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Database: UniProt
Entry: M1VTU7_CLAP2
LinkDB: M1VTU7_CLAP2
Original site: M1VTU7_CLAP2 
ID   M1VTU7_CLAP2            Unreviewed;       892 AA.
AC   M1VTU7;
DT   01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT   01-MAY-2013, sequence version 1.
DT   31-JUL-2019, entry version 33.
DE   SubName: Full=Probable urease {ECO:0000313|EMBL:CCE26642.1};
GN   ORFNames=CPUR_00111 {ECO:0000313|EMBL:CCE26642.1};
OS   Claviceps purpurea (strain 20.1) (Ergot fungus) (Sphacelia segetum).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina;
OC   Sordariomycetes; Hypocreomycetidae; Hypocreales; Clavicipitaceae;
OC   Claviceps.
OX   NCBI_TaxID=1111077 {ECO:0000313|EMBL:CCE26642.1, ECO:0000313|Proteomes:UP000016801};
RN   [1] {ECO:0000313|EMBL:CCE26642.1, ECO:0000313|Proteomes:UP000016801}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=20.1 {ECO:0000313|EMBL:CCE26642.1,
RC   ECO:0000313|Proteomes:UP000016801};
RX   PubMed=23468653; DOI=10.1371/journal.pgen.1003323;
RA   Schardl C.L., Young C.A., Hesse U., Amyotte S.G., Andreeva K.,
RA   Calie P.J., Fleetwood D.J., Haws D.C., Moore N., Oeser B.,
RA   Panaccione D.G., Schweri K.K., Voisey C.R., Farman M.L.,
RA   Jaromczyk J.W., Roe B.A., O'Sullivan D.M., Scott B., Tudzynski P.,
RA   An Z., Arnaoudova E.G., Bullock C.T., Charlton N.D., Chen L., Cox M.,
RA   Dinkins R.D., Florea S., Glenn A.E., Gordon A., Gueldener U.,
RA   Harris D.R., Hollin W., Jaromczyk J., Johnson R.D., Khan A.K.,
RA   Leistner E., Leuchtmann A., Li C., Liu J., Liu J., Liu M., Mace W.,
RA   Machado C., Nagabhyru P., Pan J., Schmid J., Sugawara K., Steiner U.,
RA   Takach J.E., Tanaka E., Webb J.S., Wilson E.V., Wiseman J.L.,
RA   Yoshida R., Zeng Z.;
RT   "Plant-symbiotic fungi as chemical engineers: Multi-genome analysis of
RT   the Clavicipitaceae reveals dynamics of alkaloid loci.";
RL   PLoS Genet. 9:E1003323-E1003323(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}.
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:CCE26642.1}.
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DR   EMBL; CAGA01000001; CCE26642.1; -; Genomic_DNA.
DR   STRING; 5111.M1VTU7; -.
DR   EnsemblFungi; CCE26642; CCE26642; CPUR_00111.
DR   OrthoDB; 183108at2759; -.
DR   Proteomes; UP000016801; 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; 2.10.150.10; -; 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; 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; 2.
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; 2.
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:UP000016801};
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:UP000016801}.
FT   DOMAIN      416    892       Urease. {ECO:0000259|PROSITE:PS51368}.
FT   REGION      669    722       Disordered. {ECO:0000256|SAM:MobiDB-
FT                                lite}.
FT   COMPBIAS    683    722       Polar. {ECO:0000256|SAM:MobiDB-lite}.
FT   ACT_SITE    607    607       Proton donor. {ECO:0000256|PIRSR:
FT                                PIRSR611612-52, ECO:0000256|PROSITE-
FT                                ProRule:PRU00700}.
FT   METAL       421    421       Nickel 1; via tele nitrogen.
FT                                {ECO:0000256|PIRSR:PIRSR611612-51}.
FT   METAL       423    423       Nickel 1; via tele nitrogen.
FT                                {ECO:0000256|PIRSR:PIRSR611612-51}.
FT   METAL       504    504       Nickel 1; via carbamate group.
FT                                {ECO:0000256|PIRSR:PIRSR611612-51}.
FT   METAL       504    504       Nickel 2; via carbamate group.
FT                                {ECO:0000256|PIRSR:PIRSR611612-51}.
FT   METAL       533    533       Nickel 2; via pros nitrogen.
FT                                {ECO:0000256|PIRSR:PIRSR611612-51}.
FT   METAL       559    559       Nickel 2; via tele nitrogen.
FT                                {ECO:0000256|PIRSR:PIRSR611612-51}.
FT   METAL       647    647       Nickel 1. {ECO:0000256|PIRSR:PIRSR611612-
FT                                51}.
FT   BINDING     506    506       Substrate. {ECO:0000256|PROSITE-ProRule:
FT                                PRU00700}.
FT   MOD_RES     504    504       N6-carboxylysine. {ECO:0000256|PIRSR:
FT                                PIRSR611612-50}.
SQ   SEQUENCE   892 AA;  95335 MW;  1BF18D9DA8085806 CRC64;
     MHLVPRELDK LVISQLGLLA QRRLARGVRL NHSEATALIA NNLQELIRDG NHSVADLMLL
     GTTMLGRRHV LPAVCSTLRE LQVEGTFPMG TFLVTVHNPI STDDGDLARA LYGSFLPVPD
     NEAVFPLPPA SEYQPERQPG AVVVVKGTVA LNQTPKRARR RLRVTSTGDR PIQVGSHYHF
     IEVNPQLEFD RERAYGFRLD IPAGTSVRFE PGDTKTVRLV AIGGHRIIRG GNNVASGPVD
     MRLIKEIVSN MQAKGYAHTT ALDEGDGNED TFLVDPRGDG AHMDMVQMDR AAYATMFGPT
     TGDLVRLSNT NLWIQVERDM TSYGDECKFG GGKTLRDGMG QASGRRDADT LDVVVTNALI
     VDWTGIYKAD IGIKDGMIVG IGKAGNPDVM DGVAPNMVVG SCTDVVAAEG KIVTAGGIDT
     HVHFICPQQV DEALASGITT MIGGGTGPSA GTKATTCTPG KRHLGLMLQA CDTLPLNIGL
     TGKGSDASPV ALREQITAGA CGLKIHEDWG ATPAALDACL DACDELDVQC TLHTDTLNES
     GFVEQTLAAV RGRTVHTYHS EGAGGGHAPD ILSVVGHPNV LPASTTPTRP YTRNTLDEHL
     DMLMVCHHLS RRIPEDVAFA ESRIRAETMA AEDVLHDTGA VSIMSSDSQA MGRCGEVILR
     TWNTAHKNKL QRGPLPEDRL DSAAGMSSSS ASSPASPTAS PTPSSSSSAS SSTASSSSFS
     APNDNRRVRR YIAKYTINPA IAHGISHLVG SLEPNKLADL VLWDPALFGT KPSLILKAGL
     PAWTPMGDPN GSIPTVQPLI GRPMFAPLLP SCKMLFVSQA CVDSGAAASY NLRSRVEPVR
     NCRKIGKRDM CLNDAMPSVR VDPETYQVRA DGEECRAEAA DELPLAQAWF VY
//
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