ID A0A0D2XB04_FUSO4 Unreviewed; 779 AA. AC A0A0D2XB04; DT 29-APR-2015, integrated into UniProtKB/TrEMBL. DT 29-APR-2015, sequence version 1. DT 23-MAY-2018, entry version 24. DE SubName: Full=Urease {ECO:0000313|EMBL:KNA95550.1}; GN ORFNames=FOXG_01071 {ECO:0000313|EMBL:KNA95550.1}; OS Fusarium oxysporum f. sp. lycopersici (strain 4287 / CBS 123668 / FGSC OS 9935 / NRRL 34936) (Fusarium vascular wilt of tomato). OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; OC Sordariomycetes; Hypocreomycetidae; Hypocreales; Nectriaceae; OC Fusarium; Fusarium oxysporum species complex. OX NCBI_TaxID=426428 {ECO:0000313|EnsemblFungi:FOXG_01071P0, ECO:0000313|Proteomes:UP000009097}; RN [1] {ECO:0000313|EMBL:KNA95550.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=4287 {ECO:0000313|EMBL:KNA95550.1}; RG The Broad Institute Genome Sequencing Platform; RA Birren B., Lander E., Galagan J., Nusbaum C., Devon K., Ma L.-J., RA Jaffe D., Butler J., Alvarez P., Gnerre S., Grabherr M., Kleber M., RA Mauceli E., Brockman W., MacCallum I.A., Young S., LaButti K., RA DeCaprio D., Crawford M., Koehrsen M., Engels R., Montgomery P., RA Pearson M., Howarth C., Larson L., White J., O'Leary S., Kodira C., RA Zeng Q., Yandava C., Alvarado L., Kistler C., Shim W.-B., Kang S., RA Woloshuk C.; RL Submitted (APR-2007) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:KNA95550.1, ECO:0000313|EnsemblFungi:FOXG_01071P0, ECO:0000313|Proteomes:UP000009097} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=4287 {ECO:0000313|EMBL:KNA95550.1}, and 4287 / CBS 123668 / RC FGSC 9935 / NRRL 34936 {ECO:0000313|EnsemblFungi:FOXG_01071P0, RC ECO:0000313|Proteomes:UP000009097}; RX PubMed=20237561; DOI=10.1038/nature08850; RA Ma L.-J., van der Does H.C., Borkovich K.A., Coleman J.J., RA Daboussi M.-J., Di Pietro A., Dufresne M., Freitag M., Grabherr M., RA Henrissat B., Houterman P.M., Kang S., Shim W.-B., Woloshuk C., RA Xie X., Xu J.-R., Antoniw J., Baker S.E., Bluhm B.H., Breakspear A., RA Brown D.W., Butchko R.A.E., Chapman S., Coulson R., Coutinho P.M., RA Danchin E.G.J., Diener A., Gale L.R., Gardiner D.M., Goff S., RA Hammond-Kosack K.E., Hilburn K., Hua-Van A., Jonkers W., Kazan K., RA Kodira C.D., Koehrsen M., Kumar L., Lee Y.-H., Li L., Manners J.M., RA Miranda-Saavedra D., Mukherjee M., Park G., Park J., Park S.-Y., RA Proctor R.H., Regev A., Ruiz-Roldan M.C., Sain D., Sakthikumar S., RA Sykes S., Schwartz D.C., Turgeon B.G., Wapinski I., Yoder O., RA Young S., Zeng Q., Zhou S., Galagan J., Cuomo C.A., Kistler H.C., RA Rep M.; RT "Comparative genomics reveals mobile pathogenicity chromosomes in RT Fusarium."; RL Nature 464:367-373(2010). RN [3] {ECO:0000313|EnsemblFungi:FOXG_01071P0} RP IDENTIFICATION. RC STRAIN=4287 / CBS 123668 / FGSC 9935 / NRRL 34936 RC {ECO:0000313|EnsemblFungi:FOXG_01071P0}; RG EnsemblFungi; RL Submitted (MAR-2015) to UniProtKB. 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 --------------------------------------------------------------------------- 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; DS231696; KNA95550.1; -; Genomic_DNA. DR EMBL; DS231696; KNA95551.1; -; Genomic_DNA. DR EMBL; DS231696; KNA95552.1; -; Genomic_DNA. DR RefSeq; XP_018233596.1; XM_018377804.1. DR RefSeq; XP_018233597.1; XM_018377805.1. DR RefSeq; XP_018233598.1; XM_018377806.1. DR EnsemblFungi; FOXG_01071T0; FOXG_01071P0; FOXG_01071. DR GeneID; 28943345; -. DR OMA; GFDSHIH; -. DR Proteomes; UP000009097; Chromosome 1. 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; -; 2. 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 PANTHER; PTHR43440; PTHR43440; 1. 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 ProDom; PD002319; Urease_gamma_reg; 1. DR SUPFAM; SSF51278; SSF51278; 1. DR SUPFAM; SSF51338; SSF51338; 1. DR SUPFAM; SSF51556; SSF51556; 2. 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:UP000009097}; 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:UP000009097}. 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; 83745 MW; C0930F6874728716 CRC64; MALGATMLGR RHVLPSVCTT LHEIQVEGTF PSGTYLVTVH NPISSDDGDL RRALYGSFLP VPDNSIFPMA ATEDYQLDKQ PGAVVPVKTK KITLNEGRKR IRLQVTSTGD RPIQVGSHYH FIETNPQLEF DRIRAYGYRL DIPAGTSVRF EPGDTKTVTL VEIGGNRVIR GGNNLASGVV DLSRADEILA RLQEAGYAHK PDPAGDMAHI DVFQMDHASY ATMFGPTTGD LVRLGSTDLW IKVERDETVY GDECKFGGGK TLREGMGQAT GRHDADTLDL VVTNALIVDW TGIYKADIGV KEGMIVGIGK AGNPDVMDGV TEGMVVGSCT DVVAGEGKIV TAGAIDTHIH FICPQQVPEA LASGVTTMLG GGTGPSAGTN ATTCTPGAHY MRQMLQACDQ LPINIGITGK GNDSSPEGLR DQVNAGACGL KLHEDWGCTP AAIDACLSVC DEFDIQCLIH TDTLNESGFV ESTIAAFKNR TIHTYHTEGA GGGHAPDIIS VVEHQNVLPS STNPTRPFTR NTLDEHLDML MVCHHLSKNI PEDVAFAESR IRAETIAAED VLHDKGAISM MSSDSQAMGR CGEVVLRTWN TAHKNKVQRG WLPEDEGTGA DNARVKRYVS KYTINPAIAQ GFGHVIGSIE VGKFADLVLW DPAWFGTKPS HVLKGGHIAY AQMGDPNASI PTVQPIIARP MFSPHCASTS ILFVSSASIE TGAIASYGLR SRVEAVKGCR NIGKSDMRHN DLKPKMRVDP ESYTVEADGE VCVAAPAETL PLTQQFYVY //