ID A0A0V0WZS1_9BILA Unreviewed; 696 AA.
AC A0A0V0WZS1;
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:KRX81144.1};
GN Name=Srsf4 {ECO:0000313|EMBL:KRX81144.1};
GN ORFNames=T06_13548 {ECO:0000313|EMBL:KRX81144.1};
OS Trichinella sp. T6.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Trichinellida; Trichinellidae; Trichinella.
OX NCBI_TaxID=92179 {ECO:0000313|EMBL:KRX81144.1, ECO:0000313|Proteomes:UP000054673};
RN [1] {ECO:0000313|EMBL:KRX81144.1, ECO:0000313|Proteomes:UP000054673}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ISS34 {ECO:0000313|EMBL:KRX81144.1};
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:KRX81144.1}.
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DR EMBL; JYDK01000034; KRX81144.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0V0WZS1; -.
DR STRING; 92179.A0A0V0WZS1; -.
DR Proteomes; UP000054673; 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:KRX81144.1};
KW Nucleotide-binding {ECO:0000256|RuleBase:RU003651};
KW Protease {ECO:0000313|EMBL:KRX81144.1};
KW Proteasome {ECO:0000256|ARBA:ARBA00022942};
KW Reference proteome {ECO:0000313|Proteomes:UP000054673};
KW RNA-binding {ECO:0000256|PROSITE-ProRule:PRU00176}.
FT DOMAIN 54..124
FT /note="RRM"
FT /evidence="ECO:0000259|PROSITE:PS50102"
FT DOMAIN 171..243
FT /note="RRM"
FT /evidence="ECO:0000259|PROSITE:PS50102"
FT REGION 141..163
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 237..301
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 143..163
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 249..264
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 265..289
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 696 AA; 78884 MW; E822BBB72509E539 CRC64;
MMALQSVSQC ASSASASSES LQPVYSIDDQ FGRWEKGGCA 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
//
