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Database: UniProt
Entry: M3JA88_CANMX
LinkDB: M3JA88_CANMX
Original site: M3JA88_CANMX 
ID   M3JA88_CANMX            Unreviewed;      1026 AA.
AC   M3JA88;
DT   01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT   01-MAY-2013, sequence version 1.
DT   27-MAR-2024, entry version 37.
DE   SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:EMG49023.1};
GN   ORFNames=G210_0303 {ECO:0000313|EMBL:EMG49023.1};
OS   Candida maltosa (strain Xu316) (Yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX   NCBI_TaxID=1245528 {ECO:0000313|EMBL:EMG49023.1, ECO:0000313|Proteomes:UP000011777};
RN   [1] {ECO:0000313|EMBL:EMG49023.1, ECO:0000313|Proteomes:UP000011777}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Xu316 {ECO:0000313|Proteomes:UP000011777};
RA   Yu J., Wang Q., Geng X., Bao W., He P., Cai J.;
RT   "Genome sequence of Candida maltosa Xu316, a potential industrial strain
RT   for xylitol and ethanol production.";
RL   Submitted (FEB-2013) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the sorting nexin family.
CC       {ECO:0000256|ARBA:ARBA00010883}.
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:EMG49023.1}.
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DR   EMBL; AOGT01000862; EMG49023.1; -; Genomic_DNA.
DR   AlphaFoldDB; M3JA88; -.
DR   STRING; 1245528.M3JA88; -.
DR   eggNOG; KOG2101; Eukaryota.
DR   HOGENOM; CLU_002131_1_0_1; -.
DR   OMA; AMYVVEV; -.
DR   OrthoDB; 5392990at2759; -.
DR   Proteomes; UP000011777; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0043226; C:organelle; IEA:UniProt.
DR   GO; GO:0035091; F:phosphatidylinositol binding; IEA:InterPro.
DR   CDD; cd06876; PX_MDM1p; 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:SF3; SORTING NEXIN-13; 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:UP000011777};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        6..23
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        30..50
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          97..287
FT                   /note="PXA"
FT                   /evidence="ECO:0000259|PROSITE:PS51207"
FT   DOMAIN          348..482
FT                   /note="RGS"
FT                   /evidence="ECO:0000259|PROSITE:PS50132"
FT   DOMAIN          677..799
FT                   /note="PX"
FT                   /evidence="ECO:0000259|PROSITE:PS50195"
FT   REGION          542..590
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1026 AA;  119134 MW;  9DB1D362178F7CC7 CRC64;
     MVNYLSYKVL IWGTILLISF LSIKANSLSL IFSFISGAFI LILVSGYYSI KLRQSSPKLH
     KSYTRRFKFT YPEKWTREII ELQNDSVTIK QPIFPESFLI SETVQELIDL IIGEFITPWY
     SQITSSTLVT EDISLEIKTV VRNLQERLRD LDFAQLLVSN ILPLIQEHFE SFIHAQEVVR
     SQGKFNKFDS NEYHLAVISQ YRRGKLHPAV TVSSAHEESN FKEKQYLRKK IESILPYLLS
     KNEKNNEVGV NLVTEILSCT VLCNVFNLLT ESDFYNLMIV KLIGDNLRRR DQVKQLRAAL
     EEHTKTNKVP ELNESILLSQ STSDLNLQNK LKTKINQQKT TTAKLVLKLN DILFDQNNLK
     IFKEFMNSRG RLKYVEFWEE VEQIKVPLEG AENEDPLALS LEFGDNDDVI KVFDKYLANG
     DIPYADSSGV FTKLSNPNEE LKTKTYQECR VELFKIQNEV FEEMERTDLP LFNASDVYEK
     LINQSKSTEI NSDVIHAVEN AFTQIMSKPN VTDMVDFNGN DDNYDKLLST IQLKKDIFGD
     SSNYGSEENL SNRNSRLFDD DLSDEDNSDT DSDSLHSDRP SQNSTILTSS DSEVQFAAPG
     NLNLAEEIPK LTEQVEDLHR QITVLDPLIN KAELTNNVSE LKLLQKLKVG MIREINFKEL
     QKQQYIVQEN DNSLYGKSKV CIQSYITDNE KSGKEFTLYI IEVQKFSRED PNVIKAGWVV
     ARRFSQFYRL HEYLKSRYNR VGYLKFPKKS ISVLKFQQKQ VVEIRQRQLE EYLQELIKIQ
     EVCSDKAFRS FLSSENFNLK KNQRFDERKE SSHNNNYQLL FGSKWYRGIP IFMNSPKPNN
     TNLGETVMDL GIMENIKDME TELKQFDESA STKAPFVKPI CDLLITVFKL HSSKSWLRGR
     ALVVILQQIL GTTVEKKVYD MVESQLKREE SILDLVIMLK NLLFPNGKFK DPPVIRSLYQ
     QSNTRQEAKM LMEIFIYDTC SRIFGSHNSI FASNEVFKML QNDYLNRHLI YEIFDEIIKQ
     LFPEVD
//
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