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Database: UniProt
Entry: A0A167V0X4_9HYPO
LinkDB: A0A167V0X4_9HYPO
Original site: A0A167V0X4_9HYPO 
ID   A0A167V0X4_9HYPO        Unreviewed;       873 AA.
AC   A0A167V0X4;
DT   06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT   06-JUL-2016, sequence version 1.
DT   31-JUL-2019, entry version 25.
DE   SubName: Full=Urease {ECO:0000313|EMBL:OAA62106.1};
GN   ORFNames=ISF_05115 {ECO:0000313|EMBL:OAA62106.1};
OS   Cordyceps fumosorosea ARSEF 2679.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina;
OC   Sordariomycetes; Hypocreomycetidae; Hypocreales; Cordycipitaceae;
OC   Cordyceps.
OX   NCBI_TaxID=1081104 {ECO:0000313|EMBL:OAA62106.1, ECO:0000313|Proteomes:UP000076744};
RN   [1] {ECO:0000313|EMBL:OAA62106.1, ECO:0000313|Proteomes:UP000076744}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ARSEF 2679 {ECO:0000313|EMBL:OAA62106.1,
RC   ECO:0000313|Proteomes:UP000076744};
RX   PubMed=27071652; DOI=10.1093/gbe/evw082;
RA   Shang Y., Xiao G., Zheng P., Cen K., Zhan S., Wang C.;
RT   "Divergent and convergent evolution of fungal pathogenicity.";
RL   Genome Biol. Evol. 8:1374-1387(2016).
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}.
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:OAA62106.1}.
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DR   EMBL; AZHB01000012; OAA62106.1; -; Genomic_DNA.
DR   RefSeq; XP_018703856.1; XM_018848720.1.
DR   EnsemblFungi; OAA62106; OAA62106; ISF_05115.
DR   GeneID; 30021407; -.
DR   OrthoDB; 183108at2759; -.
DR   Proteomes; UP000076744; 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; 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; 2.
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:UP000076744};
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:UP000076744}.
FT   DOMAIN      437    873       Urease. {ECO:0000259|PROSITE:PS51368}.
FT   REGION      262    284       Disordered. {ECO:0000256|SAM:MobiDB-
FT                                lite}.
FT   COMPBIAS    268    284       Polar. {ECO:0000256|SAM:MobiDB-lite}.
FT   ACT_SITE    628    628       Proton donor. {ECO:0000256|PIRSR:
FT                                PIRSR611612-52, ECO:0000256|PROSITE-
FT                                ProRule:PRU00700}.
FT   METAL       442    442       Nickel 1; via tele nitrogen.
FT                                {ECO:0000256|PIRSR:PIRSR001222-51}.
FT   METAL       444    444       Nickel 1; via tele nitrogen.
FT                                {ECO:0000256|PIRSR:PIRSR001222-51}.
FT   METAL       525    525       Nickel 1; via carbamate group.
FT                                {ECO:0000256|PIRSR:PIRSR001222-51}.
FT   METAL       525    525       Nickel 2; via carbamate group.
FT                                {ECO:0000256|PIRSR:PIRSR001222-51}.
FT   METAL       554    554       Nickel 2; via pros nitrogen.
FT                                {ECO:0000256|PIRSR:PIRSR001222-51}.
FT   METAL       580    580       Nickel 2; via tele nitrogen.
FT                                {ECO:0000256|PIRSR:PIRSR001222-51}.
FT   METAL       668    668       Nickel 1. {ECO:0000256|PIRSR:PIRSR001222-
FT                                51}.
FT   BINDING     527    527       Substrate. {ECO:0000256|PROSITE-ProRule:
FT                                PRU00700}.
FT   MOD_RES     525    525       N6-carboxylysine. {ECO:0000256|PIRSR:
FT                                PIRSR001222-50}.
SQ   SEQUENCE   873 AA;  93171 MW;  C8A1E835B00FD86C CRC64;
     MHLVPKELDK LVISQLGLLA QRRLARGVKL NHAEATALIT NNIQELIRDG NHTVADLMAL
     GATMLGRRHV MPSVCHTLRE IQVEGTFPTG TYLVTVHNPI STDDGDLARA LYGSFLPVPR
     GAEADALFPA ELDAAAFAPA RQPGALVPLK AEKITLNPGR RRISLRVTSR GDRPIQVGSH
     YHFIEANPEL AFDRGRAYGF RLDIPAGTSY RFEPGDAKTV TLVEIAGHQV IRGGNGLATG
     GVERWRVDDI VERLQAQGYA HLPEPDEKTT NGITNGSTAR RRGSATTRAA AAAGAVANRV
     PRAPRPYRMD RAAYAVMFGP TTGDRVRLGA TDLWVRVERD CTAYGDECKF GGGKTLREGM
     GQATGRPDAD ALDLVITNAL IVDHSGIYKA DIGVKAGMIV GIGKAGNPDV MDGVAPNMVV
     GSCTDVIAGE NKIVTAGAID THIHLICPQQ AQEALASGVT TFLGGGTGPS SGSNATTCTP
     GKHLMKQMLR ACDTLPVNVG ITGKGNDSAP AALREQVAAG ACGLKIHEDW GATPSAIDAC
     LTVCDEMDVQ CLIHTDTLNE SGFVESTVAA FRGRTIHTYH TEGAGGGHAP DIISVVERAN
     VLPSSTNPTR PYTRNTLDEH LDMLMVCHHL SKDIPEDVAF AESRIRAETI AAEDVLHDVG
     AISMMSSDSQ AMGRCGEVVL RTWNTAHKNR CQRGPLPEDE GSGADNFRVK RYVSKYTVNP
     ALAQGFAHLV GSVEVGKLAD LVIWDPAWFG TKPHQVIKSG LIAWSQMGDP NASIPTVQPV
     IGRPMFAPLV PETSVLFVSQ AAVASGTVAS YGLRKRVEAV HGCRSVGKAD MKFNDAMPRM
     RVDPESYTVE ADGEVCTAEP AETLPLTQAY YVF
//
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