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Database: UniProt
Entry: A0A3B4ZUD3_9TELE
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ID   A0A3B4ZUD3_9TELE        Unreviewed;       747 AA.
AC   A0A3B4ZUD3;
DT   05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT   05-DEC-2018, sequence version 1.
DT   24-JAN-2024, entry version 24.
DE   RecName: Full=Vesicle-fusing ATPase {ECO:0000256|ARBA:ARBA00019912, ECO:0000256|RuleBase:RU367045};
DE            EC=3.6.4.6 {ECO:0000256|ARBA:ARBA00012674, ECO:0000256|RuleBase:RU367045};
GN   Name=LOC103367352 {ECO:0000313|RefSeq:XP_008293574.1};
OS   Stegastes partitus (bicolor damselfish).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Ovalentaria; Pomacentridae; Stegastes.
OX   NCBI_TaxID=144197 {ECO:0000313|Ensembl:ENSSPAP00000011890.1, ECO:0000313|Proteomes:UP000261400};
RN   [1] {ECO:0000313|Ensembl:ENSSPAP00000011890.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-2023) to UniProtKB.
RN   [2] {ECO:0000313|RefSeq:XP_008293574.1}
RP   IDENTIFICATION.
RG   RefSeq;
RL   Submitted (SEP-2023) to UniProtKB.
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|ARBA:ARBA00000161,
CC         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|ARBA:ARBA00004496,
CC       ECO:0000256|RuleBase:RU367045}.
CC   -!- SIMILARITY: Belongs to the AAA ATPase family.
CC       {ECO:0000256|ARBA:ARBA00006914, ECO:0000256|RuleBase:RU367045}.
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DR   RefSeq; XP_008293574.1; XM_008295352.1.
DR   AlphaFoldDB; A0A3B4ZUD3; -.
DR   STRING; 144197.ENSSPAP00000011890; -.
DR   Ensembl; ENSSPAT00000012097.1; ENSSPAP00000011890.1; ENSSPAG00000009009.1.
DR   GeneID; 103367352; -.
DR   GeneTree; ENSGT00530000064085; -.
DR   OrthoDB; 553800at2759; -.
DR   Proteomes; UP000261400; Unplaced.
DR   Proteomes; UP000694891; Unplaced.
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:0048757; P:pigment granule maturation; IEA:Ensembl.
DR   GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR   GO; GO:0003406; P:retinal pigment epithelium development; IEA:Ensembl.
DR   GO; GO:0035494; P:SNARE complex disassembly; IEA:InterPro.
DR   CDD; cd00009; AAA; 1.
DR   CDD; cd19504; RecA-like_NSF-SEC18_r1-like; 1.
DR   Gene3D; 1.10.8.60; -; 2.
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; IPR003338; CDC4_N-term_subdom.
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   Pfam; PF02359; CDC48_N; 1.
DR   SMART; SM00382; AAA; 2.
DR   SMART; SM01072; CDC48_2; 1.
DR   SMART; SM01073; CDC48_N; 1.
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|ARBA:ARBA00022490, 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:RU367045};
KW   Protein transport {ECO:0000256|ARBA:ARBA00022927,
KW   ECO:0000256|RuleBase:RU367045};
KW   Reference proteome {ECO:0000313|Proteomes:UP000694891};
KW   Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|RuleBase:RU367045}.
FT   DOMAIN          5..85
FT                   /note="CDC48 N-terminal subdomain"
FT                   /evidence="ECO:0000259|SMART:SM01073"
FT   DOMAIN          111..183
FT                   /note="CDC48"
FT                   /evidence="ECO:0000259|SMART:SM01072"
FT   DOMAIN          252..399
FT                   /note="AAA+ ATPase"
FT                   /evidence="ECO:0000259|SMART:SM00382"
FT   DOMAIN          535..671
FT                   /note="AAA+ ATPase"
FT                   /evidence="ECO:0000259|SMART:SM00382"
SQ   SEQUENCE   747 AA;  82963 MW;  CFADD3A5E7B5BA6E CRC64;
     MSSRIMQAAR CPTDELSLTN CVVINDKEQQ QFEKHVIVRN VTHKFVFTLT KHPSVNSGTI
     GFSLPQRKWA GLSIGQEVEV TNYNFDKSKQ CISSMTMEID FLQKKNADSN PYDSDKMAGE
     FTVRFNNQAF TVGQQLVFSY NDKLFQLVVK DMEAMDPSIL KSGNASAKKQ KIEIGLLLGD
     SQVVFEKAES SSMTLIGKSK TRESRQSIIS PDWNFERMGI GGLDKEFSDI FRRAFASRVF
     PPDIVEQMGG KHVKGILLYG PPGCGKTLMA RQIGKMLKAR EPKIVNGPEI LNKYVGESEA
     NIRKLFADAE DEQKRLGANS GLHIIIFDEI DAICKQRGSM AGSTGVHDTV VNQLLSKIDG
     VEQLNNILVI GMTNRPDLID EALLRPGRLE VKMEIGLPDE KGRIQILNIH TAKMRLHDLL
     AKDVDVKELA VETKNYSGAE LEGLVRAAQS TAMNRHIKAS NTVEVNIETA EKLQVSRLDF
     MASLNNDIKP AFGTNQEDYA SYIMNGIIRW GDPVSAVLED GELLVQQTKN SERTPLVSVL
     LEGPPNSGKT ALAAKISEDS QFPFIKICSP DKMIGHSEIA KCQAIKKIFE DAYKSQLSCV
     VVDDIERLLD YVPIGPRFSN LVLQALLVLL KKPPPKGRKL LIIGTTSRKD VLQEMEMLDA
     FSTTIHIPNI SRGEQLVEAL ELLGSFQENE RAKIAKAVKG QSLWIGIKKL LMLIEMAAQM
     DPDYRVSKFL SLLKDEGALG SDKFVAI
//
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