ID A0A077ZPH8_STYLE Unreviewed; 904 AA.
AC A0A077ZPH8;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE RecName: Full=PH domain-containing protein {ECO:0000259|PROSITE:PS50003};
GN Name=Contig11339.g12118 {ECO:0000313|EMBL:CDW71808.1};
GN ORFNames=STYLEM_758 {ECO:0000313|EMBL:CDW71808.1};
OS Stylonychia lemnae (Ciliate).
OC Eukaryota; Sar; Alveolata; Ciliophora; Intramacronucleata; Spirotrichea;
OC Stichotrichia; Sporadotrichida; Oxytrichidae; Stylonychinae; Stylonychia.
OX NCBI_TaxID=5949 {ECO:0000313|EMBL:CDW71808.1, ECO:0000313|Proteomes:UP000039865};
RN [1] {ECO:0000313|EMBL:CDW71808.1, ECO:0000313|Proteomes:UP000039865}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=130c {ECO:0000313|EMBL:CDW71808.1,
RC ECO:0000313|Proteomes:UP000039865};
RA Swart Estienne;
RL Submitted (JUN-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: Belongs to the LIMR family.
CC {ECO:0000256|ARBA:ARBA00010487}.
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DR EMBL; CCKQ01000717; CDW71808.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A077ZPH8; -.
DR EnsemblProtists; CDW71808; CDW71808; STYLEM_758.
DR InParanoid; A0A077ZPH8; -.
DR OrthoDB; 5644416at2759; -.
DR Proteomes; UP000039865; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 1.
DR InterPro; IPR006876; LMBR1-like_membr_prot.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR001849; PH_domain.
DR PANTHER; PTHR21355:SF0; G-PROTEIN COUPLED RECEPTOR-ASSOCIATED PROTEIN LMBRD2; 1.
DR PANTHER; PTHR21355; UNCHARACTERIZED; 1.
DR Pfam; PF04791; LMBR1; 1.
DR Pfam; PF00169; PH; 1.
DR SMART; SM00233; PH; 1.
DR SUPFAM; SSF50729; PH domain-like; 1.
DR PROSITE; PS50003; PH_DOMAIN; 1.
PE 3: Inferred from homology;
KW Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000039865};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 20..42
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 98..121
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 133..156
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 329..354
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 360..379
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 406..428
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 778..892
FT /note="PH"
FT /evidence="ECO:0000259|PROSITE:PS50003"
FT REGION 452..472
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 511..609
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 641..785
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 511..535
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 536..564
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 565..581
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 583..609
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 641..668
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 689..703
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 719..736
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 748..762
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 763..785
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 904 AA; 103906 MW; ACA7490A1D658091 CRC64;
MSLQNLKDRF IQYASTRKGL AVVSWSIGGL LIVILAASIA HINVTSQMAV MVASTFIRKA
SNANGYIMEY HLLGIADSWN NTKQIFLQIL VKWSFFSLWP YQAFIQTGGC VFSILIFSIY
YKFGFQGLNG VKAVAMIMLN IYGMLQMVVL LAYGLFNLPV FLWKRADNQN KLYSELECAD
QVRQQYRQAM ADFQMFVIEC RNLIRNHRNG YNSIFMDILE EELPEKDLEG QSIMQSNNFM
MAMKDGQAVT EDFLANIRYQ LKVQFFLYKR KKARWVSLFE TVDELVQKPI NYELIKEKID
KKNVIEKEQN VSLEEMILKP LPNNKRKILI FRSLAIISLL YCIIVLSTEG LVVFEPSYTL
LYQTVSCFNY MIIIGEMAIG KDVDPFGTSY CDFYSSMIRV PLFGQYFNNI MSLFILLIGG
VFALLSFFKY QNKALSAFKN YSKKVEEQVE KLQKKKDKDE KSGNTQKKKD DEIKPIGKSE
LEIIERILKG EKAILAEYEI TRRKDERNKL TRINHGDDIE MQKANEGKAT KKKPSNNELN
KSNLKNAGDT SSLSVNAIDK GKKKSSNLSV NKDDKKQPLL QKKKTQNIKS SSESESSISN
NSNPQQAKRQ IGKLNPNAIS KFQPISAQNK IHYGMLRKAK IEEENEAKPA KQIESDDEIK
EETKKPNQKK QGTNNISQNA KSKNNEKKPR KKITISSDSD ESDKKESDDS DDEDETQQLS
QPKNLLKKNN QALGKKNNDV GDFRSKLALK RNQQNSNKQQ SDKALKSKGK NKKTNKNDSE
KEGYLLKRKG KRIRKIWVKR YAALEGSNLN FYDNEDKENL IKTIDVTQIK AVTFHYDAEA
PVQSKNITKK DKEESRFDLY SIIKNKKYKF KTEDDNVWDS QGWVDALKKI VDENFDDSDD
SDSS
//
