ID A0A0D1Z0H6_9EURO Unreviewed; 795 AA.
AC A0A0D1Z0H6;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 46.
DE SubName: Full=Cell division control protein 48 {ECO:0000313|EMBL:KIW21101.1};
GN ORFNames=PV08_01680 {ECO:0000313|EMBL:KIW21101.1};
OS Exophiala spinifera.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae; Exophiala.
OX NCBI_TaxID=91928 {ECO:0000313|EMBL:KIW21101.1, ECO:0000313|Proteomes:UP000053328};
RN [1] {ECO:0000313|EMBL:KIW21101.1, ECO:0000313|Proteomes:UP000053328}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 89968 {ECO:0000313|EMBL:KIW21101.1,
RC ECO:0000313|Proteomes:UP000053328};
RG The Broad Institute Genomics Platform;
RA Cuomo C., de Hoog S., Gorbushina A., Stielow B., Teixiera M.,
RA Abouelleil A., Chapman S.B., Priest M., Young S.K., Wortman J., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Exophiala spinifera CBS89968.";
RL Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; KN847492; KIW21101.1; -; Genomic_DNA.
DR RefSeq; XP_016241317.1; XM_016376041.1.
DR AlphaFoldDB; A0A0D1Z0H6; -.
DR STRING; 91928.A0A0D1Z0H6; -.
DR GeneID; 27328763; -.
DR VEuPathDB; FungiDB:PV08_01680; -.
DR HOGENOM; CLU_000688_12_0_1; -.
DR OrthoDB; 168438at2759; -.
DR Proteomes; UP000053328; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
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 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; 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 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 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 4: Predicted;
KW Cell cycle {ECO:0000313|EMBL:KIW21101.1};
KW Cell division {ECO:0000313|EMBL:KIW21101.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000053328}.
FT DOMAIN 45..128
FT /note="CDC48 N-terminal subdomain"
FT /evidence="ECO:0000259|SMART:SM01073"
FT DOMAIN 145..211
FT /note="CDC48"
FT /evidence="ECO:0000259|SMART:SM01072"
FT DOMAIN 257..381
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
FT DOMAIN 519..668
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
FT REGION 1..54
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 704..724
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..45
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 795 AA; 87258 MW; 7C39E97B9CA44C5A CRC64;
MSDQPDHTQH KPHKVNLNDA SGAEKKEELD TSTAILKKKK EPNESNSVTD ATNDDNSIIA
LSNNTMETLQ LFRGDTVLVK GKKRKDTVLI VLADDDLDDG SARINRVVRH NLRVKHGDII
TVHPCPDIKY AKRIAVLPIA DTIEGLTGSL FDVFLAPYFR EAYRPVRQGD LFTVRASMRQ
VEFKVVEVDP PEYGIVAQDT VIHCEGEPIQ REDEEGNLNE VGYDDIGGCR KQMAQIRELV
ELPLRHPQLF KSIGIRPPRG ILMYGPPGTG KTLMARAVAN GTGACFFLIN GPEIMSKMAG
KSESNLRKAF EEAEKNSPAI ISIDEIDSIA PKREKTNGET DGMKARSNVV VMAATNRPNS
IDPALRRFGR FDREVDIDIP NPTGRLETLQ IHTKNMTLAD DIERESIAAE TRGYVGSDIA
SLCSEAAMQQ IREKMDLIDL DEDTIDAEVF DSLGVTMENF RFALGVSNPS ALREVAVVEV
PNVRWDDIGG LEGVKRELIE SVQYPVDHPE KFLKFGLSPS RGVLFYGPPG TGKTMLAKAV
ANECAANFIS VKGPELLSMW FGESESNIRD IFDKARAAAP CVVFLDELDS IARSRGGSVG
GAGGASDRVV NQLLTEMDGM TSKKNVFVIG ATNRPEQLDN ALCYEASRAS ILRAQLRKTP
VAPDVDIDYI ASKTHGFSGA DLDFVTQRAV KLAIKQSIAA DIERQKEREA AGEDTMDEDL
DDPVPELTKT HFEEAMQAAR RSVSDVEIRR YEAFAQAMKQ SDGSAFFKFP SAEETAAAAN
GNGFGEAGND DSLYD
//
