ID V9EN57_PHYPR Unreviewed; 1255 AA.
AC V9EN57;
DT 19-FEB-2014, integrated into UniProtKB/TrEMBL.
DT 19-FEB-2014, sequence version 1.
DT 27-MAR-2024, entry version 42.
DE RecName: Full=VASt domain-containing protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=F443_14030 {ECO:0000313|EMBL:ETI40669.1};
OS Phytophthora parasitica P1569.
OC Eukaryota; Sar; Stramenopiles; Oomycota; Peronosporales; Peronosporaceae;
OC Phytophthora.
OX NCBI_TaxID=1317065 {ECO:0000313|EMBL:ETI40669.1, ECO:0000313|Proteomes:UP000018721};
RN [1] {ECO:0000313|EMBL:ETI40669.1, ECO:0000313|Proteomes:UP000018721}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=P1569 {ECO:0000313|EMBL:ETI40669.1,
RC ECO:0000313|Proteomes:UP000018721};
RG The Broad Institute Genomics Platform;
RA Russ C., Tyler B., Panabieres F., Shan W., Tripathy S., Grunwald N.,
RA Machado M., Johnson C.S., Arredondo F., Hong C., Coffey M., Young S.K.,
RA Zeng Q., Gargeya S., Fitzgerald M., Abouelleil A., Alvarado L.,
RA Chapman S.B., Gainer-Dewar J., Goldberg J., Griggs A., Gujja S., Hansen M.,
RA Howarth C., Imamovic A., Ireland A., Larimer J., McCowan C., Murphy C.,
RA Pearson M., Poon T.W., Priest M., Roberts A., Saif S., Shea T., Sykes S.,
RA Wortman J., Nusbaum C., Birren B.;
RT "The Genome Sequence of Phytophthora parasitica P1569.";
RL Submitted (NOV-2013) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004167}; Single-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004167}.
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:ETI40669.1}.
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DR EMBL; ANIZ01002432; ETI40669.1; -; Genomic_DNA.
DR AlphaFoldDB; V9EN57; -.
DR EnsemblProtists; ETI40669; ETI40669; F443_14030.
DR HOGENOM; CLU_006848_0_0_1; -.
DR OrthoDB; 54126at2759; -.
DR Proteomes; UP000018721; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0043226; C:organelle; IEA:UniProt.
DR CDD; cd13220; PH-GRAM_GRAMDC; 1.
DR Gene3D; 1.20.1270.60; Arfaptin homology (AH) domain/BAR domain; 2.
DR Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 1.
DR InterPro; IPR027267; AH/BAR_dom_sf.
DR InterPro; IPR031160; F_BAR.
DR InterPro; IPR001060; FCH_dom.
DR InterPro; IPR004182; GRAM.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR031968; VASt.
DR PANTHER; PTHR23065:SF7; CYTOKINESIS PROTEIN 2; 1.
DR PANTHER; PTHR23065; PROLINE-SERINE-THREONINE PHOSPHATASE INTERACTING PROTEIN 1; 1.
DR Pfam; PF00611; FCH; 1.
DR Pfam; PF02893; GRAM; 1.
DR Pfam; PF16016; VASt; 1.
DR SMART; SM00568; GRAM; 1.
DR SUPFAM; SSF103657; BAR/IMD domain-like; 2.
DR PROSITE; PS51741; F_BAR; 1.
DR PROSITE; PS51778; VAST; 1.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|PROSITE-ProRule:PRU01077, ECO:0000256|SAM:Coils};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000018721};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 1195..1215
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 29..329
FT /note="F-BAR"
FT /evidence="ECO:0000259|PROSITE:PS51741"
FT DOMAIN 953..1132
FT /note="VASt"
FT /evidence="ECO:0000259|PROSITE:PS51778"
FT REGION 1..35
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 185..206
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 685..765
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 877..947
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1128..1192
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 542..576
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 185..202
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 685..714
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 715..733
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 741..758
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 877..904
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 907..946
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1128..1159
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1167..1192
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1255 AA; 139952 MW; 4F5C84975C8E7B04 CRC64;
MTSDSSPNHG GVSPTAKSEE GSVASPRSSQ TEGTYSTDLF QSFPKVCQKA KSGVQLCQAV
SAFVIERAGL ESNYAQSLLK LAQSAKAEDW SKQFTECWAT FQEATEHLAQ ERWAFAQTMQ
TSIVPGAKAF AAQQETQVHR LVSEGTKVRW AQQQVISSME KAKEKYDRKC QEAIEITTAM
RKSDNSTLAD VNSSSSDSSD EVSASKELTD KLAAGAGQLL TKMWDTTSSF GRNPLERQRS
KLYSSLEDVI AAEKHYVHTV DYTNAQRLIF EREIKENLHA FQLTEEQRLE YLRDVLMRMQ
KAFISMFSRS QQFVERMKAS ANKVDELADI EKGFQSLGGQ DEIDVDRADL STNPSYLRMT
HIQEMSDTGH RMVGIINSVV TEFIASETRF SHSLRKLLRL HENGGHAPPT DLFGTSSNTM
NFLSDEGASM ANGWMAVKDQ VKLLLEVHQE FRSLLAEPVS LSLATMKSEY ESVRVTTQES
FSKLHSSLCN EAGAHKKLHQ KLDTKARDFV MTFSYLPGAT PVATNSYGID VTQALMVLSA
NARLFNEKER RSEAKLRQLA EEIRQLQAQA TESTKVLKQT YQNYVQEIEV FISTCMKNEK
YRLQVGKNSL QSLAKAVEHM LQGGASVGNK ALIEFEKIDP STDMAEFIRI NRQPYERTKR
IVPAYHGNDN LKEAMREYLS SLRAPSSITS ENSDNNPRSR TSSFSPFGEI NASSEKKSPR
TRVRQEGDDH TATANENGAD GSLSDEDESE DSGTEQEEEF TESQPLGVSD FQKKFKLDSP
EQVVESFSCA LYLSNFPYHG RLYLTRDRMC FSGWMDTIFV ASFSDISAME KKNTALIVPN
AIELTVKGEK IFFASFVFRD ECYQSIQQLR SIKKETEELM SDPANHSDPE TTDSESRRRR
SSKDLAAVAP SSESSSTDAT PVDDNRPPSS FSSKTMASTP PTNIPDKDTL LSEYDILMDE
EVEFSVETAY STLWIESDTF SRNLLEAAGA TNISLPAWEK KSTSYTAVAT PDTFDGSRVV
SYTHNKKYMV GPSVIPTTQT QRYAYTPGSR LVVSTTTCVS DVPYCDYFRV EHRWVFSATK
NRGMCLAQVG LRVQWSKNTW LKKQIESTTV TEAKDAVKAW LNAALDATKE QTSTGSSSKS
PAPANKPSEQ PSESVSTRDA PPKEPTKEVD SSTSSSSTAP NKAASTSSNG LPAQLHPTIQ
AAIIICALMF VYTMYRVCAA MNQMQALTRE SLVQQRQQHE LLKELLEKLG STRER
//
