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Database: UniProt
Entry: A0A364L251_9EURO
LinkDB: A0A364L251_9EURO
Original site: A0A364L251_9EURO 
ID   A0A364L251_9EURO        Unreviewed;      1035 AA.
AC   A0A364L251;
DT   07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT   07-NOV-2018, sequence version 1.
DT   13-SEP-2023, entry version 17.
DE   RecName: Full=Cytomegalovirus gH-receptor family protein {ECO:0008006|Google:ProtNLM};
GN   ORFNames=BHQ10_005882 {ECO:0000313|EMBL:RAO69870.1};
OS   Talaromyces amestolkiae.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Trichocomaceae; Talaromyces;
OC   Talaromyces sect. Talaromyces.
OX   NCBI_TaxID=1196081 {ECO:0000313|EMBL:RAO69870.1, ECO:0000313|Proteomes:UP000249363};
RN   [1] {ECO:0000313|EMBL:RAO69870.1, ECO:0000313|Proteomes:UP000249363}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CIB {ECO:0000313|EMBL:RAO69870.1,
RC   ECO:0000313|Proteomes:UP000249363};
RX   PubMed=28649280; DOI=10.1186/s13068-017-0844-7;
RA   de Eugenio L.I., Mendez-Liter J.A., Nieto-Dominguez M., Alonso L.,
RA   Gil-Munoz J., Barriuso J., Prieto A., Martinez M.J.;
RT   "Differential ?-glucosidase expression as a function of carbon source
RT   availability in Talaromyces amestolkiae: a genomic and proteomic
RT   approach.";
RL   Biotechnol. Biofuels 10:161-161(2017).
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC       pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
CC   -!- SIMILARITY: Belongs to the TAPT1 family.
CC       {ECO:0000256|ARBA:ARBA00008803}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:RAO69870.1}.
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DR   EMBL; MIKG01000010; RAO69870.1; -; Genomic_DNA.
DR   STRING; 1196081.A0A364L251; -.
DR   OrthoDB; 1215898at2759; -.
DR   Proteomes; UP000249363; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR   InterPro; IPR008010; Tatp1.
DR   PANTHER; PTHR13317:SF4; TRANSMEMBRANE ANTERIOR POSTERIOR TRANSFORMATION PROTEIN 1 HOMOLOG; 1.
DR   PANTHER; PTHR13317; UNCHARACTERIZED; 1.
DR   Pfam; PF05346; DUF747; 1.
PE   3: Inferred from homology;
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000249363};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        885..912
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   REGION          1..194
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          219..309
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          436..493
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          930..958
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        38..54
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        66..94
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        139..154
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        171..185
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        219..274
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        283..297
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        446..464
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        467..481
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        934..958
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1035 AA;  116094 MW;  BD060602639E94BE CRC64;
     MMAPIEAPET HQESKNDLLT LQEISVPPRA ALXDLGSGPN SSLPTNGNSS SKKAQETEVQ
     REWDQVASHI RSNGSKHGVD VQPTGSGVTA SSNGESHDEQ ERTRQSSSHG LGIQLDGLNV
     NREEDKVTVS LGNGHRSSSP QDRKQDKERV LKLSPTQIKE LISSPDSIPM QKVPEDHERD
     HESTPIPKPL PSIDDMAKAR NRAEFLRSIS GSFYQKRNSK LSNHLDDPPS FLISSEDTPL
     SAPISQRPQA ARMMTSPMTF PRRNSVSDEQ RLNSNPALRS RHKGAPTHID MPERKTLAED
     PNPSPMPQSI PLPPLSIPAY LELELSSSRP SPLYIHRSAK SQFPYESSQV KLERLLNFIL
     LPPALEQVLW FGALACIDSW LYSFTILPLR FAKALYILVS SWILNFYREA QFVCTFIING
     VGRVWRRRLR SSEKMLSDPT HSVQQKEHAE TNGSSANGNT DTRLKSRSNA RKRKTSAQPK
     HRRQKSTPSA LEPDDKADLL KGFLMICTCI ILSSLDASRM YHWIRGQNAI KLYVIYNVLE
     VGDRLLSAIG QDVLECLFSE EALDRGQDGR SKVVRPFWLF LLALTYTTTH ATALFYQVIT
     LNVAVNSYSN ALITLLLSNQ FVEIKSTVFK KFEKENLFQL TCADVVERFQ LWLMLTIIAS
     RNIVETGALT SWFTVGSTVV NQVRSTVTNS TPLTTSPRSS TSILPQSFTF LPSTIFTSLT
     GGANTLLPHF AQVLGPFLIV LGSEMFVDWL KHAYIAKFNN TRPAIYGRFL DVLTKDYYTN
     AFVDQNLTKR MGLAVIPMAC LFFRVSVQTY QMFLQALLPM QASSTEHSAS LTAMHEHYSN
     LPQPSTPPIP FTVQSVMSTS LDRLSWVFNT IVENAIPSPI QSVTFFTIVL VVTGYLILLI
     LKLTLGILLL SFSRSRYKAM KDREQKLYYG AQHDPNGISS SASQEAPEQH RPSHSSTTNA
     VRDYTVEGGR RVGGWGVVEL DEDKRRWIYA DDPDALRKIK EKERAQKDKQ SVKDSGTLLN
     LDGVKRYEMV AKRIW
//
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