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Database: UniProt
Entry: A0A0D2ASY0_9EURO
LinkDB: A0A0D2ASY0_9EURO
Original site: A0A0D2ASY0_9EURO 
ID   A0A0D2ASY0_9EURO        Unreviewed;       779 AA.
AC   A0A0D2ASY0;
DT   29-APR-2015, integrated into UniProtKB/TrEMBL.
DT   29-APR-2015, sequence version 1.
DT   18-SEP-2019, entry version 24.
DE   SubName: Full=Urease, variant {ECO:0000313|EMBL:KIW28277.1};
GN   ORFNames=PV07_07954 {ECO:0000313|EMBL:KIW28277.1};
OS   Cladophialophora immunda.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae;
OC   Cladophialophora.
OX   NCBI_TaxID=569365 {ECO:0000313|EMBL:KIW28277.1, ECO:0000313|Proteomes:UP000054466};
RN   [1] {ECO:0000313|EMBL:KIW28277.1, ECO:0000313|Proteomes:UP000054466}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 83496 {ECO:0000313|EMBL:KIW28277.1,
RC   ECO:0000313|Proteomes:UP000054466};
RG   The Broad Institute Genomics Platform;
RA   Cuomo C., de Hoog S., Gorbushina A., Stielow B., Teixiera M.,
RA   Abouelleil A., Chapman S.B., Priest M., Young S.K., Wortman J.,
RA   Nusbaum C., Birren B.;
RT   "The Genome Sequence of Cladophialophora immunda CBS83496.";
RL   Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=Ni cation; Xref=ChEBI:CHEBI:25516;
CC         Evidence={ECO:0000256|PIRSR:PIRSR611612-51};
CC       Note=Binds 2 nickel ions per subunit.
CC       {ECO:0000256|PIRSR:PIRSR611612-51};
CC   -!- PTM: Carbamylation allows a single lysine to coordinate two nickel
CC       ions. {ECO:0000256|PIRSR:PIRSR611612-50}.
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DR   EMBL; KN847043; KIW28277.1; -; Genomic_DNA.
DR   RefSeq; XP_016248493.1; XM_016395074.1.
DR   EnsemblFungi; KIW28277; KIW28277; PV07_07954.
DR   GeneID; 27347148; -.
DR   EuPathDB; FungiDB:PV07_07954; -.
DR   OrthoDB; 183108at2759; -.
DR   Proteomes; UP000054466; Unassembled WGS sequence.
DR   GO; GO:0016151; F:nickel cation binding; IEA:InterPro.
DR   GO; GO:0009039; F:urease activity; IEA:InterPro.
DR   GO; GO:0043419; P:urea catabolic process; IEA:InterPro.
DR   CDD; cd00375; Urease_alpha; 1.
DR   CDD; cd00407; Urease_beta; 1.
DR   Gene3D; 2.10.150.10; -; 1.
DR   Gene3D; 2.30.40.10; -; 1.
DR   Gene3D; 3.30.280.10; -; 1.
DR   HAMAP; MF_01953; Urease_alpha; 1.
DR   HAMAP; MF_01954; Urease_beta; 1.
DR   InterPro; IPR006680; Amidohydro-rel.
DR   InterPro; IPR011059; Metal-dep_hydrolase_composite.
DR   InterPro; IPR032466; Metal_Hydrolase.
DR   InterPro; IPR011612; Urease_alpha_N_dom.
DR   InterPro; IPR017950; Urease_AS.
DR   InterPro; IPR005848; Urease_asu.
DR   InterPro; IPR017951; Urease_asu_c.
DR   InterPro; IPR002019; Urease_beta.
DR   InterPro; IPR036461; Urease_betasu_sf.
DR   InterPro; IPR002026; Urease_gamma/gamma-beta_su.
DR   InterPro; IPR036463; Urease_gamma_sf.
DR   InterPro; IPR029754; Urease_Ni-bd.
DR   Pfam; PF01979; Amidohydro_1; 1.
DR   Pfam; PF00449; Urease_alpha; 1.
DR   Pfam; PF00699; Urease_beta; 1.
DR   Pfam; PF00547; Urease_gamma; 1.
DR   PRINTS; PR01752; UREASE.
DR   SUPFAM; SSF51278; SSF51278; 1.
DR   SUPFAM; SSF51338; SSF51338; 1.
DR   SUPFAM; SSF51556; SSF51556; 1.
