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Database: UniProt
Entry: A0A094EJT9_9PEZI
LinkDB: A0A094EJT9_9PEZI
Original site: A0A094EJT9_9PEZI 
ID   A0A094EJT9_9PEZI        Unreviewed;      1655 AA.
AC   A0A094EJT9;
DT   26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT   26-NOV-2014, sequence version 1.
DT   31-JUL-2019, entry version 22.
DE   SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:KFY78981.1};
GN   ORFNames=V499_01977 {ECO:0000313|EMBL:KFY78981.1};
OS   Pseudogymnoascus sp. VKM F-103.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC   Leotiomycetes incertae sedis; Pseudeurotiaceae; Pseudogymnoascus.
OX   NCBI_TaxID=1420912 {ECO:0000313|EMBL:KFY78981.1, ECO:0000313|Proteomes:UP000029295};
RN   [1] {ECO:0000313|EMBL:KFY78981.1, ECO:0000313|Proteomes:UP000029295}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=VKM F-103 {ECO:0000313|EMBL:KFY78981.1,
RC   ECO:0000313|Proteomes:UP000029295};
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:KFY78981.1}.
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DR   EMBL; JPKB01000287; KFY78981.1; -; Genomic_DNA.
DR   EnsemblFungi; KFY78981; KFY78981; V499_01977.
DR   Proteomes; UP000029295; 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:UP000029295};
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:UP000029295};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM   1226   1244       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM   1264   1287       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM   1293   1310       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM   1317   1336       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM   1387   1407       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM   1437   1454       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM   1474   1494       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM   1501   1521       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM   1527   1547       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM   1606   1626       Helical. {ECO:0000256|SAM:Phobius}.
FT   DOMAIN      399    835       Urease. {ECO:0000259|PROSITE:PS51368}.
FT   DOMAIN     1228   1631       MFS. {ECO:0000259|PROSITE:PS50850}.
FT   REGION     1067   1095       Disordered. {ECO:0000256|SAM:MobiDB-
FT                                lite}.
FT   REGION     1134   1181       Disordered. {ECO:0000256|SAM:MobiDB-
FT                                lite}.
FT   COMPBIAS   1135   1153       Polyampholyte. {ECO:0000256|SAM:MobiDB-
FT                                lite}.
FT   COMPBIAS   1154   1170       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   1655 AA;  178783 MW;  65AD20AFF1EC920B CRC64;
     MHLIPREIDK LVISQLGLLA QRRLARGVRL NHSEACALIA NNLQELIRDG NHNVADLMSI
     GTTMLGRRHV LPAVVSTLKQ IQVEGTFPQG TYLVTVQTPI SSDDGDLNKA LYGSFLPIPD
     ADLFKVPEDE ECTAEKMPGA VIAVKGKIAI NKGRKRIQLK VTNHGDRPVQ VGSHYHFIET
     NPHLEFDRIR SYGYRLDIAA GTSIRFEAGD EKTVTLVEIA GRKIVRGGNN IASGVFDLSR
     TDEILKNIEA GNFRNILEPA GDAAHIKPFE LDRSVYASMF GPTVGDKIRL GDTDLWIKVE
     KDLTSYGDEC KFGGGKTLRD GMGQATGESD EDSLDLVIIN ALIVDWSGIY KADIGIKNGF
     ISGIGKAGSP DVMNGVTEGM IVGSCTDVMA GEGMIVTAGG IDTHIHYICP QQASECMATG
     VTTLLGGGTG PTAATTATTC TPGKNNMRDM LQALDAMPLN YGITGKGNDS DPKALREQVE
     AGACGLKLHE DWGCTPAAID SCLTVCDEYD VQCLIHTDTL NESGFVESTI AAFKDRAIHT
     YHTEGAGGGH APDIISVVEY DNVLPSSTNP TRPFTRNTLD EHLDMVMVCH HLSKNIPEDI
     AFAESRIRAE TIAAEDVLHD MGAISMMSSD SQAMGRCGEV VLRTWNTAHK NKVQRGFLKE
     DEGTDADNFR VKRYVSKYTI NPALAQGMSH LLGSVEVGKL ADLVIWDPAW FGTKPTMVVK
     SGLISYSMMG DPNASISTVQ PVIGRPMFAP HVPSTSVLFV SQASIDCGNI ESYGLKKRVE
     AVKGCRTVRK KDMKHNYEMP KIHVDPENYR VEADGVHCTA EPSTELPLTQ SVTAILHYFN
     MKTCVTSLTA FALASQVFGA PQGFISLASE RNTDTATPAR AANALEWIGP IGPAGEVYSY
     YGNLKACPIP DNEMVQVARD AQVHHVGGLV RRKKVTASKA PQDKIVCDRE DMTVAQYGET
     WAAYKLAAVV GALAATNDSA VVVIGGGHGH CVDLTACDEA ERARIQLCND NPQANHVKVQ
     TIAEYAYRII YECARQDGSG LIWGQEFDDN QFNVIISGCP VYYPPKKEEP KTPLAPPKVK
     GPKVKGPKGQ EPNGTQRTIS LRWLARARAP VRDDMGSDAA ATAVAGLSKN DAVVTKDDNS
     NDAAERIETS TTRDDSATLE TATSGAATKA EGEQQRGAKK GWRRKGWFGK MNASAEGEAL
     ENMGSRDGLL EGGEGEVVWK VYKRRWFGLL QLVLLNVVVS WDWLSFAPVS TTASEYFDIS
     MTAVNWLSTG FLFAFCVATP FTIYVLHKGG PKPAIITASV LLLVGNWIRY GGTRVRNYGV
     VMFGQILTGF AQPFVLSSPT HYSDLWFTNN GRVAATAIMT LANPLGGALG QLIDPFFAPN
     KGDIPNMVLY ISIIATVASI PSFFIPATPP TPSSPSSTEH KLDIIPSIKT LFKSPEFIMM
     LIPYTVYVGL FNSISSLLNQ MLSPYGFTEE EAGIAGAILI VVGLVAAAIS SPILDRSKKF
     LLAIKIQVPL IALAYLAFIW APPTRGVAAP YTILAILGAA SFTLLPVALE YVTELTHPVS
     PEVTSTILWS GGQLLGGLFI VISDALTDGD KGGPGSDVPR NMQRALWFQA VIAMVVMVPP
     LCLGLFGRRE QVKMRRVEAD KVYREGQRTN GGVVS
//
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