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Database: UniProt
Entry: F2STJ3_TRIRC
LinkDB: F2STJ3_TRIRC
Original site: F2STJ3_TRIRC 
ID   F2STJ3_TRIRC            Unreviewed;       854 AA.
AC   F2STJ3;
DT   31-MAY-2011, integrated into UniProtKB/TrEMBL.
DT   29-OCT-2014, sequence version 2.
DT   03-JUL-2019, entry version 49.
DE   RecName: Full=Urease {ECO:0000256|PIRNR:PIRNR001222};
DE            EC=3.5.1.5 {ECO:0000256|PIRNR:PIRNR001222};
DE   AltName: Full=Urea amidohydrolase {ECO:0000256|PIRNR:PIRNR001222};
GN   ORFNames=TERG_05791 {ECO:0000313|EMBL:EGD89553.2};
OS   Trichophyton rubrum (strain ATCC MYA-4607 / CBS 118892) (Athlete's
OS   foot fungus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Onygenales; Arthrodermataceae; Trichophyton.
OX   NCBI_TaxID=559305 {ECO:0000313|EMBL:EGD89553.2, ECO:0000313|Proteomes:UP000008864};
RN   [1] {ECO:0000313|Proteomes:UP000008864}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC MYA-4607 / CBS 118892 {ECO:0000313|Proteomes:UP000008864};
RX   PubMed=22951933; DOI=10.1128/mBio.00259-12;
RA   Martinez D.A., Oliver B.G., Graeser Y., Goldberg J.M., Li W.,
RA   Martinez-Rossi N.M., Monod M., Shelest E., Barton R.C., Birch E.,
RA   Brakhage A.A., Chen Z., Gurr S.J., Heiman D., Heitman J., Kosti I.,
RA   Rossi A., Saif S., Samalova M., Saunders C.W., Shea T.,
RA   Summerbell R.C., Xu J., Young S., Zeng Q., Birren B.W., Cuomo C.A.,
RA   White T.C.;
RT   "Comparative genome analysis of Trichophyton rubrum and related
RT   dermatophytes reveals candidate genes involved in infection.";
RL   MBio 3:E259-E259(2012).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2 H(+) + H2O + urea = CO2 + 2 NH4(+);
CC         Xref=Rhea:RHEA:20557, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:16199, ChEBI:CHEBI:16526, ChEBI:CHEBI:28938;
CC         EC=3.5.1.5; Evidence={ECO:0000256|PIRNR:PIRNR001222};
CC   -!- COFACTOR:
CC       Name=Ni cation; Xref=ChEBI:CHEBI:25516;
CC         Evidence={ECO:0000256|PIRNR:PIRNR001222,
CC         ECO:0000256|PIRSR:PIRSR001222-51};
CC       Note=Binds 2 nickel ions per subunit.
CC       {ECO:0000256|PIRNR:PIRNR001222, ECO:0000256|PIRSR:PIRSR001222-51};
CC   -!- PATHWAY: Nitrogen metabolism; urea degradation; CO(2) and NH(3)
CC       from urea (urease route): step 1/1.
CC       {ECO:0000256|PIRNR:PIRNR001222}.
CC   -!- PTM: Carbamylation allows a single lysine to coordinate two nickel
CC       ions. {ECO:0000256|PIRSR:PIRSR001222-50}.
CC   -!- SIMILARITY: In the C-terminal section; belongs to the metallo-
CC       dependent hydrolases superfamily. Urease alpha subunit family.
CC       {ECO:0000256|PIRNR:PIRNR001222}.
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DR   EMBL; GG700653; EGD89553.2; -; Genomic_DNA.
DR   STRING; 5551.XP_003233922.1; -.
DR   EnsemblFungi; EGD89553; EGD89553; TERG_05791.
DR   InParanoid; F2STJ3; -.
DR   UniPathway; UPA00258; UER00370.
DR   Proteomes; UP000008864; Unassembled WGS sequence.
DR   GO; GO:0016151; F:nickel cation binding; IEA:InterPro.
DR   GO; GO:0009039; F:urease activity; IEA:UniProtKB-EC.
DR   GO; GO:0043419; P:urea catabolic process; IEA:UniProtKB-UniPathway.
