ID A7TLN6_VANPO Unreviewed; 835 AA.
AC A7TLN6;
DT 02-OCT-2007, integrated into UniProtKB/TrEMBL.
DT 02-OCT-2007, sequence version 1.
DT 27-MAR-2024, entry version 68.
DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:EDO16828.1};
GN ORFNames=Kpol_1056p29 {ECO:0000313|EMBL:EDO16828.1};
OS Vanderwaltozyma polyspora (strain ATCC 22028 / DSM 70294 / BCRC 21397 / CBS
OS 2163 / NBRC 10782 / NRRL Y-8283 / UCD 57-17) (Kluyveromyces polysporus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Vanderwaltozyma.
OX NCBI_TaxID=436907 {ECO:0000313|Proteomes:UP000000267};
RN [1] {ECO:0000313|EMBL:EDO16828.1, ECO:0000313|Proteomes:UP000000267}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 22028 / DSM 70294 / BCRC 21397 / CBS 2163 / NBRC 10782 /
RC NRRL Y-8283 / UCD 57-17 {ECO:0000313|Proteomes:UP000000267};
RX PubMed=17494770; DOI=10.1073/pnas.0608218104;
RA Scannell D.R., Frank A.C., Conant G.C., Byrne K.P., Woolfit M., Wolfe K.H.;
RT "Independent sorting-out of thousands of duplicated gene pairs in two yeast
RT species descended from a whole-genome duplication.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:8397-8402(2007).
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DR EMBL; DS480416; EDO16828.1; -; Genomic_DNA.
DR RefSeq; XP_001644686.1; XM_001644636.1.
DR AlphaFoldDB; A7TLN6; -.
DR STRING; 436907.A7TLN6; -.
DR GeneID; 5545000; -.
DR KEGG; vpo:Kpol_1056p29; -.
DR eggNOG; KOG2645; Eukaryota.
DR HOGENOM; CLU_017594_3_1_1; -.
DR InParanoid; A7TLN6; -.
DR OMA; SEPIWET; -.
DR OrthoDB; 1366859at2759; -.
DR PhylomeDB; A7TLN6; -.
DR Proteomes; UP000000267; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0019637; P:organophosphate metabolic process; IEA:UniProt.
DR GO; GO:0006796; P:phosphate-containing compound metabolic process; IEA:UniProt.
DR CDD; cd16018; Enpp; 1.
DR Gene3D; 3.30.1360.180; -; 1.
DR Gene3D; 3.40.720.10; Alkaline Phosphatase, subunit A; 1.
DR InterPro; IPR017850; Alkaline_phosphatase_core_sf.
DR InterPro; IPR002591; Phosphodiest/P_Trfase.
DR PANTHER; PTHR10151:SF120; BIS(5'-ADENOSYL)-TRIPHOSPHATASE; 1.
DR PANTHER; PTHR10151; ECTONUCLEOTIDE PYROPHOSPHATASE/PHOSPHODIESTERASE; 1.
DR Pfam; PF01663; Phosphodiest; 1.
DR SUPFAM; SSF53649; Alkaline phosphatase-like; 1.
PE 4: Predicted;
KW Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000000267};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 112..130
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT REGION 665..735
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 681..715
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 835 AA; 95551 MW; E49824EDE851C99D CRC64;
MTTDVDSFEI EGDDHNDEHI LSNEDLEFTD YSGGGSGGQW WRNVKYWFYR NRLYWQNGGG
LNDRINESSG RGIPLYDLDG NGDRLNDDSN EFITPQKKYF GRHNWIVRKG PVIKLLLAIF
ILVMPATLLL RDTFKTDYSH RSFTNGNSNS LVDIMKVHEF DPYMKYNNGT NDFYPMTIVI
SLDGFHPSLV SERYTPFLHQ LFTLELDGYN ITSTPYMIPS FPTQTFPNHW TLVTGEYPIE
HGIVSNLFWD SKLDLEFSPS IMDPLIWVNA SEPIWQTVQS AFAKKSSHSD FPFKVATHMW
PGSFVNYTKL DYVPKERMPY YADEFNPSEP LDKKLSKIME YIDIDSIHDR PQMILNYIPN
IDAFGHAHGY PMSTRDGVDE EDTKVGKKFA AMLTEVDTYI QNLFERIEER NMESFTNIVI
LSDHGMSDIK IPENAIVWEN LLDSKTRKSH VSHVYFEGPM LALYMNKVED TNKVYQELKA
NLNEHLLSPY FKIYLNGQFP EGLDFNGGTN DAMGKRRVAP IWIVPEPGFA IMSKSSLKGK
ETIIGSHGYD KNSIDMRALF IGVGPYFNHG YVESFENIEI YKLLCDICGV SPKDRHVHER
QKKVTDDKSK SKDVYDIGAD IFALEDDIEL LVEDDFDYLS ERFGPWSSYN YIWGGFDAWK
DPAEYDEVNS EGEGSQEYDE QNEGQNENQN ENQNEDQNEN QNENQNENQN ENQNEGQEEG
QEEGQNNEQN NEQNNNEKSI ANESSALSIT TPFSSIVPTT LTTEIMTSHS TYSSAVSSAL
PKTDTSETSN SSNGGGFFGW LDDILGDAMN WYDDTKEIID DVVEDIEDLV SPSAK
//
