ID E9ERI8_METRA Unreviewed; 840 AA.
AC E9ERI8;
DT 05-APR-2011, integrated into UniProtKB/TrEMBL.
DT 05-APR-2011, sequence version 1.
DT 24-JAN-2024, entry version 68.
DE RecName: Full=Vesicular-fusion protein SEC18 {ECO:0000256|RuleBase:RU367045};
DE EC=3.6.4.6 {ECO:0000256|RuleBase:RU367045};
GN ORFNames=MAA_02584 {ECO:0000313|EMBL:EFZ01355.1};
OS Metarhizium robertsii (strain ARSEF 23 / ATCC MYA-3075) (Metarhizium
OS anisopliae (strain ARSEF 23)).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Clavicipitaceae; Metarhizium.
OX NCBI_TaxID=655844 {ECO:0000313|EMBL:EFZ01355.1, ECO:0000313|Proteomes:UP000002498};
RN [1] {ECO:0000313|EMBL:EFZ01355.1, ECO:0000313|Proteomes:UP000002498}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ARSEF 23 / ATCC MYA-3075 {ECO:0000313|Proteomes:UP000002498};
RX PubMed=21253567; DOI=10.1371/journal.pgen.1001264;
RA Gao Q., Jin K., Ying S.H., Zhang Y., Xiao G., Shang Y., Duan Z., Hu X.,
RA Xie X.Q., Zhou G., Peng G., Luo Z., Huang W., Wang B., Fang W., Wang S.,
RA Zhong Y., Ma L.J., St Leger R.J., Zhao G.P., Pei Y., Feng M.G., Xia Y.,
RA Wang C.;
RT "Genome sequencing and comparative transcriptomics of the model
RT entomopathogenic fungi Metarhizium anisopliae and M. acridum.";
RL PLoS Genet. 7:E1001264-E1001264(2011).
RN [2] {ECO:0000313|EMBL:EFZ01355.1, ECO:0000313|Proteomes:UP000002498}
RP GENOME REANNOTATION.
RC STRAIN=ARSEF 23 / ATCC MYA-3075 {ECO:0000313|Proteomes:UP000002498};
RX PubMed=25368161; DOI=10.1073/pnas.1412662111;
RA Hu X., Xiao G., Zheng P., Shang Y., Su Y., Zhang X., Liu X., Zhan S.,
RA St Leger R.J., Wang C.;
RT "Trajectory and genomic determinants of fungal-pathogen speciation and host
RT adaptation.";
RL Proc. Natl. Acad. Sci. U.S.A. 111:16796-16801(2014).
CC -!- FUNCTION: Required for vesicle-mediated transport. Catalyzes the fusion
CC of transport vesicles within the Golgi cisternae. Is also required for
CC transport from the endoplasmic reticulum to the Golgi stack. Seems to
CC function as a fusion protein required for the delivery of cargo
CC proteins to all compartments of the Golgi stack independent of vesicle
CC origin. {ECO:0000256|RuleBase:RU367045}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.6;
CC Evidence={ECO:0000256|RuleBase:RU367045};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|RuleBase:RU367045}.
CC -!- SIMILARITY: Belongs to the AAA ATPase family.
CC {ECO:0000256|ARBA:ARBA00006914, ECO:0000256|RuleBase:RU367045}.
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:EFZ01355.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; ADNJ02000004; EFZ01355.1; -; Genomic_DNA.
DR RefSeq; XP_007818773.1; XM_007820582.1.
DR AlphaFoldDB; E9ERI8; -.
DR GeneID; 19256870; -.
DR KEGG; maj:MAA_02584; -.
DR HOGENOM; CLU_008037_2_0_1; -.
DR OrthoDB; 553800at2759; -.
DR Proteomes; UP000002498; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR GO; GO:0035494; P:SNARE complex disassembly; IEA:InterPro.
DR CDD; cd00009; AAA; 1.
