ID L2GJ53_COLFN Unreviewed; 1020 AA.
AC L2GJ53;
DT 06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2013, sequence version 1.
DT 24-JAN-2024, entry version 51.
DE RecName: Full=Protein transport protein SEC23 {ECO:0000256|ARBA:ARBA00021212};
DE AltName: Full=Protein transport protein sec23 {ECO:0000256|ARBA:ARBA00013451};
GN ORFNames=CGGC5_15112 {ECO:0000313|EMBL:ELA38420.1};
OS Colletotrichum fructicola (strain Nara gc5) (Anthracnose fungus)
OS (Colletotrichum gloeosporioides (strain Nara gc5)).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Glomerellales; Glomerellaceae; Colletotrichum;
OC Colletotrichum gloeosporioides species complex.
OX NCBI_TaxID=1213859 {ECO:0000313|EMBL:ELA38420.1};
RN [1] {ECO:0000313|EMBL:ELA38420.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Nara gc5 {ECO:0000313|EMBL:ELA38420.1};
RA Gan P.H.P., Ikeda K., Irieda H., Narusaka M., O'Connell R.J., Narusaka Y.,
RA Takano Y., Kubo Y., Shirasu K.;
RT "Genome analysis of Colletotrichum orbiculare and Colletotrichum
RT fructicola.";
RL Submitted (AUG-2012) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Component of the coat protein complex II (COPII) which
CC promotes the formation of transport vesicles from the endoplasmic
CC reticulum (ER). The coat has two main functions, the physical
CC deformation of the endoplasmic reticulum membrane into vesicles and the
CC selection of cargo molecules. {ECO:0000256|ARBA:ARBA00025471}.
CC -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle, COPII-coated vesicle
CC membrane {ECO:0000256|ARBA:ARBA00004299}; Peripheral membrane protein
CC {ECO:0000256|ARBA:ARBA00004299}; Cytoplasmic side
CC {ECO:0000256|ARBA:ARBA00004299}. Endoplasmic reticulum membrane
CC {ECO:0000256|ARBA:ARBA00004397}; Peripheral membrane protein
CC {ECO:0000256|ARBA:ARBA00004397}; Cytoplasmic side
CC {ECO:0000256|ARBA:ARBA00004397}. Golgi apparatus membrane
CC {ECO:0000256|ARBA:ARBA00004255}; Peripheral membrane protein
CC {ECO:0000256|ARBA:ARBA00004255}; Cytoplasmic side
CC {ECO:0000256|ARBA:ARBA00004255}. Membrane
CC {ECO:0000256|ARBA:ARBA00004287}; Peripheral membrane protein
CC {ECO:0000256|ARBA:ARBA00004287}; Cytoplasmic side
CC {ECO:0000256|ARBA:ARBA00004287}.
CC -!- SIMILARITY: Belongs to the SEC23/SEC24 family. SEC23 subfamily.
CC {ECO:0000256|ARBA:ARBA00009210}.
CC -!- SIMILARITY: Belongs to the universal ribosomal protein uL11 family.
CC {ECO:0000256|ARBA:ARBA00010537, ECO:0000256|RuleBase:RU003978}.
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DR EMBL; KB020228; ELA38420.1; -; Genomic_DNA.
DR RefSeq; XP_007272521.1; XM_007272459.1.
DR AlphaFoldDB; L2GJ53; -.
DR STRING; 1213859.L2GJ53; -.
DR EnsemblFungi; ELA38420; ELA38420; CGGC5_15112.
DR HOGENOM; CLU_008658_3_0_1; -.
DR OrthoDB; 5474700at2759; -.
DR GO; GO:0030127; C:COPII vesicle coat; IEA:InterPro.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR GO; GO:1990904; C:ribonucleoprotein complex; IEA:UniProtKB-KW.
DR GO; GO:0005840; C:ribosome; IEA:UniProtKB-KW.
DR GO; GO:0003735; F:structural constituent of ribosome; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0090114; P:COPII-coated vesicle budding; IEA:InterPro.
