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Database: UniProt
Entry: A0A0N1P2Y7_9EURO
LinkDB: A0A0N1P2Y7_9EURO
Original site: A0A0N1P2Y7_9EURO 
ID   A0A0N1P2Y7_9EURO        Unreviewed;      1097 AA.
AC   A0A0N1P2Y7;
DT   09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT   09-DEC-2015, sequence version 1.
DT   31-JUL-2019, entry version 26.
DE   SubName: Full=Urease {ECO:0000313|EMBL:KPI44652.1};
GN   ORFNames=AB675_8622 {ECO:0000313|EMBL:KPI44652.1};
OS   Phialophora attae.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae;
OC   Phialophora.
OX   NCBI_TaxID=1664694 {ECO:0000313|EMBL:KPI44652.1, ECO:0000313|Proteomes:UP000038010};
RN   [1] {ECO:0000313|EMBL:KPI44652.1, ECO:0000313|Proteomes:UP000038010}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 131958 {ECO:0000313|EMBL:KPI44652.1,
RC   ECO:0000313|Proteomes:UP000038010};
RA   Moreno L.F., Stielow B.J., de Hoog S., Vicente V.A., Weiss V.A.,
RA   de Vries M., Cruz L.M., Souza E.M.;
RT   "Draft genome of the ant-associated black yeast Phialophora attae CBS
RT   131958.";
RL   Submitted (JUN-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}.
CC   -!- CAUTION: The sequence shown here is derived from an
CC       EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is
CC       preliminary data. {ECO:0000313|EMBL:KPI44652.1}.
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DR   EMBL; LFJN01000003; KPI44652.1; -; Genomic_DNA.
DR   RefSeq; XP_018004615.1; XM_018149083.1.
DR   EnsemblFungi; KPI44652; KPI44652; AB675_8622.
DR   GeneID; 28740963; -.
DR   OrthoDB; 183108at2759; -.
DR   Proteomes; UP000038010; Unassembled WGS sequence.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-UniRule.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-UniRule.
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   CDD; cd00390; Urease_gamma; 1.
DR   Gene3D; 1.10.30.10; -; 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   InterPro; IPR006680; Amidohydro-rel.
DR   InterPro; IPR009071; HMG_box_dom.
DR   InterPro; IPR036910; HMG_box_dom_sf.
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; PF00505; HMG_box; 1.
DR   Pfam; PF00449; Urease_alpha; 1.
DR   Pfam; PF00699; Urease_beta; 1.
DR   Pfam; PF00547; Urease_gamma; 1.
DR   PRINTS; PR01752; UREASE.
DR   SMART; SM00398; HMG; 1.
DR   SUPFAM; SSF47095; SSF47095; 1.
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   TIGRFAMs; TIGR00193; urease_gam; 1.
DR   PROSITE; PS50118; HMG_BOX_2; 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:UP000038010};
KW   DNA-binding {ECO:0000256|PROSITE-ProRule:PRU00267,
KW   ECO:0000256|SAAS:SAAS00879239};
KW   Hydrolase {ECO:0000256|PROSITE-ProRule:PRU00700};
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR611612-51};
KW   Nickel {ECO:0000256|PIRSR:PIRSR611612-51};
KW   Nucleus {ECO:0000256|PROSITE-ProRule:PRU00267};
KW   Reference proteome {ECO:0000313|Proteomes:UP000038010}.
FT   DOMAIN      113    182       HMG box. {ECO:0000259|PROSITE:PS50118}.
FT   DOMAIN      677   1097       Urease. {ECO:0000259|PROSITE:PS51368}.
FT   DNA_BIND    113    182       HMG box. {ECO:0000256|PROSITE-ProRule:
FT                                PRU00267}.
FT   REGION       85    115       Disordered. {ECO:0000256|SAM:MobiDB-
FT                                lite}.
FT   REGION      135    157       Disordered. {ECO:0000256|SAM:MobiDB-
FT                                lite}.
FT   REGION      184    203       Disordered. {ECO:0000256|SAM:MobiDB-
FT                                lite}.
FT   REGION      209    286       Disordered. {ECO:0000256|SAM:MobiDB-
FT                                lite}.
FT   COMPBIAS    218    243       Polyampholyte. {ECO:0000256|SAM:MobiDB-
FT                                lite}.
FT   COMPBIAS    250    264       Polyampholyte. {ECO:0000256|SAM:MobiDB-
FT                                lite}.
