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Database: UniProt
Entry: A0A2H3GEG9_FUSOX
LinkDB: A0A2H3GEG9_FUSOX
Original site: A0A2H3GEG9_FUSOX 
ID   A0A2H3GEG9_FUSOX        Unreviewed;      1321 AA.
AC   A0A2H3GEG9;
DT   31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT   31-JAN-2018, sequence version 1.
DT   31-JUL-2019, entry version 11.
DE   RecName: Full=Urease domain-containing protein {ECO:0000259|PROSITE:PS51368};
GN   ORFNames=AU210_015457 {ECO:0000313|EMBL:PCD23943.1};
OS   Fusarium oxysporum f. sp. radicis-cucumerinum.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina;
OC   Sordariomycetes; Hypocreomycetidae; Hypocreales; Nectriaceae;
OC   Fusarium; Fusarium oxysporum species complex.
OX   NCBI_TaxID=327505 {ECO:0000313|EMBL:PCD23943.1, ECO:0000313|Proteomes:UP000219602};
RN   [1] {ECO:0000313|EMBL:PCD23943.1, ECO:0000313|Proteomes:UP000219602}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Forc016 {ECO:0000313|EMBL:PCD23943.1,
RC   ECO:0000313|Proteomes:UP000219602};
RX   PubMed=27387256; DOI=10.1111/1462-2920.13445;
RA   van Dam P., Fokkens L., Schmidt S.M., Linmans J.H., Kistler H.C.,
RA   Ma L.J., Rep M.;
RT   "Effector profiles distinguish formae speciales of Fusarium
RT   oxysporum.";
RL   Environ. Microbiol. 18:4087-4102(2016).
RN   [2] {ECO:0000313|EMBL:PCD23943.1, ECO:0000313|Proteomes:UP000219602}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Forc016 {ECO:0000313|EMBL:PCD23943.1,
RC   ECO:0000313|Proteomes:UP000219602};
RX   PubMed=28831051; DOI=10.1038/s41598-017-07995-y;
RA   van Dam P., Fokkens L., Ayukawa Y., van der Gragt M., Ter Horst A.,
RA   Brankovics B., Houterman P.M., Arie T., Rep M.;
RT   "A mobile pathogenicity chromosome in Fusarium oxysporum for infection
RT   of multiple cucurbit species.";
RL   Sci. Rep. 7:9042-9042(2017).
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:PCD23943.1}.
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DR   EMBL; MABQ02000011; PCD23943.1; -; Genomic_DNA.
DR   OrthoDB; 183108at2759; -.
DR   Proteomes; UP000219602; Chromosome 13.
DR   GO; GO:0005634; C:nucleus; IEA:InterPro.
DR   GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR   GO; GO:0016151; F:nickel cation binding; IEA:InterPro.
DR   GO; GO:0009039; F:urease activity; IEA:InterPro.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0006351; P:transcription, DNA-templated; 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   InterPro; IPR006680; Amidohydro-rel.
DR   InterPro; IPR011059; Metal-dep_hydrolase_composite.
DR   InterPro; IPR032466; Metal_Hydrolase.
DR   InterPro; IPR007219; Transcription_factor_dom_fun.
DR   InterPro; IPR011612; Urease_alpha_N_dom.
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; PF04082; Fungal_trans; 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; SM00906; Fungal_trans; 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   PROSITE; PS01120; UREASE_1; 1.
DR   PROSITE; PS51368; UREASE_3; 1.
PE   3: Inferred from homology;
KW   Complete proteome {ECO:0000313|Proteomes:UP000219602};
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:UP000219602}.
FT   DOMAIN      400    862       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:PIRSR611612-51}.
FT   METAL       407    407       Nickel 1; via tele nitrogen.
FT                                {ECO:0000256|PIRSR:PIRSR611612-51}.
FT   METAL       488    488       Nickel 1; via carbamate group.
FT                                {ECO:0000256|PIRSR:PIRSR611612-51}.
FT   METAL       488    488       Nickel 2; via carbamate group.
FT                                {ECO:0000256|PIRSR:PIRSR611612-51}.