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   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; 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; 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:UP000008864};
KW   Hydrolase {ECO:0000256|PIRNR:PIRNR001222, ECO:0000256|PROSITE-
KW   ProRule:PRU00700};
KW   Metal-binding {ECO:0000256|PIRNR:PIRNR001222,
KW   ECO:0000256|PIRSR:PIRSR001222-51};
KW   Nickel {ECO:0000256|PIRNR:PIRNR001222, ECO:0000256|PIRSR:PIRSR001222-
KW   51}; Reference proteome {ECO:0000313|Proteomes:UP000008864}.
FT   DOMAIN      400    854       Urease. {ECO:0000259|PROSITE:PS51368}.
FT   ACT_SITE    591    591       Proton donor. {ECO:0000256|PIRSR:
FT                                PIRSR611612-52, ECO:0000256|PROSITE-
FT                                ProRule:PRU00700}.
FT   METAL       405    405       Nickel 1; via tele nitrogen.
FT                                {ECO:0000256|PIRSR:PIRSR001222-51}.
FT   METAL       407    407       Nickel 1; via tele nitrogen.
FT                                {ECO:0000256|PIRSR:PIRSR001222-51}.
FT   METAL       488    488       Nickel 1; via carbamate group.
FT                                {ECO:0000256|PIRSR:PIRSR001222-51}.
FT   METAL       488    488       Nickel 2; via carbamate group.
FT                                {ECO:0000256|PIRSR:PIRSR001222-51}.
FT   METAL       517    517       Nickel 2; via pros nitrogen.
FT                                {ECO:0000256|PIRSR:PIRSR001222-51}.
FT   METAL       543    543       Nickel 2; via tele nitrogen.
FT                                {ECO:0000256|PIRSR:PIRSR001222-51}.
FT   METAL       631    631       Nickel 1. {ECO:0000256|PIRSR:PIRSR001222-
FT                                51}.
FT   BINDING     490    490       Substrate. {ECO:0000256|PROSITE-ProRule:
FT                                PRU00700}.
FT   MOD_RES     488    488       N6-carboxylysine. {ECO:0000256|PIRSR:
FT                                PIRSR001222-50}.
SQ   SEQUENCE   854 AA;  92857 MW;  E8FDFE9CC84B1E8A CRC64;
     MRLVPRELDK LTISQLGFLA QRRLARGVRL NHAEATALIS SNLHELIRDG NHTVADLMAI
     GKSMLGRRHV LPSVVSSLTQ LQVEGTFVCG SYLVTVHNPI CSDDGDLEKA LYGSFLPVPP
     EDLFPDPDPE EYLPERMPGA VVVVKESKIE LSPGRRRIKL RVTSKGDRPI QVGSHYHFIE
     TNPQLEFDRA QAYGFRLDIP AGASHRFEPG ESKTVQLVEI AGHKVIKGGN FLATGEINHG
     RKDRILSRIA QAGFMHTPEP TADASLIKPY TMTREAYART FGPTTGDLIK LAATDLWVKV
     EKDLTSYGDE CTFGGGKSLR EGMGQATGRH AHEVLDSCVT NAVILDWSGI YKADIGIKDG
     IIVGIGKAGN PDVMDGITPG MVIGSSTDII AAERMIVTAG GIDTHVHFIC PQQVDEALSS
     GITTMLGGGT GPSEGSNATT CTPSPNSIRQ MIQSSDGFPM NFAFTGKGND SEPRGLRDQI
     RAGAAGLKIH EDWGATPAAI DSCLSVCDEL DVQCLIHTDT LNESGFVEQT IKALKGRVIH
     TYHTEGAGGG HAPDIISVCE HPNVLPSSTN PSRPYTLNTL DEHLDMVMVC HHLSKDIPED
     VAFAESRIRA ETIAAEDVLH DIGAISMMSS DSQAMGRCGE VVLRTWHTAH KNKLQRGVLP
     EDEGTGCDNF RAKRYVSKYT INPAIAQGMS HVIGSVEVGK VADLVLWKFA EFGVKPNLTL
     KSGMIARAQM VFYLPLSLRS SHHLTILQGD ANGSIPTIEP ILSRPMWASC LPNTSIIFVS
     QSSVDDGVID TYDIKKRVEP VKNCRNIGKE DMKFNDTRPK MHVDPESYTV EADGMVCDAD
     PIDILPLCQD YFIY
//
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