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Database: UniProt
Entry: A0A094DB64_9PEZI
LinkDB: A0A094DB64_9PEZI
Original site: A0A094DB64_9PEZI 
ID   A0A094DB64_9PEZI        Unreviewed;      1716 AA.
AC   A0A094DB64;
DT   26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT   26-NOV-2014, sequence version 1.
DT   31-JUL-2019, entry version 23.
DE   SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:KFY61443.1};
GN   ORFNames=V497_02962 {ECO:0000313|EMBL:KFY61443.1};
OS   Pseudogymnoascus sp. VKM F-4516 (FW-969).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC   Leotiomycetes incertae sedis; Pseudeurotiaceae; Pseudogymnoascus.
OX   NCBI_TaxID=1420910 {ECO:0000313|EMBL:KFY61443.1, ECO:0000313|Proteomes:UP000029268};
RN   [1] {ECO:0000313|EMBL:KFY61443.1, ECO:0000313|Proteomes:UP000029268}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=VKM F-4516 (FW-969) {ECO:0000313|Proteomes:UP000029268};
RA   Leushkin E.V., Logacheva M.D., Penin A.A., Sutormin R.A.,
RA   Gerasimov E.S., Kochkina G.A., Ivanushkina N.E., Vasilenko O.V.,
RA   Kondrashov A.S., Ozerskaya S.M.;
RT   "Population genomics of a fungus Geomyces pannorum provides evidence
RT   of horizontal gene transfer but not of sexual reproduction.";
RL   Submitted (JUL-2014) to the EMBL/GenBank/DDBJ databases.
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:KFY61443.1}.
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DR   EMBL; JPJZ01000718; KFY61443.1; -; Genomic_DNA.
DR   EnsemblFungi; KFY61443; KFY61443; V497_02962.
DR   OrthoDB; 55068at2759; -.
DR   Proteomes; UP000029268; Unassembled WGS sequence.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0016151; F:nickel cation binding; IEA:InterPro.
DR   GO; GO:0009039; F:urease activity; IEA:InterPro.
DR   GO; GO:0055085; P:transmembrane transport; 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; IPR011701; MFS.
DR   InterPro; IPR020846; MFS_dom.
DR   InterPro; IPR036259; MFS_trans_sf.
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; PF07690; MFS_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; SSF103473; SSF103473; 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   TIGRFAMs; TIGR00193; urease_gam; 1.
DR   PROSITE; PS50850; MFS; 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:UP000029268};
KW   Hydrolase {ECO:0000256|PROSITE-ProRule:PRU00700};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR611612-51};
KW   Nickel {ECO:0000256|PIRSR:PIRSR611612-51};
KW   Reference proteome {ECO:0000313|Proteomes:UP000029268};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM   1319   1337       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM   1357   1380       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM   1386   1403       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM   1410   1429       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM   1480   1498       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM   1567   1587       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM   1594   1614       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM   1620   1642       Helical. {ECO:0000256|SAM:Phobius}.
FT   DOMAIN      399    835       Urease. {ECO:0000259|PROSITE:PS51368}.
FT   DOMAIN     1321   1716       MFS. {ECO:0000259|PROSITE:PS50850}.
FT   REGION     1058   1103       Disordered. {ECO:0000256|SAM:MobiDB-
FT                                lite}.
FT   REGION     1145   1166       Disordered. {ECO:0000256|SAM:MobiDB-
FT                                lite}.
FT   REGION     1216   1268       Disordered. {ECO:0000256|SAM:MobiDB-
FT                                lite}.
FT   COMPBIAS   1217   1241       Polar. {ECO:0000256|SAM:MobiDB-lite}.
FT   ACT_SITE    590    590       Proton donor. {ECO:0000256|PIRSR:
FT                                PIRSR611612-52, ECO:0000256|PROSITE-
FT                                ProRule:PRU00700}.
FT   METAL       404    404       Nickel 1; via tele nitrogen.
FT                                {ECO:0000256|PIRSR:PIRSR611612-51}.
FT   METAL       406    406       Nickel 1; via tele nitrogen.
FT                                {ECO:0000256|PIRSR:PIRSR611612-51}.
FT   METAL       487    487       Nickel 1; via carbamate group.
FT                                {ECO:0000256|PIRSR:PIRSR611612-51}.
FT   METAL       487    487       Nickel 2; via carbamate group.
FT                                {ECO:0000256|PIRSR:PIRSR611612-51}.
FT   METAL       516    516       Nickel 2; via pros nitrogen.
FT                                {ECO:0000256|PIRSR:PIRSR611612-51}.
FT   METAL       542    542       Nickel 2; via tele nitrogen.
FT                                {ECO:0000256|PIRSR:PIRSR611612-51}.
