ID G9NZE9_HYPAI Unreviewed; 1061 AA.
AC G9NZE9;
DT 22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT 22-FEB-2012, sequence version 1.
DT 27-MAR-2024, entry version 56.
DE SubName: Full=Sfb3 protein {ECO:0000313|EMBL:EHK43855.1};
GN ORFNames=TRIATDRAFT_150324 {ECO:0000313|EMBL:EHK43855.1};
OS Hypocrea atroviridis (strain ATCC 20476 / IMI 206040) (Trichoderma
OS atroviride).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Hypocreaceae; Trichoderma.
OX NCBI_TaxID=452589 {ECO:0000313|EMBL:EHK43855.1, ECO:0000313|Proteomes:UP000005426};
RN [1] {ECO:0000313|EMBL:EHK43855.1, ECO:0000313|Proteomes:UP000005426}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 20476 / IMI 206040 {ECO:0000313|Proteomes:UP000005426};
RX PubMed=21501500; DOI=10.1186/gb-2011-12-4-r40;
RA Kubicek C.P., Herrera-Estrella A., Seidl-Seiboth V., Martinez D.A.,
RA Druzhinina I.S., Thon M., Zeilinger S., Casas-Flores S., Horwitz B.A.,
RA Mukherjee P.K., Mukherjee M., Kredics L., Alcaraz L.D., Aerts A., Antal Z.,
RA Atanasova L., Cervantes-Badillo M.G., Challacombe J., Chertkov O.,
RA McCluskey K., Coulpier F., Deshpande N., von Doehren H., Ebbole D.J.,
RA Esquivel-Naranjo E.U., Fekete E., Flipphi M., Glaser F.,
RA Gomez-Rodriguez E.Y., Gruber S., Han C., Henrissat B., Hermosa R.,
RA Hernandez-Onate M., Karaffa L., Kosti I., Le Crom S., Lindquist E.,
RA Lucas S., Luebeck M., Luebeck P.S., Margeot A., Metz B., Misra M.,
RA Nevalainen H., Omann M., Packer N., Perrone G., Uresti-Rivera E.E.,
RA Salamov A., Schmoll M., Seiboth B., Shapiro H., Sukno S.,
RA Tamayo-Ramos J.A., Tisch D., Wiest A., Wilkinson H.H., Zhang M.,
RA Coutinho P.M., Kenerley C.M., Monte E., Baker S.E., Grigoriev I.V.;
RT "Comparative genome sequence analysis underscores mycoparasitism as the
RT ancestral life style of Trichoderma.";
RL Genome Biol. 12:R40.1-R40.15(2011).
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}.
CC -!- SIMILARITY: Belongs to the SEC23/SEC24 family. SEC24 subfamily.
CC {ECO:0000256|ARBA:ARBA00008334}.
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:EHK43855.1}.
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DR EMBL; ABDG02000025; EHK43855.1; -; Genomic_DNA.
DR RefSeq; XP_013942127.1; XM_014086652.1.
DR AlphaFoldDB; G9NZE9; -.
DR STRING; 452589.G9NZE9; -.
DR GeneID; 25776056; -.
DR eggNOG; KOG1984; Eukaryota.
DR HOGENOM; CLU_004589_1_0_1; -.
DR OMA; INPFMTF; -.
DR OrthoDB; 977017at2759; -.
DR Proteomes; UP000005426; Unassembled WGS sequence.
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:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0006888; P:endoplasmic reticulum to Golgi vesicle-mediated transport; IEA:InterPro.
DR GO; GO:0006886; P:intracellular protein transport; IEA:InterPro.
DR Gene3D; 2.60.40.1670; beta-sandwich domain of Sec23/24; 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 InterPro; IPR029006; ADF-H/Gelsolin-like_dom_sf.
DR InterPro; IPR007123; Gelsolin-like_dom.
DR InterPro; IPR036180; Gelsolin-like_dom_sf.
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; IPR036465; vWFA_dom_sf.
DR InterPro; IPR006895; Znf_Sec23_Sec24.
DR InterPro; IPR036174; Znf_Sec23_Sec24_sf.
DR PANTHER; PTHR13803; SEC24-RELATED PROTEIN; 1.
