ID A0A0V1PAB9_9BILA Unreviewed; 656 AA.
AC A0A0V1PAB9;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 40.
DE SubName: Full=26S protease regulatory subunit 4 {ECO:0000313|EMBL:KRZ93080.1};
DE Flags: Fragment;
GN Name=Pros26.4 {ECO:0000313|EMBL:KRZ93080.1};
GN ORFNames=T08_1159 {ECO:0000313|EMBL:KRZ93080.1};
OS Trichinella sp. T8.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Trichinellida; Trichinellidae; Trichinella.
OX NCBI_TaxID=92180 {ECO:0000313|EMBL:KRZ93080.1, ECO:0000313|Proteomes:UP000054924};
RN [1] {ECO:0000313|EMBL:KRZ93080.1, ECO:0000313|Proteomes:UP000054924}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ISS272 {ECO:0000313|EMBL:KRZ93080.1};
RA Korhonen P.K., Edoardo P., Giuseppe L.R., Gasser R.B.;
RT "Evolution of Trichinella species and genotypes.";
RL Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC -!- SIMILARITY: Belongs to the AAA ATPase family.
CC {ECO:0000256|ARBA:ARBA00006914, ECO:0000256|RuleBase:RU003651}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KRZ93080.1}.
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DR EMBL; JYDM01000028; KRZ93080.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0V1PAB9; -.
DR STRING; 92180.A0A0V1PAB9; -.
DR Proteomes; UP000054924; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
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 GO; GO:0008233; F:peptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd19502; RecA-like_PAN_like; 1.
DR CDD; cd12337; RRM1_SRSF4_like; 1.
DR Gene3D; 1.10.8.60; -; 1.
DR Gene3D; 3.30.70.330; -; 2.
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; IPR012677; Nucleotide-bd_a/b_plait_sf.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR032501; Prot_ATP_ID_OB_2nd.
DR InterPro; IPR035979; RBD_domain_sf.
DR InterPro; IPR000504; RRM_dom.
DR PANTHER; PTHR23073; 26S PROTEASOME REGULATORY SUBUNIT; 1.
DR PANTHER; PTHR23073:SF24; 26S PROTEASOME REGULATORY SUBUNIT 4; 1.
DR Pfam; PF00004; AAA; 1.
DR Pfam; PF17862; AAA_lid_3; 1.
DR Pfam; PF16450; Prot_ATP_ID_OB_C; 1.
DR Pfam; PF00076; RRM_1; 2.
DR SMART; SM00382; AAA; 1.
DR SMART; SM00360; RRM; 2.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF54928; RNA-binding domain, RBD; 1.
DR PROSITE; PS00674; AAA; 1.
DR PROSITE; PS50102; RRM; 2.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|RuleBase:RU003651};
KW Hydrolase {ECO:0000313|EMBL:KRZ93080.1};
KW Nucleotide-binding {ECO:0000256|RuleBase:RU003651};
KW Protease {ECO:0000313|EMBL:KRZ93080.1};
KW Proteasome {ECO:0000256|ARBA:ARBA00022942};
KW Reference proteome {ECO:0000313|Proteomes:UP000054924};
KW RNA-binding {ECO:0000256|PROSITE-ProRule:PRU00176}.
FT DOMAIN 14..84
FT /note="RRM"
FT /evidence="ECO:0000259|PROSITE:PS50102"
FT DOMAIN 131..203
FT /note="RRM"
FT /evidence="ECO:0000259|PROSITE:PS50102"
FT REGION 101..123
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 197..261
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 103..123
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 209..224
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 225..249
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KRZ93080.1"
SQ SEQUENCE 656 AA; 74688 MW; C47236C4D2E0E164 CRC64;
LFEISILTRT MESTRVYVGQ LTSDIRENDL ENFFKGYGRI REITLKNGYG FVEFDERRDA
DDAVHDLNGK PLLGEKIRVE MAHRFSRDRF ASGRGGGFRG RYNGDRGYDR SRHGGRWERR
RPVNPPRRSR YRLLVENLSS AISWRELKDF MNQAGEVCFT DVYPQRREGI VEFESSSAME
NALKKLNGEE LNGRRIRITE EKLDSNKSNR NRNSVMGQQQ SAHGHGFNRD KKDDKDKKRR
YEPPIPTRVG KKKRRAKGPD AAVKLPHITP HARCRLKLLK AERIKDYLLL EEEFLKNIQI
AKPQEERQEE ERGKVDDLRG SPMAVGTLEE VIDDTHAIVS TSVGSEHYVT ILSFVDKDQL
EPGCTVLLNH KTHSVIGVLT DDTDPMVSVM KLEKAPKETY ADVGGLDNQI QEIKESVELP
LTHPELYEEM GIRPPKGVIL YGAPGTGKTL LAKAVANQTS ATFLRVVGSE LIQKYLGDGP
KLVRELFRVA EEHAPSIVFI DEIDAIGTKR YESNSGGERE IQRTMLELLN QLDGFDSRGD
VKVIMATNRI ETLDPALIRP GRIDRKIEFP LPDEVTIRKI FQIHTSRMTI ADNVDFEEFI
MAKDDLSGAD IKAICTEAGL QALRDRRMKV THEDFKKARE SVLYRKKEGA PSGLYI
//
