ID W4JS26_HETIT Unreviewed; 1322 AA.
AC W4JS26;
DT 19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT 19-MAR-2014, sequence version 1.
DT 24-JAN-2024, entry version 53.
DE RecName: Full=Urea carboxylase {ECO:0008006|Google:ProtNLM};
GN ORFNames=HETIRDRAFT_480433 {ECO:0000313|EMBL:ETW76338.1};
OS Heterobasidion irregulare (strain TC 32-1).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Russulales; Bondarzewiaceae; Heterobasidion;
OC Heterobasidion annosum species complex.
OX NCBI_TaxID=747525 {ECO:0000313|EMBL:ETW76338.1, ECO:0000313|Proteomes:UP000030671};
RN [1] {ECO:0000313|EMBL:ETW76338.1, ECO:0000313|Proteomes:UP000030671}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TC 32-1 {ECO:0000313|EMBL:ETW76338.1,
RC ECO:0000313|Proteomes:UP000030671};
RX PubMed=22463738; DOI=10.1111/j.1469-8137.2012.04128.x;
RA Olson A., Aerts A., Asiegbu F., Belbahri L., Bouzid O., Broberg A.,
RA Canback B., Coutinho P.M., Cullen D., Dalman K., Deflorio G.,
RA van Diepen L.T., Dunand C., Duplessis S., Durling M., Gonthier P.,
RA Grimwood J., Fossdal C.G., Hansson D., Henrissat B., Hietala A.,
RA Himmelstrand K., Hoffmeister D., Hogberg N., James T.Y., Karlsson M.,
RA Kohler A., Kues U., Lee Y.H., Lin Y.C., Lind M., Lindquist E., Lombard V.,
RA Lucas S., Lunden K., Morin E., Murat C., Park J., Raffaello T., Rouze P.,
RA Salamov A., Schmutz J., Solheim H., Stahlberg J., Velez H., de Vries R.P.,
RA Wiebenga A., Woodward S., Yakovlev I., Garbelotto M., Martin F.,
RA Grigoriev I.V., Stenlid J.;
RT "Insight into trade-off between wood decay and parasitism from the genome
RT of a fungal forest pathogen.";
RL New Phytol. 194:1001-1013(2012).
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; KI925464; ETW76338.1; -; Genomic_DNA.
DR RefSeq; XP_009551260.1; XM_009552965.1.
DR STRING; 747525.W4JS26; -.
DR GeneID; 20677913; -.
DR KEGG; hir:HETIRDRAFT_480433; -.
DR eggNOG; KOG0238; Eukaryota.
DR HOGENOM; CLU_002162_0_1_1; -.
DR InParanoid; W4JS26; -.
DR OrthoDB; 313213at2759; -.
DR Proteomes; UP000030671; 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; 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:UP000030671}.
FT DOMAIN 18..529
FT /note="Biotin carboxylation"
FT /evidence="ECO:0000259|PROSITE:PS50979"
FT DOMAIN 164..369
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT REGION 783..807
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1322 AA; 143307 MW; 4B8CCD71B7579C3B CRC64;
MPWPNTQPQT ATPKVKPPGH TLLVANRGEI AVRIIRTARA VTMDGAGAIS TISLYTPSDA
HALHVSLADI AVPLSLPLPS FNAEPNTSQY ESAAYLDPRA LLTLAAEHSA TLLHPGYGLL
SESAHFAELC RTAGVTFLGP SPEAMRELGG KDAARRVAGR VGVRVLEGSG MIPLREEDSE
RERESAVEEA RRIGWPVVVK PVLGGGGRGI VVCNDEEQVR RAVKEASRSA GGRMGDEEEE
EDGGVIIECY VDRARHVEVQ VFGNSAGHVV PLGVRECSVQ RRHQKVLEEA PGAFLAVHPE
VVREICASAI KLCESVNYGS AGTCEFLVDC DTCEVFFLEM NTRIQVEHPV TEYAHPGVPQ
LDIVRLMIEQ GIAEREGRGG LDPAYLDGFA FHLPDFNSGS DGSLTCTVHA IEARVCAENP
AAGFVPSAGV MQRVVFGPKE AMKGDEAWLR VDTWATPGTA ISPHFDSLLA KLIVRAPTRA
QAVERMLRAL DATQIYGPPT NVQFLRAVVS SEAFRRGEVT TKFLDDFNHN SRSVHVLAPG
LSTTVQSLPH RTVGHGIPQS GPFDTLSMRI ASLLVNNTDP VPRDGVSTNA ACDVLEITLA
GPTLLFRAPA VLALTGARAL LLVNGESRPM WARVAVRSGA RVSVGRLESV GESVGCRAYL
AVRGGFPEVA AYLGSKATSV GMGGYQGRAL VVGDELALRA CDIRHDELDA GPLVLPASLR
PPYPSPQTDS PNATWILHVL LGPHSDAEFL TSRGLHTFFA SSWTVQPSSS RSGIRLSRYH
TRGFSENPPA PPSGPAIQWA RTGGSEGGAH PSNVLDCAYA RGSVNLNGDT PVILGVEGPD
MGGFVCVCVV VTADLWKLGQ LRPGCLLRFE PISVDRAVQM MEHTEHMVDT VRKFVRTGTV
VAHPEPADLE TSDDLQDPRL HVVEENPGNQ RPQVVFRQAG DSAVLVEYGS MHLDFGIRAR
IHAFEVEVRR RKIPGITSLA PCIRSIMCYY DPRSVSQSSL LAHLIAAEHA LPDSTSDMHF
RSRKFEFPIV IDDRWNRDAL ERYMRSVRSK AVYLPSNIEY LARNNGLKGG AEEALRLLVV
FGVGFYLGCP FLVPADPRCR LVGQKMNPSR TFTPRGAVGI AGLVAAIYPT ESPGGYQLFG
RTLPAWQTWG RGENFTPEKP WLLNSFDQIT FKPVMEDEYL ELEKQFDAGL YKFKVEETVF
SMAEYETFVS SVADEEARFK ARQAEGVRRE SERFAHELTA ASDTNTGITI TAPLAARMWK
IRCKLGDVID SAEVVVVVLE AMKTEVSIVA GEEAVGRTVK GFGTAAREGT SVSAGDVLII
LE
//