DR PANTHER; PTHR13803:SF4; SECRETORY 24CD, ISOFORM C; 1.
DR Pfam; PF00626; Gelsolin; 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 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; SSF53300; vWA-like; 1.
DR SUPFAM; SSF82919; Zn-finger domain of Sec23/24; 1.
PE 3: Inferred from homology;
KW Cytoplasmic vesicle {ECO:0000256|ARBA:ARBA00023329};
KW ER-Golgi transport {ECO:0000256|ARBA:ARBA00022892};
KW Protein transport {ECO:0000256|ARBA:ARBA00022927};
KW Reference proteome {ECO:0000313|Proteomes:UP000005426};
KW Transport {ECO:0000256|ARBA:ARBA00022448}.
FT DOMAIN 335..373
FT /note="Zinc finger Sec23/Sec24-type"
FT /evidence="ECO:0000259|Pfam:PF04810"
FT DOMAIN 413..659
FT /note="Sec23/Sec24 trunk"
FT /evidence="ECO:0000259|Pfam:PF04811"
FT DOMAIN 666..750
FT /note="Sec23/Sec24 beta-sandwich"
FT /evidence="ECO:0000259|Pfam:PF08033"
FT DOMAIN 772..873
FT /note="Sec23/Sec24 helical"
FT /evidence="ECO:0000259|Pfam:PF04815"
FT DOMAIN 902..967
FT /note="Gelsolin-like"
FT /evidence="ECO:0000259|Pfam:PF00626"
FT REGION 1..98
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 22..39
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 60..97
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1061 AA; 115843 MW; FC89E28E11575E2E CRC64;
MDYTQYHALG HGEPLDPNDP NKTSAPAPQQ FQQSVPPSPY APQAAFGAPQ YGAHQGMPPP
RTPGYGPPMT PGYGPPMTPG YGPQTPGYGP PQSFPGSPMP SQDGVLAAQL GGMNLGADAG
AASARKKKKD RHAYHTVEPT GSSQAFNGLP PGTPAEQFLN VNNPQGIPAL GGQFASPLAS
PQMVNPNQFP VPVGAPFSPA NLASSHEFAE RYLTADDDDE PIGPPTGPVG AGGQLSADDM
PSVPAARDSI QQHFFRNVYP TFERHVPPPA TVSFVAFDQG NSSPKFTRLT LNNIPTTSEG
LHATGLPLGM LIQPLAPLQA DEAEIPVLDY GEAGPPRCRR CRAYINPFMM FRSGGNKFVC
NLCSYPNDTP PEYFCAITPQ GVRLDRDQRP ELHRGTVEFV VPKEYWTREP VGLRWLFVID
VTQESYNKGF VETFCEGILS ALYGGDDEEK DENNEPKRRI PEGAKVGFIT YDKDIHFYNI
NPQLDQAHMM IMPDLEDPFL PLGEGLFVDP YESKAIITSL LTRLPEMFST IKNPEPALLA
TLNSAVAALE ATGGKVICSC SSLPTWGPGR LFMRDDGNHP GGELDKKLYT TEHPAWKKVA
EKMASSGIGI DFFLAAPSGG YLDVATIGHV AATTGGETFY YPNFISPRDG PKLSMEITHA
VTRETGYQGL MKVRCSNGLQ VEGYHGNFVQ HTFGADLEIG VIDADKALGV SFSYDGKLDP
KLDAHFQTAL LYTAASGQRR VRCSNVIASV SDTSKESSTK EQAIRQCMKF ADQDAVIGIL
AKEASTKLAT TSSNLKDIRN WLTERTIDIM ASYRKHSANQ YPPGQLVMPE KLKEYCMYML
GLLKCRAFKG GVENSDRRVH DLRMVRSMGP LELSLYIYPR MIALHNLQPE EGFADAETGH
LKLPPSIRAS FSRVEPGGVY LVDNGQQCLL WLHAQTSPNL ITDLFGEGHD SLKGLDAYTS
SLPVLETHLS AQVRNILEFL KSMRGSKGLT IQLARQGIDG AEYEFARTLV EDRNNEAQSY
VDWLVHVHRG VQLELSGQRK KDDGEATAVM ANFAGLRPSY W
//
