ID G3B345_CANTC Unreviewed; 834 AA.
AC G3B345;
DT 16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT 16-NOV-2011, sequence version 1.
DT 27-MAR-2024, entry version 67.
DE RecName: Full=Cell division control protein 48 {ECO:0008006|Google:ProtNLM};
GN ORFNames=CANTEDRAFT_105619 {ECO:0000313|EMBL:EGV64076.1};
OS Candida tenuis (strain ATCC 10573 / BCRC 21748 / CBS 615 / JCM 9827 / NBRC
OS 10315 / NRRL Y-1498 / VKM Y-70) (Yeast) (Yamadazyma tenuis).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Yamadazyma.
OX NCBI_TaxID=590646 {ECO:0000313|Proteomes:UP000000707};
RN [1] {ECO:0000313|EMBL:EGV64076.1, ECO:0000313|Proteomes:UP000000707}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 10573 / BCRC 21748 / CBS 615 / JCM 9827 / NBRC 10315 /
RC NRRL Y-1498 / VKM Y-70 {ECO:0000313|Proteomes:UP000000707};
RX PubMed=21788494; DOI=10.1073/pnas.1103039108;
RA Wohlbach D.J., Kuo A., Sato T.K., Potts K.M., Salamov A.A., LaButti K.M.,
RA Sun H., Clum A., Pangilinan J.L., Lindquist E.A., Lucas S., Lapidus A.,
RA Jin M., Gunawan C., Balan V., Dale B.E., Jeffries T.W., Zinkel R.,
RA Barry K.W., Grigoriev I.V., Gasch A.P.;
RT "Comparative genomics of xylose-fermenting fungi for enhanced biofuel
RT production.";
RL Proc. Natl. Acad. Sci. U.S.A. 108:13212-13217(2011).
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; GL996521; EGV64076.1; -; Genomic_DNA.
DR RefSeq; XP_006686390.1; XM_006686327.1.
DR AlphaFoldDB; G3B345; -.
DR STRING; 590646.G3B345; -.
DR GeneID; 18245825; -.
DR KEGG; cten:CANTEDRAFT_105619; -.
DR eggNOG; KOG0730; Eukaryota.
DR HOGENOM; CLU_000688_12_3_1; -.
DR OrthoDB; 168438at2759; -.
DR Proteomes; UP000000707; 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: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 CDD; cd19528; RecA-like_CDC48_r2-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 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 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 Reference proteome {ECO:0000313|Proteomes:UP000000707}.
FT DOMAIN 35..118
FT /note="CDC48 N-terminal subdomain"
FT /evidence="ECO:0000259|SMART:SM01073"
FT DOMAIN 135..201
FT /note="CDC48"
FT /evidence="ECO:0000259|SMART:SM01072"
FT DOMAIN 247..383
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
FT DOMAIN 520..659
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
FT REGION 720..752
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 798..834
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 720..735
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 736..750
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 834 AA; 91497 MW; 5B0B1272287EECAC CRC64;
MAADEHKPLL DASGSQSKED ATATAILRRK KKDNALIVDD AVNDDNSVIT MSSNTMELLQ
LFRGDTVLVK GKKRKDTVLI VLADDDMDDG VARVNRCVRN NLRVRLGDII TVHPCPDIKY
ANRISVLPIA DTVEGLTGSL FDVYLKPYFV EAYRPVRKGD LFTVRGGMRQ VEFKVVEVDP
EDFAIVAQDT VIHCEGEPIN REDEENSLNE VGYDDIGGCK KQMAQIRELV ELPLRHPQLF
KSIGIKPPKG ILMYGPPGTG KTIMARAVAN ETGAFFFLIN GPEIMSKMAG ESESNLRKAF
EEAEKNSPSI IFIDEIDSIA PKRDKTNGEV ERRVVSQLLT LMDGMKARSN VVVIAATNRP
NSIDPALRRF GRFDREVDIG VPDAAGRLEI LKIHTKNMKL ADDVDLEAIA SETHGFVGAD
VASLCSEAAM QQIREKMDLI DLDEDTIDAE VLDSLGVTME NFRFALGNSN PSALRETVVE
NVNVTWDDIG GLDDIKNELK ETVEYPVLHP DQYQKFGLAP SKGVLFFGPP GTGKTLLAKA
VATEVSANFI SVKGPELLSM WYGESESNIR DIFDKARAAA PTVVFLDELD SIAKSRGGSN
GDAGGASDRV VNQLLTEMDG MNAKKNVFVI GATNRPDQID PALLRPGRLD QLIYVPLPDE
PARLSILEAQ LRNTPLEPGL NLNEIARITN GFSGADLSYI VQRSAKFAIK DSIEAQIKSK
KLKDEKKAEA GEEGTEDVNM KEEEPEEPEE DPVPFITKAH FEEAMKTAKR SVSDAELRRY
ESYASQILAS RGQYTNFRFS DENGESEVGA TGATGEASTG AAFGANDDDD DLYN
//
