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Database: UniProt
Entry: K2SFH2_MACPH
LinkDB: K2SFH2_MACPH
Original site: K2SFH2_MACPH 
ID   K2SFH2_MACPH            Unreviewed;       899 AA.
AC   K2SFH2;
DT   28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT   28-NOV-2012, sequence version 1.
DT   24-JAN-2024, entry version 43.
DE   SubName: Full=Zinc finger Sec23/Sec24-type protein {ECO:0000313|EMBL:EKG21214.1};
GN   ORFNames=MPH_01477 {ECO:0000313|EMBL:EKG21214.1};
OS   Macrophomina phaseolina (strain MS6) (Charcoal rot fungus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Dothideomycetes incertae sedis; Botryosphaeriales; Botryosphaeriaceae;
OC   Macrophomina.
OX   NCBI_TaxID=1126212 {ECO:0000313|EMBL:EKG21214.1, ECO:0000313|Proteomes:UP000007129};
RN   [1] {ECO:0000313|EMBL:EKG21214.1, ECO:0000313|Proteomes:UP000007129}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MS6 {ECO:0000313|EMBL:EKG21214.1,
RC   ECO:0000313|Proteomes:UP000007129};
RX   PubMed=22992219; DOI=10.1186/1471-2164-13-493;
RA   Islam M.S., Haque M.S., Islam M.M., Emdad E.M., Halim A., Hossen Q.M.M.,
RA   Hossain M.Z., Ahmed B., Rahim S., Rahman M.S., Alam M.M., Hou S., Wan X.,
RA   Saito J.A., Alam M.;
RT   "Tools to kill: Genome of one of the most destructive plant pathogenic
RT   fungi Macrophomina phaseolina.";
RL   BMC Genomics 13:493-493(2012).
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:EKG21214.1}.
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DR   EMBL; AHHD01000055; EKG21214.1; -; Genomic_DNA.
DR   AlphaFoldDB; K2SFH2; -.
DR   STRING; 1126212.K2SFH2; -.
DR   VEuPathDB; FungiDB:MPH_01477; -.
DR   eggNOG; KOG1984; Eukaryota.
DR   HOGENOM; CLU_004589_1_0_1; -.
DR   InParanoid; K2SFH2; -.
DR   OrthoDB; 977017at2759; -.
DR   Proteomes; UP000007129; 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:UP000007129};
KW   Transport {ECO:0000256|ARBA:ARBA00022448};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT   DOMAIN          210..248
FT                   /note="Zinc finger Sec23/Sec24-type"
FT                   /evidence="ECO:0000259|Pfam:PF04810"
FT   DOMAIN          288..535
FT                   /note="Sec23/Sec24 trunk"
FT                   /evidence="ECO:0000259|Pfam:PF04811"
FT   DOMAIN          541..625
FT                   /note="Sec23/Sec24 beta-sandwich"
FT                   /evidence="ECO:0000259|Pfam:PF08033"
FT   DOMAIN          637..737
FT                   /note="Sec23/Sec24 helical"
FT                   /evidence="ECO:0000259|Pfam:PF04815"
FT   DOMAIN          765..838
FT                   /note="Gelsolin-like"
FT                   /evidence="ECO:0000259|Pfam:PF00626"
FT   REGION          1..34
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   899 AA;  98628 MW;  3B279DEC12101822 CRC64;
     MSGLTQQMGG MGLGVDTAGQ AHAARPHKKK DRHAYHQLDA AGSSQAYNGV PQGDAATPSQ
     FLNQPITPAM SQFPAAANNF VPATSATPMQ YAARGSSFNG SVASSAQGKV DPEQVPSIPR
     ARDVPAQFYQ ENVYPTMERH LPPPAAVPFV AFDQGNSAPR FARLTLNSIP QSADALASTA
     LPLGLVLQPL AAPQEGEQPV PVLDFGEAGP PRCRRCRAYI NPFMTFRSGG NKFVCNMCTF
     PNDVAPEYFA PTDPSGVRVD RLQRPELTLG TVDFMVPKEY WSKEPVGLRW LFLVDVSAEA
     VNKGFLDGFC EGIMNALYGN ENEREEQEGA NLKKLPKGAK VGIVTYDKEI HFYNLSSSLD
     KAQMLVMPDI EDPFVPLSEG LFVDPEESKS VITALLTQLP TMFSQIKNPE PALLSTLHSA
     LDALKDTGGK IVCSLASLPT WGPGRLFLRD DGKVHGTDAE KKLLTTEHPG YKKIGGKFCE
     AGIGIDFFLA APSGGYLDVA TIGHVSEVTG GEVFYYPNFH GPRDTLKLSK EIKHTVTRET
     GYQALMKVRC SNGLQVSAYH GNFYHHTFGA DLEFGVIDAD KSIGVMFSYD GKLDPKLDAH
     FQSALLYTTA GGERRVRCCN LVASVNDNAV ETMKFVDQDA VVNIIAKEAA SRMAERSLKD
     IRNAITEKTV DILAAYRKNF SHGHPPGQLV LPEHLKEFAM YMLGLIKSRA FKGGKEPTDR
     RVYDARMLKA MGPTELSLYL YPRIYSLHNL EPTEGFANES GRLRMPPGVR ASYSRIEEGG
     AYLVDNGQQV ILWLHGAVSP NLLEDLFGPG ANELRNLDPF LNNIPVLETH LNAQVRNIMQ
     FLEQTRGSKA VTIQLARQGL DGAEYEFARL LYEDRNGEAQ SYVDWLVHVH RNIQLEVSL
//
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