DR GO; GO:0006886; P:intracellular protein transport; IEA:InterPro.
DR GO; GO:0006412; P:translation; IEA:InterPro.
DR CDD; cd00349; Ribosomal_L11; 1.
DR CDD; cd01478; Sec23-like; 1.
DR CDD; cd11287; Sec23_C; 1.
DR Gene3D; 2.60.40.1670; beta-sandwich domain of Sec23/24; 1.
DR Gene3D; 1.10.10.250; Ribosomal protein L11, C-terminal domain; 1.
DR Gene3D; 3.30.1550.10; Ribosomal protein L11/L12, N-terminal domain; 1.
DR Gene3D; 1.20.120.730; Sec23/Sec24 helical domain; 1.
DR Gene3D; 3.40.20.10; Severin; 1.
DR Gene3D; 3.40.50.410; von Willebrand factor, type A domain; 1.
DR Gene3D; 2.30.30.380; Zn-finger domain of Sec23/24; 1.
DR HAMAP; MF_00736; Ribosomal_L11; 1.
DR InterPro; IPR029006; ADF-H/Gelsolin-like_dom_sf.
DR InterPro; IPR007123; Gelsolin-like_dom.
DR InterPro; IPR036180; Gelsolin-like_dom_sf.
DR InterPro; IPR000911; Ribosomal_uL11.
DR InterPro; IPR020783; Ribosomal_uL11_C.
DR InterPro; IPR036769; Ribosomal_uL11_C_sf.
DR InterPro; IPR020785; Ribosomal_uL11_CS.
DR InterPro; IPR020784; Ribosomal_uL11_N.
DR InterPro; IPR036796; Ribosomal_uL11_N_sf.
DR InterPro; IPR037364; Sec23.
DR InterPro; IPR006900; Sec23/24_helical_dom.
DR InterPro; IPR036175; Sec23/24_helical_dom_sf.
DR InterPro; IPR006896; Sec23/24_trunk_dom.
DR InterPro; IPR012990; Sec23_24_beta_S.
DR InterPro; IPR037550; Sec23_C.
DR InterPro; IPR036465; vWFA_dom_sf.
DR InterPro; IPR006895; Znf_Sec23_Sec24.
DR InterPro; IPR036174; Znf_Sec23_Sec24_sf.
DR PANTHER; PTHR11141; PROTEIN TRANSPORT PROTEIN SEC23; 1.
DR PANTHER; PTHR11141:SF0; PROTEIN TRANSPORT PROTEIN SEC23; 1.
DR Pfam; PF00626; Gelsolin; 1.
DR Pfam; PF00298; Ribosomal_L11; 1.
DR Pfam; PF03946; Ribosomal_L11_N; 1.
DR Pfam; PF08033; Sec23_BS; 1.
DR Pfam; PF04815; Sec23_helical; 1.
DR Pfam; PF04811; Sec23_trunk; 1.
DR Pfam; PF04810; zf-Sec23_Sec24; 1.
DR SMART; SM00649; RL11; 1.
DR SUPFAM; SSF81995; beta-sandwich domain of Sec23/24; 1.
DR SUPFAM; SSF82754; C-terminal, gelsolin-like domain of Sec23/24; 1.
DR SUPFAM; SSF81811; Helical domain of Sec23/24; 1.
DR SUPFAM; SSF54747; Ribosomal L11/L12e N-terminal domain; 1.
DR SUPFAM; SSF46906; Ribosomal protein L11, C-terminal domain; 1.
DR SUPFAM; SSF53300; vWA-like; 1.
DR SUPFAM; SSF82919; Zn-finger domain of Sec23/24; 1.
DR PROSITE; PS00359; RIBOSOMAL_L11; 1.
