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Database: UniProt
Entry: A0A059D8S4_EUCGR
LinkDB: A0A059D8S4_EUCGR
Original site: A0A059D8S4_EUCGR 
ID   A0A059D8S4_EUCGR        Unreviewed;       649 AA.
AC   A0A059D8S4;
DT   09-JUL-2014, integrated into UniProtKB/TrEMBL.
DT   09-JUL-2014, sequence version 1.
DT   11-DEC-2019, entry version 24.
DE   RecName: Full=Urease domain-containing protein {ECO:0000259|PROSITE:PS51368};
GN   ORFNames=EUGRSUZ_B03469 {ECO:0000313|EMBL:KCW86884.1};
OS   Eucalyptus grandis (Flooded gum).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Myrtales; Myrtaceae; Myrtoideae; Eucalypteae; Eucalyptus.
OX   NCBI_TaxID=71139 {ECO:0000313|EMBL:KCW86884.1, ECO:0000313|Proteomes:UP000030711};
RN   [1] {ECO:0000313|Proteomes:UP000030711}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. BRASUZ1 {ECO:0000313|Proteomes:UP000030711};
RX   PubMed=24919147; DOI=10.1038/nature13308;
RA   Myburg A.A., Grattapaglia D., Tuskan G.A., Hellsten U., Hayes R.D.,
RA   Grimwood J., Jenkins J., Lindquist E., Tice H., Bauer D., Goodstein D.M.,
RA   Dubchak I., Poliakov A., Mizrachi E., Kullan A.R., Hussey S.G., Pinard D.,
RA   van der Merwe K., Singh P., van Jaarsveld I., Silva-Junior O.B.,
RA   Togawa R.C., Pappas M.R., Faria D.A., Sansaloni C.P., Petroli C.D.,
RA   Yang X., Ranjan P., Tschaplinski T.J., Ye C.Y., Li T., Sterck L.,
RA   Vanneste K., Murat F., Soler M., Clemente H.S., Saidi N., Cassan-Wang H.,
RA   Dunand C., Hefer C.A., Bornberg-Bauer E., Kersting A.R., Vining K.,
RA   Amarasinghe V., Ranik M., Naithani S., Elser J., Boyd A.E., Liston A.,
RA   Spatafora J.W., Dharmwardhana P., Raja R., Sullivan C., Romanel E.,
RA   Alves-Ferreira M., Kulheim C., Foley W., Carocha V., Paiva J., Kudrna D.,
RA   Brommonschenkel S.H., Pasquali G., Byrne M., Rigault P., Tibbits J.,
RA   Spokevicius A., Jones R.C., Steane D.A., Vaillancourt R.E., Potts B.M.,
RA   Joubert F., Barry K., Pappas G.J., Strauss S.H., Jaiswal P.,
RA   Grima-Pettenati J., Salse J., Van de Peer Y., Rokhsar D.S., Schmutz J.;
RT   "The genome of Eucalyptus grandis.";
RL   Nature 510:356-362(2014).
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. {ECO:0000256|PIRSR:PIRSR611612-
CC       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; KK198754; KCW86884.1; -; Genomic_DNA.
DR   Proteomes; UP000030711; 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; cd00407; Urease_beta; 1.
DR   CDD; cd00390; Urease_gamma; 1.
DR   Gene3D; 2.10.150.10; -; 1.
DR   Gene3D; 3.30.280.10; -; 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; IPR040881; Urease_linker.
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   Pfam; PF18473; Urease_linker; 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; 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   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:UP000030711}.
FT   DOMAIN          399..640
FT                   /note="Urease"
FT                   /evidence="ECO:0000259|PROSITE:PS51368"
FT   ACT_SITE        590
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR611612-52,
FT                   ECO:0000256|PROSITE-ProRule:PRU00700"
FT   METAL           404
FT                   /note="Nickel 1; via tele nitrogen"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR611612-51"
FT   METAL           406
FT                   /note="Nickel 1; via tele nitrogen"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR611612-51"
FT   METAL           487
FT                   /note="Nickel 1; via carbamate group"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR611612-51"
FT   METAL           487
FT                   /note="Nickel 2; via carbamate group"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR611612-51"
FT   METAL           516
FT                   /note="Nickel 2; via pros nitrogen"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR611612-51"
FT   METAL           542
FT                   /note="Nickel 2; via tele nitrogen"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR611612-51"
FT   METAL           630
FT                   /note="Nickel 1"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR611612-51"
FT   BINDING         489
FT                   /note="Substrate"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00700"
FT   MOD_RES         487
FT                   /note="N6-carboxylysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR611612-50"
SQ   SEQUENCE   649 AA;  69575 MW;  F2AA5CF0B35A1F32 CRC64;
     MKLTPRELEK LSLHQAGSLA QKRLARGLRL NYTESVALVA TQILEFVRDG DKTVADLMDL
     GKQILGRRQV LPAVPHLLDT VQVEGTFPDG TKLITVHDVI CREDGNLELA LHGSFLPVPP
     LEKFSRIEED KCPGEVICGN ENIVINRGRK AVILKVTNTG DRPIQVGSHY HFIEANPFLV
     FDRRKAHGMR LNIPAGTATR FEPGETKSVT LVSIGGRKVI RGGNNFADGP IDDATCSVAM
     ETLSSRQIRH LEEVGASAGI TGESLTFTKV ISREAYANIY GPTTGDKIRL GDTNLYAEIE
     RDCATYGDEC VFGGGKVIRD GMGQTCGCQP ADSLDTVITN AVIIDYTGIF KSDIGIKDGI
     IFALGKAGNR DMMDGVCPDM VVGANTEVIA GEGMIVTAGA IDCHVHFICP QLAYEAISSG
     VTTLIGGGTG PADGTRATTC TPAPSHMKLM LQSTDDLPLN FGFTGKGNTS RPEELHEIVK
     AGAMGLKLHE DWGTTPAAID NCLTVGDEHD IQVNIHTDTL NESGFVEHTI AAFKGRTIHT
     YHSEGAGGGH APDIIKVCGV KNVLPSSTNP TRPFTSNTID EHLDMLMVCH HLDKDIPEDV
     AFAESRIRAE TIAAEDILHD MGAISIISSD AQAMGRIGEV PGFLSLLLV
//
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