FT   METAL       630    630       Nickel 1. {ECO:0000256|PIRSR:PIRSR611612-
FT                                51}.
FT   BINDING     489    489       Substrate. {ECO:0000256|PROSITE-ProRule:
FT                                PRU00700}.
FT   MOD_RES     487    487       N6-carboxylysine. {ECO:0000256|PIRSR:
FT                                PIRSR611612-50}.
SQ   SEQUENCE   1716 AA;  184551 MW;  B34BED08D668AD45 CRC64;
     MHLIPREIDK LVISQLGLLA QRRLARGVRL NHSEACALIA NNLQELIRDG NHNVADLMSI
     GTTMLGRRHV LPAVVSTLKQ IQVEGTFPQG TYLVTVQNPI SSDDGDLDKA LYASFLPIPD
     ADLFKLPEDE ECKAENMPGA VIAVKGKITI NEGRKRIQLK VTNHGDRPIQ VGSHYHFIET
     NPNLEFDRIR SYGYRLDIAA GTSIRFEAGD EKTVTLVEIA GRRIIRGGNN IASGVFDLSR
     TDEILKNIEA GNFKHTLEPA GDAAHIKPFE IDRSVYASMF GPTVGDKIRL GDTDLWIKVE
     KDLTSYGDEC KFGGGKTLRD GMGQTTGESD EDSLDLVIVN ALIVDWSGIY KADIGIKNGF
     ISGIGKAGSP DVMEGVTDGM IVGACTDVMA GEGMIVTAGG IDTHIHYICP QQASECMATG
     VTTLLGGGTG PTAATTATTC TPGKNNIRNM MQALDQLPLN YGITGKGNDS DPKALREQVE
     AGACGLKLHE DWGCTPAAID SCLTVCDEYD VQCLIHTDTL NESGFVESTI AAFKDRAIHT
     YHSEGAGGGH APDIISVVEH NNVLPSSTNP TRPYTRNTLD EHLDMVMVCH HLSKNIPEDI
     AFAESRIRAE TIAAEDVLHD MGAISMMSSD SQAMGRCGEV VLRTWNTAHK NKVQRGFLKE
     DEGTDADNFR VKRYVSKYTI NPAITQGMGH LLGSVEVGKL ADLVIWEPAW FGTKPTYVVK
     SGLISYSMMG DPNASISTVQ PIIGRPMFAP HVPSSSVIFV SQASIDNGVI ESYGLKKRVE
     AVKNCRKIRK KDMKHNFNMP KIHVDPENYR VEANGEHCTA EPSSELPLTQ AIGKVYVHFN
     MKPSVASLTT AALAFVGQVL AAPQGQILSL SHDLKADTTT PARAANSLQW IGPIAPAGED
     VGMQMVRVAR DAQVHHVGHL VRRKKVDASK APQDRIVCDR EDMALNQYGE TWAAYKLASV
     VGALAATNES SVVVIGGGHG HCVDLTACDE AERARIQLCN DNPEPNHVKV QTIAEFAYRI
     IYECARQDGS GIIWGQEFGD NEFNVIISGC PANYKKEGPK GPLLPSKVDG PKAPVTPPKT
     EGPKTSVTPP KVKGPKGKDA NIETGHGYGA TWLAARSNKQ TTFPFGLDWT PSQKCRVPRN
     AKATLKPAPQ PTRVSSERPD GYLEQRTDDT GSFLIEETIP YDRDKCDTVE ANYLGTAHAP
     AGDDMATEDV KVKVGLSKND TGNSKDDNGI SNGNGNDAPE RIESTATRDE GATLGTASTG
     ATKGGEGAAA AKKGWKRKGW FGRMNASAEG EALENMGSRD GLLEGGAGEV VWKVYKRRWF
     GLLQLVLLNV VVSWDWLSFA PVSTTASEYF DTSMTAINWL STGFLFAFCV ATPFTIYVLH
     KGGPKPAIIT ASVLLLIGNW IRYGGTRAQN FGVVMFGQIL TGFAQPFVLS SPTHYSDLWF
     TNNGRVAATA VMTLANPLGG ALGQLIDPFF APNAKDIPNM VLYVSIIATV ASIPSFFIPA
     APPTPSSPSA TDHKLDIIPS IKKLFNSREF IMMLVPYTVY VGFFNSISSL LNQILEPYGF
     SEEQAGIAGA ILIVVGLVAA AASSPILDRS KKFLLAIKIQ VPLIALSYLA FIWAPPTRGL
     AAPYTILAIL GASSFTLLPV ALEYVTEITH PVSPEVTSTI LWSGGQLLGG LFIVISDALQ
     DGPQGGYNCA GGYGAAPMSG VVWEKRAGED EESGGG
//
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