ID G3AEX0_SPAPN Unreviewed; 982 AA.
AC G3AEX0;
DT 16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT 16-NOV-2011, sequence version 1.
DT 27-MAR-2024, entry version 58.
DE SubName: Full=Exocyst complex component SEC10 {ECO:0000313|EMBL:EGW35800.1};
GN ORFNames=SPAPADRAFT_48761 {ECO:0000313|EMBL:EGW35800.1};
OS Spathaspora passalidarum (strain NRRL Y-27907 / 11-Y1).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Spathaspora.
OX NCBI_TaxID=619300 {ECO:0000313|Proteomes:UP000000709};
RN [1] {ECO:0000313|EMBL:EGW35800.1, ECO:0000313|Proteomes:UP000000709}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL Y-27907 / 11-Y1 {ECO:0000313|Proteomes:UP000000709};
RX PubMed=21788494; DOI=10.1073/pnas.1103039108;
RA Wohlbach D.J., Kuo A., Sato T.K., Potts K.M., Salamov A.A., LaButti K.M.,
RA Sun H., Clum A., Pangilinan J.L., Lindquist E.A., Lucas S., Lapidus A.,
RA Jin M., Gunawan C., Balan V., Dale B.E., Jeffries T.W., Zinkel R.,
RA Barry K.W., Grigoriev I.V., Gasch A.P.;
RT "Comparative genomics of xylose-fermenting fungi for enhanced biofuel
RT production.";
RL Proc. Natl. Acad. Sci. U.S.A. 108:13212-13217(2011).
CC -!- SIMILARITY: Belongs to the SEC10 family.
CC {ECO:0000256|ARBA:ARBA00006572}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the eukaryotic
CC ribosomal protein eS31 family. {ECO:0000256|ARBA:ARBA00009891}.
CC -!- SIMILARITY: In the N-terminal section; belongs to the ubiquitin family.
CC {ECO:0000256|ARBA:ARBA00008373}.
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DR EMBL; GL996499; EGW35800.1; -; Genomic_DNA.
DR RefSeq; XP_007373212.1; XM_007373150.1.
DR AlphaFoldDB; G3AEX0; -.
DR STRING; 619300.G3AEX0; -.
DR GeneID; 18871262; -.
DR KEGG; spaa:SPAPADRAFT_48761; -.
DR eggNOG; KOG0004; Eukaryota.
DR eggNOG; KOG3745; Eukaryota.
DR HOGENOM; CLU_008002_1_0_1; -.
DR InParanoid; G3AEX0; -.
DR OMA; PLCKHHY; -.
DR OrthoDB; 10736at2759; -.
DR Proteomes; UP000000709; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0005840; C:ribosome; IEA:InterPro.
DR GO; GO:0003735; F:structural constituent of ribosome; IEA:InterPro.
DR GO; GO:0006887; P:exocytosis; IEA:UniProtKB-KW.
DR GO; GO:0006412; P:translation; IEA:InterPro.
DR CDD; cd01803; Ubl_ubiquitin; 1.
DR Gene3D; 6.20.50.150; -; 1.
DR InterPro; IPR002906; Ribosomal_eS31.
DR InterPro; IPR038582; Ribosomal_eS31_euk-type_sf.
DR InterPro; IPR011332; Ribosomal_zn-bd.
DR InterPro; IPR009976; Sec10-like.
DR InterPro; IPR048627; Sec10_HB.
DR InterPro; IPR048625; Sec10_N.
DR InterPro; IPR000626; Ubiquitin-like_dom.
DR InterPro; IPR029071; Ubiquitin-like_domsf.
DR InterPro; IPR019954; Ubiquitin_CS.
DR InterPro; IPR019956; Ubiquitin_dom.
DR PANTHER; PTHR12100:SF0; EXOCYST COMPLEX COMPONENT 5; 1.
DR PANTHER; PTHR12100; SEC10; 1.
