ID A0A0S3RQF2_PHAAN Unreviewed; 398 AA.
AC A0A0S3RQF2;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE RecName: Full=AAA+ ATPase domain-containing protein {ECO:0000259|SMART:SM00382};
GN Name=Vigan.03G289500 {ECO:0000313|EMBL:BAT82826.1};
GN ORFNames=VIGAN_03289500 {ECO:0000313|EMBL:BAT82826.1};
OS Vigna angularis var. angularis.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC NPAAA clade; indigoferoid/millettioid clade; Phaseoleae; Vigna.
OX NCBI_TaxID=157739 {ECO:0000313|EMBL:BAT82826.1, ECO:0000313|Proteomes:UP000291084};
RN [1] {ECO:0000313|EMBL:BAT82826.1, ECO:0000313|Proteomes:UP000291084}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Shumari {ECO:0000313|Proteomes:UP000291084};
RX PubMed=26616024; DOI=10.1038/srep16780;
RA Sakai H., Naito K., Ogiso-Tanaka E., Takahashi Y., Iseki K., Muto C.,
RA Satou K., Teruya K., Shiroma A., Shimoji M., Hirano T., Itoh T., Kaga A.,
RA Tomooka N.;
RT "The power of single molecule real-time sequencing technology in the de
RT novo assembly of a eukaryotic genome.";
RL Sci. Rep. 5:16780-16780(2015).
CC -!- SIMILARITY: Belongs to the AAA ATPase family.
CC {ECO:0000256|ARBA:ARBA00006914, ECO:0000256|RuleBase:RU003651}.
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DR EMBL; AP015036; BAT82826.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0S3RQF2; -.
DR Proteomes; UP000291084; Chromosome 3.
DR GO; GO:0000502; C:proteasome complex; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR Gene3D; 1.10.8.60; -; 1.
DR Gene3D; 2.40.50.140; Nucleic acid-binding proteins; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR041569; AAA_lid_3.
DR InterPro; IPR003959; ATPase_AAA_core.
DR InterPro; IPR003960; ATPase_AAA_CS.
DR InterPro; IPR012340; NA-bd_OB-fold.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR032501; Prot_ATP_ID_OB_2nd.
DR PANTHER; PTHR23073; 26S PROTEASOME REGULATORY SUBUNIT; 1.
DR PANTHER; PTHR23073:SF31; 26S PROTEASOME REGULATORY SUBUNIT 10B HOMOLOG A-RELATED; 1.
DR Pfam; PF00004; AAA; 1.
DR Pfam; PF17862; AAA_lid_3; 1.
DR Pfam; PF16450; Prot_ATP_ID_OB_C; 1.
DR SMART; SM00382; AAA; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR PROSITE; PS00674; AAA; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|RuleBase:RU003651};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Nucleotide-binding {ECO:0000256|RuleBase:RU003651};
KW Proteasome {ECO:0000256|ARBA:ARBA00022942};
KW Reference proteome {ECO:0000313|Proteomes:UP000291084}.
FT DOMAIN 171..310
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
FT COILED 24..58
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 398 AA; 44615 MW; 12658ACF1817BD86 CRC64;
MTDTEDATRR RNAVTEYRKK LLQHKELESR VRSVRENLRA SRKEFNKTED DLKSLQSVGQ
IIGEVLRPLD NERLIVKASS GPRYVVGCRS KVDKEKLTAG TRVVLDMTTL TIMRALPREV
DPVVYNMLHE DPGNISYSAV GGLSDQIREL RESIELPLMN PELFLRVGIK PPKGVLLYGP
PGTGKTLLAR AIASNIDANF LKVVSSAIID KYIGESARLI REMFGYARDH QPCIIFMDEI
DAIGGRRFSE GTSADREIQR TLMELLNQLD GFDQLGKVKM IMATNRPDVL DPALLRPGRL
DRKIEIPLPN EQSRMEILKI HAAGIAKHGE IDYEAVVKLA EGFNGADLRN VCTEAGMAAI
RAERDYVIHE DFMKAVRKLN DAKKLESSAP YSADFGKD
//
