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Database: UniProt
Entry: M7U6Q6_BOTF1
LinkDB: M7U6Q6_BOTF1
Original site: M7U6Q6_BOTF1 
ID   M7U6Q6_BOTF1            Unreviewed;       772 AA.
AC   M7U6Q6;
DT   29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT   29-MAY-2013, sequence version 1.
DT   03-JUL-2019, entry version 30.
DE   SubName: Full=Putative urease protein {ECO:0000313|EMBL:EMR89374.1};
GN   ORFNames=BcDW1_1832 {ECO:0000313|EMBL:EMR89374.1};
OS   Botryotinia fuckeliana (strain BcDW1) (Noble rot fungus) (Botrytis
OS   cinerea).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC   Helotiales; Sclerotiniaceae; Botrytis.
OX   NCBI_TaxID=1290391 {ECO:0000313|EMBL:EMR89374.1, ECO:0000313|Proteomes:UP000012045};
RN   [1] {ECO:0000313|Proteomes:UP000012045}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BcDW1 {ECO:0000313|Proteomes:UP000012045};
RX   PubMed=23704180; DOI=10.1128/genomeA.00252-13;
RA   Blanco-Ulate B., Allen G., Powell A.L., Cantu D.;
RT   "Draft genome sequence of Botrytis cinerea BcDW1, inoculum for noble
RT   rot of grape berries.";
RL   Genome Announc. 1:E0025213-E0025213(2013).
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; KB707748; EMR89374.1; -; Genomic_DNA.
DR   EnsemblFungi; EMR89374; EMR89374; BcDW1_1832.
DR   Proteomes; UP000012045; 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:UP000012045};
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:UP000012045}.
FT   DOMAIN      336    772       Urease. {ECO:0000259|PROSITE:PS51368}.
FT   ACT_SITE    527    527       Proton donor. {ECO:0000256|PIRSR:
FT                                PIRSR611612-52, ECO:0000256|PROSITE-
FT                                ProRule:PRU00700}.
FT   METAL       341    341       Nickel 1; via tele nitrogen.
FT                                {ECO:0000256|PIRSR:PIRSR611612-51}.
FT   METAL       343    343       Nickel 1; via tele nitrogen.
FT                                {ECO:0000256|PIRSR:PIRSR611612-51}.
FT   METAL       424    424       Nickel 1; via carbamate group.
FT                                {ECO:0000256|PIRSR:PIRSR611612-51}.
FT   METAL       424    424       Nickel 2; via carbamate group.
FT                                {ECO:0000256|PIRSR:PIRSR611612-51}.
FT   METAL       453    453       Nickel 2; via pros nitrogen.
FT                                {ECO:0000256|PIRSR:PIRSR611612-51}.
FT   METAL       479    479       Nickel 2; via tele nitrogen.
FT                                {ECO:0000256|PIRSR:PIRSR611612-51}.
FT   METAL       567    567       Nickel 1. {ECO:0000256|PIRSR:PIRSR611612-
FT                                51}.
FT   BINDING     426    426       Substrate. {ECO:0000256|PROSITE-ProRule:
FT                                PRU00700}.
FT   MOD_RES     424    424       N6-carboxylysine. {ECO:0000256|PIRSR:
FT                                PIRSR611612-50}.
SQ   SEQUENCE   772 AA;  83083 MW;  0191353D70C40518 CRC64;
     MLGRRHVQPA VCSTLTEIMV EGTFPTGTYL VTVHHPVSTD DGDLAKALYG SFLPIPDIDL
     FPLPLDAEYE STKRPGALIT VKGKVKLNEG RKRIKLRVTS KGDRPIQIGS HYHFIETNPQ
     LDFDRIKAYG YRLDIPAGTS VRFEPGDAKT VGLVEIGGNR VIRGGNHIAT GKVDISRVEE
     ILVNLQEAGF AHTPDPSGDT AFIDTFEMDR KAYATMFGPT VGDTIRLGNT DLWIKVEKDL
     TFYGDECKFG GGKSLREGMG QATGVSDDIS LDLVIVNALI VDWTGIYKAD IGVKNGTIVG
     IGKAGNPDVM DGVSPNMIVG SCTDVIAGEG KIITAGGFDT HIHFICPQQF NEALASGITT
     MLGGGTGPSA GTCATTCTPG KNYMRQMLQA CDTLPMNVGI TGKGNDSDPA ALREQVIAGA
     CGLKLHEDWG TTPSAIDSCL TVCDELDIQC LIHTDTLNES GFVESTIAAF KNRAIHTYHT
     EGAGGGHAPD IISVVEHANV LPSSTNPTRP YTRNTLDEHL DMLMVCHHLS KNIPEDVAFA
     ESRIRAETIA AEDILHDLGA ISMMSSDSQA MGRCGEVIMR TWNTAHKNKV QRGALGEDLG
     TGADNFRVKR YVSKYTINPA LAQGMGHIIG SVEVGKLADL VVWDPAWFGT KPTTIIKSGM
     IAYAHMGDPN GSISTIQPII ARPMFAPLVP STSILFVSES SISSGTIATY GLKSRVEAVK
     NCRVVGKKDM KFNDQMPKMK VDPENYRVEA DGVHLVCEPA DWLPLGQNAY VY
//
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