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Database: UniProt
Entry: A0A094JTE1_9PEZI
LinkDB: A0A094JTE1_9PEZI
Original site: A0A094JTE1_9PEZI 
ID   A0A094JTE1_9PEZI        Unreviewed;      1649 AA.
AC   A0A094JTE1;
DT   26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT   26-NOV-2014, sequence version 1.
DT   18-SEP-2019, entry version 25.
DE   SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:KFZ12333.1};
GN   ORFNames=V501_04285 {ECO:0000313|EMBL:KFZ12333.1};
OS   Pseudogymnoascus sp. VKM F-4519 (FW-2642).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC   Leotiomycetes incertae sedis; Pseudeurotiaceae; Pseudogymnoascus.
OX   NCBI_TaxID=1420914 {ECO:0000313|EMBL:KFZ12333.1, ECO:0000313|Proteomes:UP000029315};
RN   [1] {ECO:0000313|EMBL:KFZ12333.1, ECO:0000313|Proteomes:UP000029315}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=VKM F-4519 (FW-2642) {ECO:0000313|Proteomes:UP000029315};
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:KFZ12333.1}.
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DR   EMBL; JPKD01001412; KFZ12333.1; -; Genomic_DNA.
DR   EnsemblFungi; KFZ12333; KFZ12333; V501_04285.
DR   Proteomes; UP000029315; Unassembled WGS sequence.
DR   GO; GO:0005887; C:integral component of plasma membrane; IEA:InterPro.
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:UP000029315};
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:UP000029315};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM   1220   1238       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM   1258   1280       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM   1287   1304       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM   1381   1402       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM   1431   1448       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM   1468   1488       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM   1495   1515       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM   1521   1541       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM   1600   1620       Helical. {ECO:0000256|SAM:Phobius}.
FT   DOMAIN      399    835       Urease. {ECO:0000259|PROSITE:PS51368}.
FT   DOMAIN     1222   1625       MFS. {ECO:0000259|PROSITE:PS50850}.
FT   REGION     1067   1091       Disordered. {ECO:0000256|SAM:MobiDB-
FT                                lite}.
FT   REGION     1124   1176       Disordered. {ECO:0000256|SAM:MobiDB-
FT                                lite}.
FT   COMPBIAS   1127   1147       Polyampholyte. {ECO:0000256|SAM:MobiDB-
FT                                lite}.
FT   COMPBIAS   1148   1163       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   1649 AA;  177913 MW;  C64B29EC3B2368EA CRC64;
     MHLIPREIDK LVISQLGLLA QRRLARGVRL NHSEACALIA NNLQELIRDG NHNVADLMSI
     GTTMLGRRHV LPAVVSTLKQ IQVEGTFPQG TYLVTVQNPI SSDDGDLNKA LYGSFLPIPD
     ADLFKVPEDE ECTAEKMPGA VIAVKGKIAI NKGRKRIQLR 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 KDMKHNSEMP KIHVDPENYR VEADGVHCTA EPSTELPLTQ SVTAILQYFN
     MKTCVASLTA LALASQVFGA PQGFISLASE RNTDAATPAR AANALEWIGP IGPAGEVYSY
     YGNLKASPIP DNEMVQVARD AQVHHVGGLV RRKKVKASKA PQDKIVCDRE DMTVAQYGET
     WAAYKLAAVV GALAATNDSA VVVIGGGHGH CVDLTACDEA ERARIQLCND NPQANHVKVQ
     TIAEYAYRII YECARQDGSG LIWGQEFDDN QFNVIISGCP AYYPPKKEEP KTPLAPPKVK
     GPKVKGPKGQ EPNLRWLALA RAPVRDDMGS DAATAVGLSK NDAVVTKDDN SNGRDNDAAE
     RIETSTTRDD STTLGTATSG AATKAEGEQR GAKKGWRRKG WFGKMNASAE GEALENMGSR
     DGLLEGGEGE VVWKVYKRRW FGLLQLVLLN VVVSWDWLSF APVSTTASEY FDISMTAVNW
     LSTGFLFAFC VATPFTIYVL HKGGPKPAII TASVLLLVGN WIRYGGTRVQ NYGVVMFGQI
     LTGFAQPFVL SSPTHYSDLW FTNNGRVAAT AIMTLANPLG GALGQLIDPF FAPNKGDIPN
     MVLYISIIAT VASIPSFFIP AAPPTPSSPS STEHKLDIIP SIKTLFKSPE FIMMLIPYTV
     YVGLFNSISS LLNQMLSPYG FTEEEAGIAG AILIVVGLVA AAISSPILDR SKKFLLAIKI
     QVPLIALAYL AFIWAPPTRG VAAPYTILAI LGAASFTLLP VALEYVTELT HPVSPEVTST
     ILWSGGQLLG GLFIVISDAL TDGENGGPGS DVPRNMQRAL WFQAVIAMVV MVPPLCLGLF
     GRREQVKMRR VEADKVYREG QRTNGGVVS
//
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