ID B8NQU3_ASPFN Unreviewed; 821 AA.
AC B8NQU3;
DT 03-MAR-2009, integrated into UniProtKB/TrEMBL.
DT 03-MAR-2009, sequence version 1.
DT 27-MAR-2024, entry version 100.
DE SubName: Full=Cell division control protein Cdc48 {ECO:0000313|EMBL:EED47596.1};
GN ORFNames=AFLA_002370 {ECO:0000313|EMBL:EED47596.1}, G4B84_007220
GN {ECO:0000313|EMBL:QMW31839.1};
OS Aspergillus flavus (strain ATCC 200026 / FGSC A1120 / IAM 13836 / NRRL 3357
OS / JCM 12722 / SRRC 167).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=332952 {ECO:0000313|EMBL:EED47596.1, ECO:0000313|Proteomes:UP000001875};
RN [1] {ECO:0000313|EMBL:EED47596.1, ECO:0000313|Proteomes:UP000001875}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 200026 / FGSC A1120 / IAM 13836 / NRRL 3357 / JCM 12722 /
RC SRRC 167 {ECO:0000313|Proteomes:UP000001875}, and NRRL3357
RC {ECO:0000313|EMBL:EED47596.1};
RX PubMed=25883274; DOI=10.1128/genomeA.00168-15;
RA Nierman W.C., Yu J., Fedorova-Abrams N.D., Losada L., Cleveland T.E.,
RA Bhatnagar D., Bennett J.W., Dean R., Payne G.A.;
RT "Genome sequence of Aspergillus flavus NRRL 3357, a strain that causes
RT aflatoxin contamination of food and feed.";
RL Genome Announc. 3:E0016815-E0016815(2015).
RN [2] {ECO:0000313|EMBL:QMW31839.1, ECO:0000313|Proteomes:UP000515286}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL3357 {ECO:0000313|EMBL:QMW31839.1,
RC ECO:0000313|Proteomes:UP000515286};
RA Fountain J.C., Clevenger J.P., Nadon B., Youngblood R.C., Korani W.,
RA Chang P.-K., Starr D., Wang H., Isett B., Johnston H.R., Wiggins R.,
RA Chu Y., Agarwal G., Kemerait R.C., Pandey M.K., Bhatnagar D.,
RA Ozias-Akins P., Varshney R.K., Scheffler B.E., Vaughn J.N., Guo B.;
RT "Two New Chromosome-Level Aspergillus flavus Reference Genomes Reveal a
RT Large Insertion Potentially Contributing to Isolate Stress Tolerance and
RT Aflatoxin Production.";
RL Submitted (JUL-2020) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; EQ963482; EED47596.1; -; Genomic_DNA.
DR EMBL; CP059869; QMW31839.1; -; Genomic_DNA.
DR RefSeq; XP_002382438.1; XM_002382397.1.
DR AlphaFoldDB; B8NQU3; -.
DR STRING; 332952.B8NQU3; -.
DR EnsemblFungi; EED47596; EED47596; AFLA_002370.
DR VEuPathDB; FungiDB:AFLA_011561; -.
DR eggNOG; KOG0730; Eukaryota.
DR HOGENOM; CLU_000688_12_0_1; -.
DR OMA; HACHDIK; -.
DR OrthoDB; 168438at2759; -.
DR Proteomes; UP000001875; Unassembled WGS sequence.
DR Proteomes; UP000515286; Chromosome 4.
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 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 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 Cell cycle {ECO:0000313|EMBL:EED47596.1};
KW Cell division {ECO:0000313|EMBL:EED47596.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741}.
FT DOMAIN 43..126
FT /note="CDC48 N-terminal subdomain"
FT /evidence="ECO:0000259|SMART:SM01073"
FT DOMAIN 143..209
FT /note="CDC48"
FT /evidence="ECO:0000259|SMART:SM01072"
FT DOMAIN 255..391
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
FT DOMAIN 529..668
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
FT REGION 1..26
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 727..756
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 789..821
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 789..814
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 821 AA; 90554 MW; 04DA9CBADDE61F61 CRC64;
MSAEPDHTHD KKRVHLQDAS GAEKKEELDT ATAILKKKKK PNSLIVTDAV NDDNSVIALS
NNTMETLQLF RGDTVLVKGK KRKDTVLIVL ADDDLDDGSA RINRVVRHNL RVKHGDVITV
HPCPDIKYAK RIAVLPIADT VEGLTGSLFD VFLAPYFREA YRPVRQGDLF TVRGGMRQVE
FKVVEVDPPE YGIVAQDTVI HCEGEPIQRE DEEGNLNEVG YDDIGGCRKQ MAQIRELVEL
PLRHPQLFKS IGIKPPRGIL MYGPPGTGKT LMARAVANET GAFFFLINGP EIMSKMAGES
ESNLRKAFEE AEKNSPAIIF IDEIDSIAPK REKTNGEVER RVVSQLLTLM DGMKARSNVV
VMAATNRPNS IDPALRRFGR FDREVDIGIP DPTGRLEIMQ IHTKNMKLGE DVDLETIAAE
THGYVGSDLA SLCSEAAMQQ IREKMDLIDL DEDTIDAEVL DSLGVTMENF RYALGVSNPS
ALREVAVVEV PNVRWEDIGG LEEVKRELIE SVQYPVDHPE KYQKFGLSPS RGVLFYGPPG
TGKTMLAKAV ANECAANFIS VKGPELLSMW FGESESNIRD IFDKARAAAP CVVFLDELDS
IAKSRGGSVG DAGGASDRVV NQLLTEMDGM TSKKNVFVIG ATNRPEQLDA ALVRPGRLDT
LVYVPLPDQA SREGILKAQL RKTPVAPDVD LPFIASKTHG FSGADLGFVT QRAVKLAIKQ
SITADIERQK QREANGEDIK MDEDEEVDEE DPVPELTRAH FEEAMKTARR SVSDVEIRRY
EAFAQSLKNS GGSSFFRFPS AGEVQDNNTF GEAGNDDSLY D
//
