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Database: UniProt
Entry: A0A091DY12_FUKDA
LinkDB: A0A091DY12_FUKDA
Original site: A0A091DY12_FUKDA 
ID   A0A091DY12_FUKDA        Unreviewed;       644 AA.
AC   A0A091DY12;
DT   26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT   26-NOV-2014, sequence version 1.
DT   24-JAN-2024, entry version 32.
DE   RecName: Full=Vesicle-fusing ATPase {ECO:0000256|RuleBase:RU367045};
DE            EC=3.6.4.6 {ECO:0000256|RuleBase:RU367045};
GN   ORFNames=H920_10938 {ECO:0000313|EMBL:KFO27676.1};
OS   Fukomys damarensis (Damaraland mole rat) (Cryptomys damarensis).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Hystricomorpha; Bathyergidae;
OC   Fukomys.
OX   NCBI_TaxID=885580 {ECO:0000313|EMBL:KFO27676.1, ECO:0000313|Proteomes:UP000028990};
RN   [1] {ECO:0000313|EMBL:KFO27676.1, ECO:0000313|Proteomes:UP000028990}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   TISSUE=Liver {ECO:0000313|EMBL:KFO27676.1};
RA   Gladyshev V.N., Fang X.;
RT   "The Damaraland mole rat (Fukomys damarensis) genome and evolution of
RT   African mole rats.";
RL   Submitted (NOV-2013) to the EMBL/GenBank/DDBJ databases.
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   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|RuleBase:RU367045};
CC       Note=Binds 1 Mg(2+) ion per subunit. {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:RU003651}.
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DR   EMBL; KN122870; KFO27676.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A091DY12; -.
DR   STRING; 885580.ENSFDAP00000016883; -.
DR   eggNOG; KOG0741; Eukaryota.
DR   Proteomes; UP000028990; 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:0046872; F:metal ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR   GO; GO:0035494; P:SNARE complex disassembly; IEA:InterPro.
DR   CDD; cd19504; RecA-like_NSF-SEC18_r1-like; 1.
DR   Gene3D; 1.10.8.60; -; 2.
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; 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   PRINTS; PR00830; ENDOLAPTASE.
DR   SMART; SM00382; AAA; 2.
DR   SMART; SM01072; CDC48_2; 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:RU003651};
KW   Cytoplasm {ECO:0000256|RuleBase:RU367045};
KW   ER-Golgi transport {ECO:0000256|RuleBase:RU367045};
KW   Hydrolase {ECO:0000256|RuleBase:RU367045};
KW   Magnesium {ECO:0000256|RuleBase:RU367045};
KW   Metal-binding {ECO:0000256|RuleBase:RU367045};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW   ECO:0000256|RuleBase:RU003651};
KW   Protein transport {ECO:0000256|ARBA:ARBA00022927,
KW   ECO:0000256|RuleBase:RU367045};
KW   Reference proteome {ECO:0000313|Proteomes:UP000028990};
KW   Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|RuleBase:RU367045}.
FT   DOMAIN          17..89
FT                   /note="CDC48"
FT                   /evidence="ECO:0000259|SMART:SM01072"
FT   DOMAIN          158..305
FT                   /note="AAA+ ATPase"
FT                   /evidence="ECO:0000259|SMART:SM00382"
FT   DOMAIN          441..577
FT                   /note="AAA+ ATPase"
FT                   /evidence="ECO:0000259|SMART:SM00382"
SQ   SEQUENCE   644 AA;  71692 MW;  4B24463003174354 CRC64;
     MTMEIDFLQK KSIDSNPYDT DKMAAEFIQQ FNNQAFSVGQ QLVFTFNEKL FGLLVKDIEA
     MDPSILRGEA ATGKRQKIEI GLVVGNSQVA FEKAENSSLN LIGKAKTKEN RQSIINPDWN
     FEKMGIGGLD KEFSDIFRRA FASRVFPPEI VEQMGCKHVK GILLYGPPGC GKTLLARQIG
     KMLNAREPKV VNGPEILNKY VGESEANIRK LFADAEEEQR RLGANSGLHI IIFDEIDAIC
     KQRGSMAGST GVHDTVVNQL LSKIDGVEQL NNILVIGMTN RPDLIDEALL RPGRLEVKME
     IGLPDEKGRL QILHIHTARM RDHQLLSTDV DIKELAVETK NFSGAELEGL VRAAQSTAMN
     RHIKASTKVE VDMEKAESLQ VTRGDFLASL ENDIKPAFGT NQEDYASYIM NGIIKWGDPV
     TRVLDDGELL VQQTKNSDRT PLVSVLLEGP PHSGKTALAA KIAEESNFPF IKICSPDKMI
     GFSETAKCQA MKKIFDDAYK SQLSCVVVDD IERLLDYVPI GPRFSNLVLQ ALLVLLKKAP
     PQGRKLLIIG TTSRKDVLQE MEMLNAFSTT IHVPNIATGE QLLEALELLG NFKDKERTTI
     AQQVKGKKVW IGIKKLLMLI EMSLQMDPEY RVKKFLALLR EEGA
//
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