ID A0A1I8C6J8_9BILA Unreviewed; 808 AA.
AC A0A1I8C6J8;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE RecName: Full=vesicle-fusing ATPase {ECO:0000256|ARBA:ARBA00012674};
DE EC=3.6.4.6 {ECO:0000256|ARBA:ARBA00012674};
OS Rhabditophanes sp. KR3021.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Tylenchina; Panagrolaimomorpha; Strongyloidoidea; Alloionematidae;
OC Rhabditophanes.
OX NCBI_TaxID=114890 {ECO:0000313|Proteomes:UP000095286, ECO:0000313|WBParaSite:RSKR_0000136200.1};
RN [1] {ECO:0000313|WBParaSite:RSKR_0000136200.1}
RP IDENTIFICATION.
RC STRAIN=KR3021 {ECO:0000313|WBParaSite:RSKR_0000136200.1};
RG WormBaseParasite;
RL Submitted (NOV-2016) to UniProtKB.
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};
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DR AlphaFoldDB; A0A1I8C6J8; -.
DR WBParaSite; RSKR_0000136200.1; RSKR_0000136200.1; RSKR_0000136200.
DR Proteomes; UP000095286; Unplaced.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0043170; P:macromolecule metabolic process; IEA:UniProt.
DR GO; GO:0006807; P:nitrogen compound metabolic process; IEA:UniProt.
DR GO; GO:0044238; P:primary metabolic process; IEA:UniProt.
DR GO; GO:0050896; P:response to stimulus; IEA:UniProt.
DR CDD; cd19519; RecA-like_CDC48_r1-like; 1.
DR Gene3D; 1.10.8.60; -; 1.
DR Gene3D; 2.40.40.20; -; 1.
DR Gene3D; 3.10.330.10; -; 1.
DR Gene3D; 6.10.20.150; -; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR005938; AAA_ATPase_CDC48.
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; IPR015415; Spast_Vps4_C.
DR NCBIfam; TIGR01243; CDC48; 1.
DR PANTHER; PTHR23077; AAA-FAMILY ATPASE; 1.
DR PANTHER; PTHR23077:SF171; ATPASE FAMILY PROTEIN 2 HOMOLOG; 1.
DR Pfam; PF00004; AAA; 2.
DR Pfam; PF17862; AAA_lid_3; 2.
DR Pfam; PF02933; CDC48_2; 1.
DR Pfam; PF02359; CDC48_N; 1.
DR Pfam; PF09336; Vps4_C; 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; 2.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741}.
FT DOMAIN 31..114
FT /note="CDC48 N-terminal subdomain"
FT /evidence="ECO:0000259|SMART:SM01073"
FT DOMAIN 131..197
FT /note="CDC48"
FT /evidence="ECO:0000259|SMART:SM01072"
FT DOMAIN 243..379
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
FT DOMAIN 516..657
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
FT REGION 776..808
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 776..792
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 808 AA; 89558 MW; 864BF80FC7FDF502 CRC64;
MASVPTEKSD VEKKNDRLAT AILNTKVRPN RLITDQSIED ENSTIYVSQA KLDELGIFRG
DTVLIKGKKR KETLAVVLLD AECPVEKVRM NRCIRNNLRI RLGDYVTINA IENVVYGERI
HVLPVDDTVE GLTGNLFEVF LKPYFTECYR PVTVGDIFTI NAAMRTVEFK VVQTQPAPHC
IVAPDTVIHC EGDPLKREDE EDSMNEIGYD DIGGVRKQLA QIKEMVELPL RHPTLFKSIG
IKPPRGILLF GPPGTGKTMI ARAVANETGA FFFLINGPEI MSKMSGESES NLRKAFAECE
KNSPAILFID EVDSIAPNRE KTHGEVERRI VSQLLTLMDG IKQRNNVVVI AATNRPNSID
PALRRFGRFD REIDIGIPDA IGRLEILRIH TKNMKLATDV NLEIVANESH GYVGADLASL
CSEAAIQQIR EKMELIDLED DTIDAKVLDS LAVTMENFRF AMNKNSPSAL RETVVETPNV
KWSDIGGLEN VKRELQEMVQ YPVEHPDKFL KFGMQPSRGC LFFGPPGCGK TLLAKAIANE
CQANFISVKG PELLTMWFGE SEANVRNIFD KARAAAPCVL FFDELDSIAV SRGGSSSGGD
AGGAGDRVIN QILTEMDGIG SKKNVFIIGA TNRPDIIDSA ILRPGRLDQL LYIPLPDADS
RFQIFKANLK KTPLAEDLDL RYLSEQTIGF SGADLTEICQ RACKLAIRQC IELDLAAERK
KQAKKAAGEE LMEEEEVDPV PVLTKKHFEE AMKFARRSVS DNDIVKYESF SETLQQQRGF
GNNFSFPTEG GNTTGGAPPA AEDDDLYN
//