DR Pfam; PF01599; Ribosomal_S27; 1.
DR Pfam; PF07393; Sec10_HB; 1.
DR Pfam; PF20667; Sec10_N; 1.
DR Pfam; PF00240; ubiquitin; 1.
DR PRINTS; PR00348; UBIQUITIN.
DR SMART; SM01402; Ribosomal_S27; 1.
DR SMART; SM00213; UBQ; 1.
DR SUPFAM; SSF54236; Ubiquitin-like; 1.
DR SUPFAM; SSF57829; Zn-binding ribosomal proteins; 1.
DR PROSITE; PS00299; UBIQUITIN_1; 1.
DR PROSITE; PS50053; UBIQUITIN_2; 1.
PE 3: Inferred from homology;
KW Coiled coil {ECO:0000256|ARBA:ARBA00023054, ECO:0000256|SAM:Coils};
KW Exocytosis {ECO:0000256|ARBA:ARBA00022483};
KW Isopeptide bond {ECO:0000256|ARBA:ARBA00022499};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000000709};
KW Ribonucleoprotein {ECO:0000256|ARBA:ARBA00023274};
KW Ribosomal protein {ECO:0000256|ARBA:ARBA00022980};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius};
KW Transport {ECO:0000256|ARBA:ARBA00022448};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT TRANSMEM 141..160
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 1..76
FT /note="Ubiquitin-like"
FT /evidence="ECO:0000259|PROSITE:PS50053"
FT COILED 233..260
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 982 AA; 113177 MW; 375853D57F3A4543 CRC64;
MQIFVKTLTG KTITLEVESS DTIDNVKSKI QDKEGIPPDQ QRLIFAGKQL EDGRTLSDYN
IQKESTLHLV LRLRGGGKKR KKKVYTTPKK IKHKHRKHKL AVLTYYKVDN EGKVERLRRE
CPAPTCGAGI FMADMKTRQY CVLYCLCIFI VWALAVSEIL TPECKHILHM NFSIYELDED
IKKLLNVDNF LNGLSVNDFI EEISKDHLLK DTEVNEFEYL DPKPYIRTFE GILRELKQLK
THANQQKSES ERLVDEYELQ HSENVLELND QITKATEKFD VLDTQISDVS TKINPLGKVL
NKITSSRDRS VETIFLIRAY HGFYTRGSYE QLELLRTSKK IEERVKCAKT VANLITLAKK
IANEHQPTTV KCIETIEQYG QTMEDNLLQT FELASEDGDF DTMKDIASVL FEYNNGINVI
QTFVSKNEIA EQEQQDNSGL VKDEATWTRL SDPNCGDHEI KDEAIESTLD HLRFEIKSRA
WIIRQVFDDP IPVLKIFIQR VYAQIIRNTV TNLLQYSLSV STLAHVRVLH SLSMLVGDFT
KDVKEFLVTN EFERDNELSH VLDQSLIDLF IEYTADEVYF AREKKNLEET IYEIVHKFNT
FHDTVISSGA LATKLENLDN LEFVDKPQAG ENPDKFNFRF SERKRMQQFK SYVKTKLASS
RQSTDLETRT SSRDLEEYAK LNVGKMEIVL KSAIESIARL LELTPTKAPQ YSLEILEILV
IDFGKLYIGS GLEVVYDEMH QEVAKIQSIQ PFDLKYLKAF NVISENLFLL SSCIKKIILP
CATNSPNIKN RMSNLLNSYV SQCEQSLNII LNETLEMLSS RISILLTKQK RRDFYCDEIE
EDTEACELIS DFLIDLQTAL KTTMNSGNLE KIFIKIGMDL LHQLLEHYKK FPVNSIGGIV
LTKDVLRYQS IIDEWGIPEL SEEFQILKEV GNLFTVSSEL VNSLIMEGQL AKMKPYTVRQ
YISKRADFNP GYAERLLKLT NI
//
