ID A0A0L6VHR5_9BASI Unreviewed; 1015 AA.
AC A0A0L6VHR5;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 24-JAN-2024, entry version 27.
DE RecName: Full=Protein transporter SEC24 {ECO:0008006|Google:ProtNLM};
GN ORFNames=VP01_1686g1 {ECO:0000313|EMBL:KNZ59655.1};
OS Puccinia sorghi.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Pucciniomycotina;
OC Pucciniomycetes; Pucciniales; Pucciniaceae; Puccinia.
OX NCBI_TaxID=27349 {ECO:0000313|EMBL:KNZ59655.1, ECO:0000313|Proteomes:UP000037035};
RN [1] {ECO:0000313|EMBL:KNZ59655.1, ECO:0000313|Proteomes:UP000037035}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RO10H11247 {ECO:0000313|EMBL:KNZ59655.1,
RC ECO:0000313|Proteomes:UP000037035};
RA Rochi L., Burguener G., Darino M., Turjanski A., Kreff E., Dieguez M.J.,
RA Sacco F.;
RT "Next Generation Sequencing and Analysis of the Genome of Puccinia sorghi L
RT Schw, the Causal Agent of Maize Common Rust.";
RL Submitted (AUG-2015) to the EMBL/GenBank/DDBJ databases.
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:KNZ59655.1}.
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DR EMBL; LAVV01006488; KNZ59655.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0L6VHR5; -.
DR STRING; 27349.A0A0L6VHR5; -.
DR VEuPathDB; FungiDB:VP01_1686g1; -.
DR OrthoDB; 977017at2759; -.
DR Proteomes; UP000037035; Unassembled WGS sequence.
DR GO; GO:0030127; C:COPII vesicle coat; IEA:InterPro.
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 Protein transport {ECO:0000256|ARBA:ARBA00022927};
KW Reference proteome {ECO:0000313|Proteomes:UP000037035};
KW Transport {ECO:0000256|ARBA:ARBA00022448}.
FT DOMAIN 273..311
FT /note="Zinc finger Sec23/Sec24-type"
FT /evidence="ECO:0000259|Pfam:PF04810"
FT DOMAIN 359..617
FT /note="Sec23/Sec24 trunk"
FT /evidence="ECO:0000259|Pfam:PF04811"
FT DOMAIN 625..709
FT /note="Sec23/Sec24 beta-sandwich"
FT /evidence="ECO:0000259|Pfam:PF08033"
FT DOMAIN 720..820
FT /note="Sec23/Sec24 helical"
FT /evidence="ECO:0000259|Pfam:PF04815"
FT DOMAIN 848..924
FT /note="Gelsolin-like"
FT /evidence="ECO:0000259|Pfam:PF00626"
FT REGION 1..156
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 986..1005
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..54
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 88..103
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 121..152
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1015 AA; 114055 MW; 1930B66D0891C252 CRC64;
MVNSQQQHYS QQQHYSQQQN QNQNSNPIDN SLAHGLSSIS LTNQQQQQQQ HAPKSKRPAR
AFHQETQPSL ATGLNSPMPP RPDLNNNLPF RHRPDRPEHL QRYHHQPMPV VPPGPPIDQP
QHNQPNSIQP LFQQQQQQQQ QQRSTGPRNR IDPNQIPSPV IVHEQDAEAF SEEPFRTCQS
VYAASNTHPF GPNNQPSPPP QIPLSLTDYV AIDQGNCSPR FVRATTYCLP AMDDIAQAAE
LPIGLLIQPL AELAQGEGDI VPIVDFSQDP TGPPRCSSCR GYINPWCTFT DGGNRFRCNL
CGKPSDVPPD YFCHLDMSGR RVDHYQRPEL CRGSVDFIVN QDYWVQSDSS DSKLNARIPQ
PMKYLFAIDV SWSANKSGML QQITKSIKSI LFNQNPQEQE VDDDLEFPSQ SLKPYRQFPV
GAQVGFVTFD RTVHFYNLKA GLDQAQMLVV PDLDDMFVPI SEDALYVNPA ESPAMIHNLL
DSLPTMFGEN NIMESALGGP VQAAFSSLKR LGGQVNIFLT CLPTIGPGGL KQREDTKLYN
TEKETTLFNP VDPWYRQIAE ECSLAGIGIN MFLFPSQYID VATISVLSSI TGGEVFFHPR
FNPQRDCFKV DSELRRVLTR ETASSVTMRI RCSNGLRISQ HFGSFLQRNV TDLEFGNLDA
DKAIAAILKI EGKLEDHSST EAQFQCALLY TSSTGQRRVR CHNLTLPVTR VIGNIFRSAD
MDATMALLTK QYIAQIVQVP LRDVRVTLTE TCVKILLAYR KHCASSTSPG QLILPESYKL
FPLYALGLMK TKAVKGGNVS SDVRTHYMRY LKSLGVAQTI LMLYPRMIPI HKLAEMPEVC
EFNPKNNKFI LPPLMRASYV RMEADGVYLI ENGDMMIMWI GSAVSVAVLE GLFGVSSLEA
LDPKLFSARL PKLKTPLSTK VRRLLKFFDM KRGDRSLPLL VSRQSLDSTE FEFANLLVED
QNNDAMSYVD YLCFVHKQIQ SDLSGSSKTN FQQNDDNNHN SSGFVDPGSL WRAAW
//