PE 3: Inferred from homology;
KW Cytoplasmic vesicle {ECO:0000256|ARBA:ARBA00023329};
KW Endoplasmic reticulum {ECO:0000256|ARBA:ARBA00022824};
KW ER-Golgi transport {ECO:0000256|ARBA:ARBA00022892};
KW Golgi apparatus {ECO:0000256|ARBA:ARBA00023034};
KW Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Protein transport {ECO:0000256|ARBA:ARBA00022927};
KW Ribonucleoprotein {ECO:0000256|ARBA:ARBA00023274,
KW ECO:0000256|RuleBase:RU003978};
KW Ribosomal protein {ECO:0000256|ARBA:ARBA00022980,
KW ECO:0000256|RuleBase:RU003978}; Transport {ECO:0000256|ARBA:ARBA00022448};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 60..99
FT /note="Zinc finger Sec23/Sec24-type"
FT /evidence="ECO:0000259|Pfam:PF04810"
FT DOMAIN 127..393
FT /note="Sec23/Sec24 trunk"
FT /evidence="ECO:0000259|Pfam:PF04811"
FT DOMAIN 404..508
FT /note="Sec23/Sec24 beta-sandwich"
FT /evidence="ECO:0000259|Pfam:PF08033"
FT DOMAIN 522..620
FT /note="Sec23/Sec24 helical"
FT /evidence="ECO:0000259|Pfam:PF04815"
FT DOMAIN 636..723
FT /note="Gelsolin-like"
FT /evidence="ECO:0000259|Pfam:PF00626"
FT DOMAIN 868..924
FT /note="Large ribosomal subunit protein uL11 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF03946"
FT DOMAIN 929..998
FT /note="Large ribosomal subunit protein uL11 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00298"
SQ SEQUENCE 1020 AA; 113192 MW; C5BA5A02B9D42A53 CRC64;
MDYEALKEQW SEVEDRDGVR LSWNVFPSSR MEASRLVVPI GALYTPLKEK PDTPLLQFEP
VTCKQPCRSV LNPFCSVDVR ARLWICPFCL SRNPLPPHYK DITANAIPPE LHPSNTTIEY
RLSRPAPSPP IFLMVVDTCQ EEDSLAALKE SLVMSLSLLP ENALVGLITY GTMAQVHEIG
YTECAKSYVF RGSKDYNAKQ VQEMLGLLSP AMRPGMPQQP GRPMPAGPAS RFLLPVQQAE
FQLTKALEQL QKDPWPVAND RRNLRCTGVA LSVAVGLLES SFQHAGGRIM LFAGGPATEG
PGMVVGPELR EPMRSHHDID RDNIKYYKKA LKFYDNLAKR TAHNGHVIDI FAGCLDQVGL
LEMKGLCQQT GGSMVLTDSF TSSMFKQSFI RMFEKDGDDN LLMGFNATLE VLTTKELKVT
GLIGHAISLN KKSTSVGETE CGIGNTCSWK MCGIDPGSSY GVYFEIAGQG GPAQHQQTPQ
KGMMQFLTYY QHSSGQFHLR VTTIARNLSG PAGDPAIAQS FDQEAAAVLM ARIAVFKAEV
DDGPDVLRWV DRMLIRLCSR FADYRKDDPS SFRLEKNFTL YPQFMFHLRR SQFLQVFNNS
PDETAFYRHV LNHEDVSNSL IMIQPTLDSY TFDQAEASPV LLDSSSIQPT HILLLDTFFH
ILIFHGETIA EWMKAGYQEQ EGYENFAALL EQPKEDARDL ITDRFPLPRF IVCNQGGSQA
RFLLSKLNPS TTHTTGAYGG VGAQNAQTIF TDDVSLQTFM DHLMKLAKLE CYKSYPGYRC
GRTLKKIAPP PPASKKAHFN DRTCGWWLVA EVFKRLLKAA ETAHTSAKFP RPSHSVSIFL
RSPTFPPDPD PRAVKMPPKF DPNEVKVIHL RATGGEVGAS SALAPKIGPL GLSPKKVGED
IAKATGDWKG LRVTVKLTIQ NRQAAVSVVP TASSLIIRAL KEPPRDRKKE KNIKHSKSVA
LDEIIEIART MRYKSFSKDL AGTVKEILGT AYSVGCQVDG KPPQAIIDAI QSGEIDIPEE
//
