OAP59303.1; -; Genomic_DNA.
DR RefSeq; XP_018692670.1; XM_018838110.1.
DR AlphaFoldDB; A0A178ZJD6; -.
DR STRING; 1367422.A0A178ZJD6; -.
DR GeneID; 30010769; -.
DR OrthoDB; 313213at2759; -.
DR Proteomes; UP000078343; 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; 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; 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 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:UP000078343}.
FT DOMAIN 3..459
FT /note="Biotin carboxylation"
FT /evidence="ECO:0000259|PROSITE:PS50979"
FT DOMAIN 121..321
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT DOMAIN 1157..1237
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
FT COILED 1096..1140
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 1241 AA; 136976 MW; 3CE61F2D49ECBCBA CRC64;
MEKLKTLLVA NRGEIAVRIC KTASNLGIKT ISIYTGADAA SAHVGAADEA VLLSGPDAKG
YIDTQQIIEI AKSKGADAII PGYGFLSENT DFARHVAEAG MVFVGPSPKC IDDFGIKHTA
RELAAKANVP IVPGTKGLVK SEDDAVEEAK KLGFPVMLKA TAGGGGMGLL TCKDENEVRQ
SFKTVQSRGE TLFKNSGVFM ERFYPSSHHI EVQVFGNGLG EAIHFGEREC SIQRRHQKVI
EECPSPFVVK HPELRQKLGS AAVRLADSIN YGSAGTIEFL VDDESGAFFF LEMNTRLQVE
HGITEMCYGI DLVELMLKQA DAELSGKGGL DAEYLRSLQP EGPSGAAIEV RVYAENPAKD
FAPSPGTLQH VSWKQVPGSR IDGWIHTGTK VTSFYDPLLA KLMVHAADRP EALRLMSEML
EGSNIFGPPT NIEFLDAILK DSTFKSGNTM TKFLETFKFQ PSAIDVLQGG AYTLIEDWPG
RPTIGRGFSH SGPMDPLAFR IANALVGNPP GKEGVEITLS GPDLKFLGPA IVAICGAPME
AKLDGKEAPM WTRLKIQAGQ RLTIGKTTGG GCRSYLAIYG GLPSIATWFG SKATAPMTAV
GGYQGRALAA GDFLVVTADL PEISGELRLP ENLIPSYPEE WDLLAMPGPY DEGFITNESI
EEFYKSTWTI SHNAARGGIR LIGPKPKWAR PDGGEGGAHP SNVIEYGYPV GTVNWTGDDP
CLFPIDAPDF GGFVSATTIV KADYWRLGQM KAGNKLRFKR VSYQDAIAKR KEVEDFLGSI
HDCCQGKGSF EHVSPLKYDG FPPSVENKGW EPAMIHQIQE QGNQPLVSYR QGGDDFILID
YGHGSFDLNY RCRAVALYRK LRENTGEISF ANGAMHTGMA CGNSLMLYYD STKVPRQKML
DYLLQLENEL GDLSEAKFPS RKYKFPITFQ SKRQKESLQR YMETQRPYAS YLPDPMEFVA
KNNAFTLQQL RDIYTKSSLM VVAVGFFVAL PIALPIDPRQ RIQCPKMNPS RVHTPEGQVG
WGGSCMALYN VESPGGYMNT GLSIPGADIL GFKKGYSPEK PWLFEDFDQI TFYEVTEDEY
ERMMATFRSG RYEYEYEDTE FDMKEHNQLL RETKDEVVQI RAKQREAQAE MDKLEKELLE
KWNKEKEAGK ISMDTVEELL HDPDIIPVEA PLNANVWKVE VKEGDRVRLE QVVSILEAMK
LEIPVKAEQS MEGATVEKLL VKPNDVVEAG KPLMLLRRPA K
//
