ID A0A183QFK1_9TREM Unreviewed; 406 AA.
AC A0A183QFK1;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE SubName: Full=AAA domain-containing protein {ECO:0000313|WBParaSite:SROB_0000240901-mRNA-1};
OS Schistosoma rodhaini.
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Platyhelminthes; Trematoda;
OC Digenea; Strigeidida; Schistosomatoidea; Schistosomatidae; Schistosoma.
OX NCBI_TaxID=6188 {ECO:0000313|WBParaSite:SROB_0000240901-mRNA-1};
RN [1] {ECO:0000313|WBParaSite:SROB_0000240901-mRNA-1}
RP IDENTIFICATION.
RG WormBaseParasite;
RL Submitted (JUN-2016) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC -!- SIMILARITY: Belongs to the AAA ATPase family.
CC {ECO:0000256|ARBA:ARBA00006914, ECO:0000256|RuleBase:RU003651}.
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DR AlphaFoldDB; A0A183QFK1; -.
DR STRING; 6188.A0A183QFK1; -.
DR WBParaSite; SROB_0000240901-mRNA-1; SROB_0000240901-mRNA-1; SROB_0000240901.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
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:SF7; 26S PROTEASOME REGULATORY SUBUNIT 6A; 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 Nucleotide-binding {ECO:0000256|RuleBase:RU003651};
KW Proteasome {ECO:0000256|ARBA:ARBA00022942}.
FT DOMAIN 208..325
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
SQ SEQUENCE 406 AA; 45567 MW; E9C9F47FC79F14C0 CRC64;
MTSTIERPIW DDVDEAMVDE VMRMSTEELT SRARLLDSEI RFMQSELKHV NHEINTKQTK
VKDSKSKIKM NKALPYLVAT VVELLDVEPQ EDEIEEGANV DLDSQRKGKC AVIKTSTRQT
YFLPVIGLVP PEDLKPGDLV GVHKDSYLIL EKLPPEFDSR VKAMEVDERP TERYSDIGGL
DKQIQELIEA VVLPMTHRDR FEALGIQPPK GVLLYGPPGT GKTLLARACA AQTKSTFLKL
AGPQLVQMFI GDGAKLVRDA FQLAKEKAPA IIFIDELDAI GTKRFNSEKA GDREVIAATN
RVDILDPALL RSGRVDRKIE FPAPNEEARA RIMQIHSRKM NVQKDVNFEE LARCTDDFNG
AQCKAVCVEA GMIALRRSAS EVTHEDYMDA ILEVQAKKRT NLNYYA
//