FT   ACT_SITE    850    850       Proton donor. {ECO:0000256|PIRSR:
FT                                PIRSR611612-52, ECO:0000256|PROSITE-
FT                                ProRule:PRU00700}.
FT   METAL       682    682       Nickel 1; via tele nitrogen.
FT                                {ECO:0000256|PIRSR:PIRSR611612-51}.
FT   METAL       684    684       Nickel 1; via tele nitrogen.
FT                                {ECO:0000256|PIRSR:PIRSR611612-51}.
FT   METAL       747    747       Nickel 1; via carbamate group.
FT                                {ECO:0000256|PIRSR:PIRSR611612-51}.
FT   METAL       747    747       Nickel 2; via carbamate group.
FT                                {ECO:0000256|PIRSR:PIRSR611612-51}.
FT   METAL       776    776       Nickel 2; via pros nitrogen.
FT                                {ECO:0000256|PIRSR:PIRSR611612-51}.
FT   METAL       802    802       Nickel 2; via tele nitrogen.
FT                                {ECO:0000256|PIRSR:PIRSR611612-51}.
FT   METAL       890    890       Nickel 1. {ECO:0000256|PIRSR:PIRSR611612-
FT                                51}.
FT   BINDING     749    749       Substrate. {ECO:0000256|PROSITE-ProRule:
FT                                PRU00700}.
FT   MOD_RES     747    747       N6-carboxylysine. {ECO:0000256|PIRSR:
FT                                PIRSR611612-50}.
SQ   SEQUENCE   1097 AA;  117767 MW;  E57DD2B93BA027CF CRC64;
     MAKKAAASAP AAADESGTVD VNVADFKRTR DSVIVALATL QTSVQDLSRA YIQHANTVLA
     PGSGGTLDAN LTNILTESGL LATGSTAAPP AGAAVEEGGK KKRKRTPHDP NAPKRALTPY
     FLYMQSARAQ IAKELGSEAK PKEVADEGTR RWQEMPQTDK GIWDEQYQKN LAAYRVKMAA
     YKAGQKVPSD EEAASLVEAG KAPEPAAIED AAAETEEEDS PEPVKAPEPA PKASKRRKTT
     DTPAKAEAAA PKSPEKEKKG KGKKLPPPPL LHQSPRSSHA TRSTRDKLVT SQLGFLAQRR
     LARGVRLNHV EACALIANNL QELIRDGNHS VAELMSIGKT MLGRRHVLPS VISTLTELQV
     EGTFTTGTYL VTVHHPVASD DGDLEKALYG SFLPVPSKDA FPPFEAHEYE EKKMPGAVIV
     KKGPNIQLNE GRKRIQLKVT SKGDRPIQIG SHYHFIETNP LLSFDRIAAY GYRLDIAAGT
     SVRFEPGDTK TVTLVEIAGH KVIRGGNGLA DGPVDLSRAD EILQKLQAAG FAHESSPQTD
     SSRLSTFNMT RADYAGMFGP TTGDLVRLAA TDLWVRVEKD LTVYGEECKF GGGKTLREGM
     GQASNRPDAE VLDTVITNAL IIDWTGIYKA DIGIKNQLIA GIGKAGNPDV MPGVSPNMIV
     GNGTDVIAGE HMIVTAGGFD THIHLICPQQ AYESIAAGIT TYLAGGTGPS QAPTPQPALP
     VNSTCKGNDS GPIPLRESIE AGACGLKLHE DWGTHPAAID ACLSVCDEYD VQCMIHTDTL
     NESGFVESTV AAFKDRTIHT YHTEGAGGGH APDIIKVVEL PNVLPSSTNP TRPYTNNTLD
     EHLDMLMVCH HLSRNIPEDV AFAESRIRAE TIAAEDVLHD LGAISMMSSD SQAMGRCGEV
     ILRTWHTAHK NKVQRGPLPE DKEDGEADNF RVKRYVSKYT INPALAQGMG HLIGSVEVGK
     YADLVVWKPA SFGVKPNLVV KGGMISWSMM GDPNASIPTI QPVLSRPMFG ALTPASTSIT
     WTSAAAVKAD LPSKLGLKKR IEAVKGCRKV SKKDMKFNDS MPKMKVDPER YVVEADGVRV
     GEGPSESLPL SQAYFAF
//
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