ID A0A0V1CUF6_TRIBR Unreviewed; 719 AA.
AC A0A0V1CUF6;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 41.
DE SubName: Full=26S protease regulatory subunit 4 {ECO:0000313|EMBL:KRY52922.1};
DE Flags: Fragment;
GN Name=Srsf4 {ECO:0000313|EMBL:KRY52922.1};
GN ORFNames=T03_7703 {ECO:0000313|EMBL:KRY52922.1};
OS Trichinella britovi (Parasitic roundworm).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Trichinellida; Trichinellidae; Trichinella.
OX NCBI_TaxID=45882 {ECO:0000313|EMBL:KRY52922.1, ECO:0000313|Proteomes:UP000054653};
RN [1] {ECO:0000313|EMBL:KRY52922.1, ECO:0000313|Proteomes:UP000054653}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ISS120 {ECO:0000313|EMBL:KRY52922.1};
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}.
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:KRY52922.1}.
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DR EMBL; JYDI01000096; KRY52922.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0V1CUF6; -.
DR Proteomes; UP000054653; 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:InterPro.
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 Hydrolase {ECO:0000313|EMBL:KRY52922.1};
KW Protease {ECO:0000313|EMBL:KRY52922.1};
KW Proteasome {ECO:0000256|ARBA:ARBA00022942};
KW Reference proteome {ECO:0000313|Proteomes:UP000054653};
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 199..250
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 282..323
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 199..220
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 221..235
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 288..312
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KRY52922.1"
SQ SEQUENCE 719 AA; 81615 MW; 7038C62E41A2BB31 CRC64;
LFEISILTRT MESTRVYVGQ LTSDIRENDL ENFFKGYGRI REITLKNGYG FVEFDERRDA
DDAVHDLNGK PLLGEKIRVE MAHRFSRDRF ASGRGGGFRG RYNGDRGYDR SRHGGRWERR
RPVNPPRRSR YRLLVENLSS AISWRELKDF MNQAGEVCFT DVYPQRREGI VEFESSSAME
NALKKLNGEE LNGRRIRITE EKLDSNKSNR NRKSKSRESS RSSSSRGSSK SKQSADSETA
EAKRKQHNNS SSANCMILLS ELENPYCGDY YCTVVYSVMG QQQSAHGHGF NRDKKDDKDK
KRRYEPPIPT RVGKKKRRAK GPDAAVKLPH ITPHARCRLK LLKAERIKDY LLLEEEFLKN
IQIAKPQEER QEEERGKVDD LRGSPMAVGT LEEVIDDTHA IVSTSVGSEH YVTILSFVDK
DQLEPGCTVL LNHKTHSVIG VLTDDTDPMV SVMKLEKAPK ETYADVGGLD NQIQEIKESV
ELPLTHPELY EEMGIRPPKG VILYGAPGTG KTLLAKAVAN QTSATFLRVV GSELIQKYLG
DGPKLVRELF RVAEEHAPSI VFIDEIDAIG TKRYESNSGG EREIQRTMLE LLNQLDGFDS
RGDVKVIMAT NRIETLDPAL IRPGRIDRKI EFPLPDEVTI RKIFQIHTSR MTIADNVDFE
EFIMAKDDLS GADIKAICTE AGLQALRDRR MKVTHEDFKK ARESVLYRKK EGAPSGLYI
//
