ID A0A0D2VT57_CAPO3 Unreviewed; 1296 AA.
AC A0A0D2VT57;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 13-SEP-2023, entry version 31.
DE RecName: Full=PX domain-containing protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=CAOG_005050 {ECO:0000313|EMBL:KJE94407.1};
OS Capsaspora owczarzaki (strain ATCC 30864).
OC Eukaryota; Filasterea; Capsaspora.
OX NCBI_TaxID=595528 {ECO:0000313|EMBL:KJE94407.1, ECO:0000313|Proteomes:UP000008743};
RN [1] {ECO:0000313|Proteomes:UP000008743}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=ATCC 30864 {ECO:0000313|Proteomes:UP000008743};
RA Russ C., Cuomo C., Burger G., Gray M.W., Holland P.W.H., King N.,
RA Lang F.B.F., Roger A.J., Ruiz-Trillo I., Young S.K., Zeng Q., Gargeya S.,
RA Alvarado L., Berlin A., Chapman S.B., Chen Z., Freedman E., Gellesch M.,
RA Goldberg J., Griggs A., Gujja S., Heilman E., Heiman D., Howarth C.,
RA Mehta T., Neiman D., Pearson M., Roberts A., Saif S., Shea T., Shenoy N.,
RA Sisk P., Stolte C., Sykes S., White J., Yandava C., Haas B., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Capsaspora owczarzaki ATCC 30864.";
RL Submitted (FEB-2011) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the sorting nexin family.
CC {ECO:0000256|ARBA:ARBA00010883}.
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DR EMBL; KE346367; KJE94407.1; -; Genomic_DNA.
DR RefSeq; XP_004346735.2; XM_004346685.2.
DR STRING; 595528.A0A0D2VT57; -.
DR EnsemblProtists; KJE94407; KJE94407; CAOG_005050.
DR GeneID; 14897528; -.
DR eggNOG; KOG2101; Eukaryota.
DR InParanoid; A0A0D2VT57; -.
DR OrthoDB; 2877434at2759; -.
DR PhylomeDB; A0A0D2VT57; -.
DR Proteomes; UP000008743; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0035091; F:phosphatidylinositol binding; IEA:InterPro.
DR CDD; cd06093; PX_domain; 1.
DR Gene3D; 3.30.1520.10; Phox-like domain; 1.
DR Gene3D; 1.10.167.10; Regulator of G-protein Signalling 4, domain 2; 1.
DR InterPro; IPR003114; Phox_assoc.
DR InterPro; IPR001683; PX_dom.
DR InterPro; IPR036871; PX_dom_sf.
DR InterPro; IPR016137; RGS.
DR InterPro; IPR036305; RGS_sf.
DR InterPro; IPR044926; RGS_subdomain_2.
DR InterPro; IPR013937; Sorting_nexin_C.
DR PANTHER; PTHR22775; SORTING NEXIN; 1.
DR PANTHER; PTHR22775:SF44; SORTING NEXIN-14; 1.
DR Pfam; PF08628; Nexin_C; 1.
DR Pfam; PF00787; PX; 1.
DR Pfam; PF02194; PXA; 1.
DR Pfam; PF00615; RGS; 1.
DR SMART; SM00312; PX; 1.
DR SMART; SM00313; PXA; 1.
DR SMART; SM00315; RGS; 1.
DR SUPFAM; SSF64268; PX domain; 1.
DR SUPFAM; SSF48097; Regulator of G-protein signaling, RGS; 1.
DR PROSITE; PS50195; PX; 1.
DR PROSITE; PS51207; PXA; 1.
DR PROSITE; PS50132; RGS; 1.
PE 3: Inferred from homology;
KW Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000008743};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 115..148
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 248..436
FT /note="PXA"
FT /evidence="ECO:0000259|PROSITE:PS51207"
FT DOMAIN 481..614
FT /note="RGS"
FT /evidence="ECO:0000259|PROSITE:PS50132"
FT DOMAIN 893..1029
FT /note="PX"
FT /evidence="ECO:0000259|PROSITE:PS50195"
FT REGION 1..98
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 623..672
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 690..721
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 733..884
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 20..43
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 78..98
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 623..637
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 657..672
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 738..877
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1296 AA; 140514 MW; 7ECCEDEB244BAEA7 CRC64;
MDDDEVDQSQ SQRQSQSQSD VDHTADHHDH PQNDKEDAAH CHDTDTTPVA ALDSQQEAEA
EAQEAAAHKR SQAEPAQAYK HTAATTDDNP ETNTATNATV VAAGTRRRLV GATSLVVLAI
ATAAAFSSVL LHPSTLIVVA VAGAYALVRV AQDGRLPSLL SWVTIARPSS RSQAPLLPAT
TANAAAAVCA VCQSDKCNHA DRLVKRNGGV TAQSSASLAG APGGLPAMAY AQSGSSGLTS
FTGAVQVPET LDRAVRLYLD KLLADYVDYW FTPISADTLF LDELRSTLRF VVLGMVDRGC
KVDWEAVACT DMLQVAAELL HAYMCALEDL KQQKRANPTR SHFISDQEMA SATLKRLPNG
GHICMQSPEL ELEYWRKISD RLASLLMPAP LPDCQSAQHL LREMFAAKVL VPSLPAIYDT
DFVNRMLYKA LCEYVPFDGP VMDGPITRLR RPDYHTVPPT QAVLLAGYGG GSPLASVLHV
ALPDILSQPP LLFVFMKFLG TQQALHILQF CLSVENYNEQ AVQATRADPE QQEALATQAK
DLFKMYIKPV GISALPVEDA ERVRIERLIF GQEESGRRFP DATCFMTTYS TCYKLLAEVY
CPLFQRSEMY FKFLCHDSKA LSGQTPTQSQ AVRPVTRQAV APTSRAPLRG AAPPMSAATG
QHSNTNAATK PSKMATFKAK NGVGLQTSAV PIPVTKSGSN NNNNNNGSLP RTPTVLSSSP
YALSSGIPSA IAGSSRRLEH ARTSSTSSSA SDPVAPLSEA GNVESTDSLA VSQSPPLRDA
TEGATTDDLS PSASVGPSAL ASTAHSQDVS LAASPVESRA HSRSHSRSTS AVSLAGVESA
VQQQQMPPRQ TSNPSNSPSR PLTPVAATLG STPPTLPHPT SDLAPVRQGI DMKRWRIAIR
NVSTQRENLK KYVLYRIAVT APMNTLQQVV DPSSIAEYAS MPGRDEETWI VSRRYSDFDA
LDTCLRNSSY GDQGQLELPG KKTFGNMDAN FVDTRRASLE KYLQALIADV NLHESVLLHA
FFTPTPTFRQ LIHDLNDHDV SRVLKAVPQK IKEISVGIVS APMQWFSEAG NRARELEGAV
QSFVPSLPAA LFDWQQHRFQ RKRAAARLNE DVTSASNDRT QNLTISGPME TALFVLENAA
DVPRSRWNAA ASPPAERAPA STPGLPLLLA LGKFAAGATF DDFIERKLRD NIEFQLRENS
ALDLLQLLYA ATFDAAPVVT DEERARNKQI AYDEMFKFLP PIAHHIVGVE YLRNCAENFF
ELLQNPQLSK QLVLSVLDIT IVKFFPELSA SATPIP
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