DR   SUPFAM; SSF54111; SSF54111; 1.
DR   TIGRFAMs; TIGR01792; urease_alph; 1.
DR   TIGRFAMs; TIGR00192; urease_beta; 1.
DR   PROSITE; PS01120; UREASE_1; 1.
DR   PROSITE; PS00145; UREASE_2; 1.
DR   PROSITE; PS51368; UREASE_3; 1.
PE   3: Inferred from homology;
KW   Complete proteome {ECO:0000313|Proteomes:UP000054466};
KW   Hydrolase {ECO:0000256|PROSITE-ProRule:PRU00700};
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR611612-51};
KW   Nickel {ECO:0000256|PIRSR:PIRSR611612-51};
KW   Reference proteome {ECO:0000313|Proteomes:UP000054466}.
FT   DOMAIN      343    779       Urease. {ECO:0000259|PROSITE:PS51368}.
FT   ACT_SITE    534    534       Proton donor. {ECO:0000256|PIRSR:
FT                                PIRSR611612-52, ECO:0000256|PROSITE-
FT                                ProRule:PRU00700}.
FT   METAL       348    348       Nickel 1; via tele nitrogen.
FT                                {ECO:0000256|PIRSR:PIRSR611612-51}.
FT   METAL       350    350       Nickel 1; via tele nitrogen.
FT                                {ECO:0000256|PIRSR:PIRSR611612-51}.
FT   METAL       431    431       Nickel 1; via carbamate group.
FT                                {ECO:0000256|PIRSR:PIRSR611612-51}.
FT   METAL       431    431       Nickel 2; via carbamate group.
FT                                {ECO:0000256|PIRSR:PIRSR611612-51}.
FT   METAL       460    460       Nickel 2; via pros nitrogen.
FT                                {ECO:0000256|PIRSR:PIRSR611612-51}.
FT   METAL       486    486       Nickel 2; via tele nitrogen.
FT                                {ECO:0000256|PIRSR:PIRSR611612-51}.
FT   METAL       574    574       Nickel 1. {ECO:0000256|PIRSR:PIRSR611612-
FT                                51}.
FT   BINDING     433    433       Substrate. {ECO:0000256|PROSITE-ProRule:
FT                                PRU00700}.
FT   MOD_RES     431    431       N6-carboxylysine. {ECO:0000256|PIRSR:
FT                                PIRSR611612-50}.
SQ   SEQUENCE   779 AA;  83892 MW;  9385B863D0D4A97E CRC64;
     MSIGKTMLGR RHVLPSVLST LTELQVEGTF KTGTYLVTVH HPISSDDGDL EKALYGSFLP
     VPSKDAFPLP DQSEYDNKKM PGAVIPVKEG KITLNEGRKR IQLKVTSKGD RPIQIGSHYH
     FIETNPQLEF DRSRAYGFRL DIPAGTSVRF EPGDTKTVNL VEIAGNKVIH GGNNLASGPV
     DISRAEEIVQ KLQQAGFAHA PEPAGDLAHI DVASMTRADY AGMFGPTTGD LVRLGTTDLW
     IKVEKDLTVY GEECKFGGGK TLREGMGQAS DRKDVDVLDT VVTNALIVDW SGIYKADVGI
     KDGIIVGIGK AGNPDVMDGV HPNMIVGNGT DVIAGEHSIL TAGGIDSHIH LICPQQVYES
     VAAGITTYLG GGTGPSTGTN ATTCTPGKWH MKQMLQAIDS LPINYGITGK GNDSSPVALR
     EQCEAGACGL KLHEDWGTTP AAIDTCLSVC DEYDVQCLIH TDTLNESGFV ESSVAAFKGR
     TIHTYHTEGA GGGHAPDIIS VVEHANVLPS STNPTRPFTR NTLDEHLDML MVCHHLSKNI
     PEDVAFAESR IRAETIAAED VLHDLGAISM MSSDSQAMGR CGEVILRTWN TAHKNKQQRG
     TLKEDEGTDA DNFRVKRYVS KYTINPAIAQ GMSHLLGSVE VGKVADLVLW KPSMFGTKPS
     LVVKGGMISH AQMGDPNASI PTVQPVLMRP MFAAHVPSRS ITFVSQHSLA SGVVASYNLA
     KRVEAVKNCR TVGKKDMKFN DVMPKMKVDP ESYRVEADGM HCTAAPAEVV PLAQTYYVY
//
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