FT   METAL       517    517       Nickel 2; via pros nitrogen.
FT                                {ECO:0000256|PIRSR:PIRSR611612-51}.
FT   METAL       543    543       Nickel 2; via tele nitrogen.
FT                                {ECO:0000256|PIRSR:PIRSR611612-51}.
FT   METAL       631    631       Nickel 1. {ECO:0000256|PIRSR:PIRSR611612-
FT                                51}.
FT   BINDING     490    490       Substrate. {ECO:0000256|PROSITE-ProRule:
FT                                PRU00700}.
FT   MOD_RES     488    488       N6-carboxylysine. {ECO:0000256|PIRSR:
FT                                PIRSR611612-50}.
SQ   SEQUENCE   1321 AA;  144423 MW;  C1EF3422E80B44B5 CRC64;
     MHYTPREVEK LLFAQAGRLA QRRLAHGKKL NHLESSALIA TVLQEIIHNE DYSVADLMKL
     GKGILGRRHV HPPVVGTLKQ MQVEGTFKTG THLITIHNPI STDEGDLKMA LYGSFLPIPT
     SDLFSAVNEA DFHPLAMPGA IRPADTGDIV LNAGRSRVRL TVTNQGTRAI HIGSHFHFME
     TNPDLDFDRG KAYGYHLDLP AGEFLRFEPN EPKTVTLVQV GGSRIIQGGS GYTKGPVDPT
     NAQKILQQLQ QAGYRHSLEG STGQQTVKPC SISREKYASA YGPTTGDCIR LGSTDLWVKV
     EKDCTSYGDE CTLGCGKTIR DGMGAASGCS DADCLDLAII NAVIIDWTGI FKGDIGVKDG
     AIVGIGKAGN PATMDGVSDN MVIGSNTDII DAGGKIVTAG GIDTHVHNIC PQQAFEAISS
     GITTLFGGGT GPSTSSTAVN GTASKKYIRQ MMQACDQLPL NFGLVGKGSD SERVGLLDQI
     KAGVIALKLH EDFGCTPSTI DNCLNVCEEQ DIQCHIHTDG LNEAGFLEHT AAIFKGRSIH
     VYHVEGAGGG HAPDVIKLVA YPNVLPSSTT PTMPFTTNTI DEHIDMAANC HRLSKDNPDD
     ASFLKNRIRE ETISAEDILH DIGAISIMSS DSQAMGRSAE VLTCTWKAAH KNKVQRGPLD
     EDKDTGADNF RVKRFISKYT INPAITQGIS HAVGSIEAGK LADLVIWGPA EFGTKPFQVL
     KKGFITYAQM GDPNGAVADV EPLIGRPMYG ALHPESSVMF VSQASIAQGG DVHSYNLKKQ
     IEVVKNCRTV KKGDLKYNSA TPKVDVDPET LVPYHQASAL GSVAATTQLQ FSKSLDDING
     QTSILLGASS ESDPWLLRHC QFDEYGLRSF YGLQFRNIGG VPNRQKIPVH FIVRQDETDM
     VDASLRARLN ELIPVSWGLR LIRLFYKHVY PVMPIISSTY FNQELLSDLY PAPGVFDHVP
     CHLLGAIYGL AIPFARNDDH LSIVDMYNQL PLEAVWRLVH ESLQVEIRHP QLSVLQAGLF
     YLHGTGQDHR PLSTAPDAFK WSWLGSLVGM AHNLGLHLET RMCAIPTEEK QLRARLWWAL
     YTEDKWISLL MGRPPYISED EWDVSPLEES DFSVPISVPF ADITHAELTR PFRDMSRLSA
     IASLVQSSFY SLKASQKLSE NLSLSIQIAQ PIFEQLSLWR ASVLAPESPT ITSNNGMLND
     KASYPAAILV AHATLVTYVW RALLRPIVPS AIPPLIVDDQ QLAEASLFME LQPHDIENLC
     WDLPDLSHLE LPLRSTVDGT SSHDAVTQNL HQSSLAWATS LSSLVKNLSP ARFHEFWYSC
     E
//
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