ID A0A0V0ZQT4_9BILA Unreviewed; 1043 AA.
AC A0A0V0ZQT4;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE SubName: Full=Putative splicing factor, arginine/serine-rich 7 {ECO:0000313|EMBL:KRY14897.1};
GN Name=rsp-7 {ECO:0000313|EMBL:KRY14897.1};
GN ORFNames=T12_16585 {ECO:0000313|EMBL:KRY14897.1};
OS Trichinella patagoniensis.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Trichinellida; Trichinellidae; Trichinella.
OX NCBI_TaxID=990121 {ECO:0000313|EMBL:KRY14897.1, ECO:0000313|Proteomes:UP000054783};
RN [1] {ECO:0000313|EMBL:KRY14897.1, ECO:0000313|Proteomes:UP000054783}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ISS2496 {ECO:0000313|EMBL:KRY14897.1};
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 -!- 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:KRY14897.1}.
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DR EMBL; JYDQ01000106; KRY14897.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0V0ZQT4; -.
DR STRING; 990121.A0A0V0ZQT4; -.
DR Proteomes; UP000054783; Unassembled WGS sequence.
DR GO; GO:0004364; F:glutathione transferase activity; IEA:UniProt.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-UniRule.
DR CDD; cd03076; GST_N_Pi; 1.
DR CDD; cd12259; RRM_SRSF11_SREK1; 1.
DR Gene3D; 1.20.1050.10; -; 1.
DR Gene3D; 3.30.70.330; -; 2.
DR Gene3D; 3.40.30.10; Glutaredoxin; 1.
DR InterPro; IPR010987; Glutathione-S-Trfase_C-like.
DR InterPro; IPR036282; Glutathione-S-Trfase_C_sf.
DR InterPro; IPR004045; Glutathione_S-Trfase_N.
DR InterPro; IPR004046; GST_C.
DR InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
DR InterPro; IPR035979; RBD_domain_sf.
DR InterPro; IPR000504; RRM_dom.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR PANTHER; PTHR11571; GLUTATHIONE S-TRANSFERASE; 1.
DR PANTHER; PTHR11571:SF141; GLUTATHIONE S-TRANSFERASE P; 1.
DR Pfam; PF14497; GST_C_3; 1.
DR Pfam; PF02798; GST_N; 1.
DR Pfam; PF00076; RRM_1; 1.
DR SFLD; SFLDG01205; AMPS.1; 1.
DR SFLD; SFLDG00363; AMPS_(cytGST):_Alpha-__Mu-__Pi; 1.
DR SMART; SM00360; RRM; 2.
DR SUPFAM; SSF47616; GST C-terminal domain-like; 1.
DR SUPFAM; SSF54928; RNA-binding domain, RBD; 2.
DR SUPFAM; SSF52833; Thioredoxin-like; 1.
DR PROSITE; PS50405; GST_CTER; 1.
DR PROSITE; PS50404; GST_NTER; 1.
DR PROSITE; PS50102; RRM; 1.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000054783};
KW RNA-binding {ECO:0000256|PROSITE-ProRule:PRU00176}.
FT DOMAIN 54..131
FT /note="GST N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS50404"
FT DOMAIN 132..251
FT /note="GST C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS50405"
FT DOMAIN 409..485
FT /note="RRM"
FT /evidence="ECO:0000259|PROSITE:PS50102"
FT REGION 529..853
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 878..1043
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 535..557
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 578..593
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 607..626
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 627..642
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 643..664
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 671..698
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 710..728
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 733..752
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 753..780
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 812..835
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 836..853
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 878..893
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 913..940
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 959..1001
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1002..1023
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1024..1043
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1043 AA; 119765 MW; 038326E0634BF2BE CRC64;
MSTDAVDSTP EVPLARSKCA FNFQFRVCSC LLLQICNFQC LSNSLKVATL AKMPLYKLVY
FDIRGLAEPI RLLLHDQRVQ FLDNRIQQKD WPEMKSQMLF GQVPCLYEDD QPIVQSGAIM
RHLGRRFGLY GNAEEMTYVD QIYEGVVDLR LKYARLIYSD SFHDSKGKFV NEVLPDELAK
FEKILTRKKY ILDDEITFAD YALAELLDVL LILSSSCLEN FTALTIYHSR FMNRPNLKNY
LSSDIQNERR WNEKVHLVQI SSISPLLTRE QIYHMFSYFG RIEEFRMYPT DTNQTNFIGQ
TKLCYIRYVR SSSADTAQHM TNTVFIDRAL ICVPVPEGKI PEEDMALMLG GPTLPGQRQL
PLGVVSETRH VDGRDLIVTI DPKLTQLGLP AYPPLSGSLP MSTVEEVRRT VFISGLAADV
DKYDLMMFLN DNIGEVMYLR MAGRRDAAQR CAYVEFSSQL SVVNALQKNG LLYKGQRLRM
WHSNTSIAKP LAKTLDMAKK EVEEAVRQSG ILATAAPFNE DEVDRLIQRA NSPLYHRGSR
RHSRRRSRSR RRYSRSRDRS PRTPPRRYFI RSSTPPHLRL RRLSRRRDRR RRRSSTSSGS
SYQRSRPEKS TARKNDSRER KSPKKDPLAS SSSSFKRSRG SRSPAETSSK ELKKRTEMEL
KFVENEADLV NLQPNEEKGK EKKHDKNDSP KRSSRSNVND EAKPLFLKTK ASSSHRRHHY
RHHRHHRLQQ QDSKQDPSLT KSTKQHNDSK SSNDSQNSKE NKSESNIDDS DSKEKKTELS
TLTPETLSKK KFISGLDELS VKGSNSDSMK ANTTDEQEEP PPENKRHRSE YDCAEVTELS
KSQNEGQNFS SPMVRLKSET VKIDGGATMV TAAEAASVEL EEKKKSQNDE RSAVDEDESL
ELDLSGGRSQ VQIDKQRSKE SSSKKHHRSS EKKNRTVELS KSFEKGSSLS SRRKPRKKND
RSPTPDRKED RHRRRKYQQD AVELSKRSRK VESSGQDRKE KYSKRGKRKS KRTSSRHGRS
TRRVRSSSSS SSSTATSSTD SRS
//