DR Gene3D; 1.10.8.60; -; 1.
DR Gene3D; 2.40.40.20; -; 1.
DR Gene3D; 3.10.330.10; -; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR041569; AAA_lid_3.
DR InterPro; IPR009010; Asp_de-COase-like_dom_sf.
DR InterPro; IPR003959; ATPase_AAA_core.
DR InterPro; IPR003960; ATPase_AAA_CS.
DR InterPro; IPR004201; Cdc48_dom2.
DR InterPro; IPR029067; CDC48_domain_2-like_sf.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR039812; Vesicle-fus_ATPase.
DR PANTHER; PTHR23078:SF3; VESICLE-FUSING ATPASE; 1.
DR PANTHER; PTHR23078; VESICULAR-FUSION PROTEIN NSF; 1.
DR Pfam; PF00004; AAA; 2.
DR Pfam; PF17862; AAA_lid_3; 1.
DR Pfam; PF02933; CDC48_2; 1.
DR SMART; SM00382; AAA; 2.
DR SUPFAM; SSF50692; ADC-like; 1.
DR SUPFAM; SSF54585; Cdc48 domain 2-like; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR PROSITE; PS00674; AAA; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|RuleBase:RU367045};
KW Cytoplasm {ECO:0000256|RuleBase:RU367045};
KW ER-Golgi transport {ECO:0000256|RuleBase:RU367045};
KW Hydrolase {ECO:0000256|RuleBase:RU367045};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU367045};
KW Protein transport {ECO:0000256|ARBA:ARBA00022927,
KW ECO:0000256|RuleBase:RU367045};
KW Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|RuleBase:RU367045}.
FT DOMAIN 345..493
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
FT DOMAIN 627..764
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
FT REGION 1..82
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 19..33
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 840 AA; 91310 MW; B410EE8826377207 CRC64;
MSRVPPGGPG RLPYAPSLPG SNPRMPPNQG RPPPGSSYGA DPSQGYGTPQ GYGDPRVSQG
SGPQSPAMPR YSEKGPSGLS GARRVTLRVE KVADRTLQSR LIYGNICAVA PEDFPPSRDG
TDLYILVRGG QPEGEFVVTA RPVPGFPQGG ISLSDPQRSW CNITIRDIFT GELYDPFAQG
GRAYLGSVDL EVGFASPNKR TDAPYDEDHL AAQFSDTFAN QVLAPGQRIL MDVRNIPLLI
VVKTVGLVDL AMSSDDPSKQ VFREGHARGI LTSQTRVLFH RDGRSDFHMK PSMSKPNSNA
ILAPDFKFED MGIGGLGDEF STIFRRAFAS RVFPPGLVAK MGIPHVKGML LYGPPGTGKT
LIARQIGKML NARPPKVING PEVLNKYVGQ SEENIRKLFA DAEKEYKEKA EESSLHIIIF
DELDAVCKQR GSGAGGGTGV GDSVVNQLLS KLDGVDQLNN ILLIGMTNRK DMIDDALMRP
GRLEVHIEIS LPDEEGRFDI FNIHTAKMRE NNILDSDVDL KELASMTKNY SGAEINGVVK
AAASFAFSRH TEVGQMAAVK QDVASMQVNR ADFMLALTEV KPAYGVSEAE LEDAVGLGII
RFSRYIGSTI DEMMRVVGMI KNDPNKFSTS VLFHGPKGAG KTALAAHIAM QSDFPFVKLV
TPADLVGYRD DFAKKDYVHK AFADAYKSPA SILILDDFER LIGWNPIGPR FSNVMLEALT
TLIVSKPPRN HRLLVFVTTS KAAVLKMLEI DTDFAKRVAV PAVADAEELA AVLQESRVFN
SNDIDQVLNL VRQRTGSDKV GIGIKTIQDL IFEAKAGESS SHVLETFSEL LLDNIQGLNL
//
