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Database: UniProt
Entry: A0A0K3CR89_RHOTO
LinkDB: A0A0K3CR89_RHOTO
Original site: A0A0K3CR89_RHOTO 
ID   A0A0K3CR89_RHOTO        Unreviewed;       869 AA.
AC   A0A0K3CR89;
DT   11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT   11-NOV-2015, sequence version 1.
DT   31-JUL-2019, entry version 19.
DE   SubName: Full=BY PROTMAP: gi|472581199|gb|EMS18948.1| urease [Rhodosporidium toruloides NP11] gi|647402845|emb|CDR49047.1| RHTO0S22e01992g1_1 [Rhodosporidium toruloides] {ECO:0000313|EMBL:CTR10990.1};
GN   Name=FGENESH: predicted gene_15.132 {ECO:0000313|EMBL:CTR10990.1};
GN   ORFNames=BN2166_0068510 {ECO:0000313|EMBL:CTR10990.1};
OS   Rhodosporidium toruloides (Yeast) (Rhodotorula gracilis).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Pucciniomycotina;
OC   Microbotryomycetes; Sporidiobolales; Sporidiobolaceae; Rhodotorula.
OX   NCBI_TaxID=5286 {ECO:0000313|EMBL:CTR10990.1, ECO:0000313|Proteomes:UP000199069};
RN   [1] {ECO:0000313|EMBL:CTR10990.1, ECO:0000313|Proteomes:UP000199069}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Single colony {ECO:0000313|EMBL:CTR10990.1};
RA   Cajimat M.N.B., Milazzo M.L., Fulhorst C.F.;
RL   Submitted (JUL-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=Ni cation; Xref=ChEBI:CHEBI:25516;
CC         Evidence={ECO:0000256|PIRSR:PIRSR001222-51};
CC       Note=Binds 2 nickel ions per subunit.
CC       {ECO:0000256|PIRSR:PIRSR001222-51};
CC   -!- PTM: Carbamylation allows a single lysine to coordinate two nickel
CC       ions. {ECO:0000256|PIRSR:PIRSR001222-50}.
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DR   EMBL; CWKI01000015; CTR10990.1; -; Genomic_DNA.
DR   EnsemblFungi; CTR10990; CTR10990; BN2166_0068510.
DR   Proteomes; UP000199069; 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   CDD; cd00390; Urease_gamma; 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; IPR008221; Urease.
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   PIRSF; PIRSF001222; Urease; 1.
DR   PRINTS; PR01752; UREASE.
DR   SUPFAM; SSF51278; SSF51278; 1.
DR   SUPFAM; SSF51338; SSF51338; 2.
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; 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:UP000199069};
KW   Hydrolase {ECO:0000256|PROSITE-ProRule:PRU00700};
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR001222-51};
KW   Nickel {ECO:0000256|PIRSR:PIRSR001222-51};
KW   Reference proteome {ECO:0000313|Proteomes:UP000199069}.
FT   DOMAIN      415    869       Urease. {ECO:0000259|PROSITE:PS51368}.
FT   REGION      674    693       Disordered. {ECO:0000256|SAM:MobiDB-
FT                                lite}.
FT   ACT_SITE    602    602       Proton donor. {ECO:0000256|PIRSR:
FT                                PIRSR611612-52, ECO:0000256|PROSITE-
FT                                ProRule:PRU00700}.
FT   METAL       420    420       Nickel 1; via tele nitrogen.
FT                                {ECO:0000256|PIRSR:PIRSR001222-51}.
FT   METAL       422    422       Nickel 1; via tele nitrogen.
FT                                {ECO:0000256|PIRSR:PIRSR001222-51}.
FT   METAL       503    503       Nickel 1; via carbamate group.
FT                                {ECO:0000256|PIRSR:PIRSR001222-51}.
FT   METAL       503    503       Nickel 2; via carbamate group.
FT                                {ECO:0000256|PIRSR:PIRSR001222-51}.
FT   METAL       532    532       Nickel 2; via pros nitrogen.
FT                                {ECO:0000256|PIRSR:PIRSR001222-51}.
FT   METAL       558    558       Nickel 2; via tele nitrogen.
FT                                {ECO:0000256|PIRSR:PIRSR001222-51}.
FT   METAL       642    642       Nickel 1. {ECO:0000256|PIRSR:PIRSR001222-
FT                                51}.
FT   BINDING     505    505       Substrate. {ECO:0000256|PROSITE-ProRule:
FT                                PRU00700}.
FT   MOD_RES     503    503       N6-carboxylysine. {ECO:0000256|PIRSR:
FT                                PIRSR001222-50}.
SQ   SEQUENCE   869 AA;  93080 MW;  450C3E4A4E9C0F81 CRC64;
     MGFDLLPREI DKLQLISLAG QLAQKRLARG CRLNVTEATA LIAHVLQELI RDGDHSVAEL
     MSIGKKILGR VHVQPAVPSL LHEIQVEGAF PDGVFLVTVH DPISSASVND DLSLALYGSF
     LPLPKEGVFP KGSDEPAGPA DEEIPGALVL RKEPIRINEG RERVRLKVTN TGDRPIQVGS
     HYHFTEVNRA LSFDRRKAFF KRLDIAAGTA VRFEPGDTKT VTLVQIGGEQ VVTGGNLLLN
     SSVARHLADP SLADSSMQRI ISSGFSHVDD PSAVLTSDTS LIVPFEVSRE TYASMFGPTT
     GDRVRLGDTS LWVEVERDET HYGDECKFGG GKVIREGMGQ ATGLPDAETL DLIITNALII
     NWDGIYKADI GVKTGHIVGI GKGGNPDVMN NITPGMVVGV NTDVIAGEKL IVTAGAIDAH
     VHYICPQLCN EALASGITTL LGGGTGPSAG SNATTCTPSR TYMHTMMAAT DGIPLNFAFT
     GKANDSGEAG LEDQVRNGAV GLKLHEDWGS TPAAIDSALS LAEKYDVQVN IHSDTLNESG
     FVQDTIDAFK GRTIHAYHIG GHAPDCCRMI SLSNVIPSST NPTRPFAPNT LDEHLDMLMV
     CHHLDRSIPE DIAFAESRIR AETIAAEDVL HDSGAISIIS SDSQAMGRIG EVVSRTWRTA
     SKMKDVVGTL KEETRDGADN ERVKARSPSL PHLLPRSSRE VSQRYIAKYT INPAIVHGMS
     HVIGDVSVGK LADLVLWQPA YFGVRPNMVV KGGVIAWANM GDANASIPTV QPVIGRPMWG
     SQPSAAALTS LLFVSSLSLS SGTIASYGLK KRPVAVKGCR KVRKEDMKNN SALPKIEVDP
     ESYKVTADGV HCTVPPATKV PLAQSYMLF
//
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