ID A0A0V1HYB2_9BILA Unreviewed; 1208 AA.
AC A0A0V1HYB2;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE SubName: Full=Putative splicing factor, arginine/serine-rich 7 {ECO:0000313|EMBL:KRZ15593.1};
GN Name=rsp-7 {ECO:0000313|EMBL:KRZ15593.1};
GN ORFNames=T11_8891 {ECO:0000313|EMBL:KRZ15593.1};
OS Trichinella zimbabwensis.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Trichinellida; Trichinellidae; Trichinella.
OX NCBI_TaxID=268475 {ECO:0000313|EMBL:KRZ15593.1, ECO:0000313|Proteomes:UP000055024};
RN [1] {ECO:0000313|EMBL:KRZ15593.1, ECO:0000313|Proteomes:UP000055024}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ISS1029 {ECO:0000313|EMBL:KRZ15593.1};
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:KRZ15593.1}.
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DR EMBL; JYDP01000017; KRZ15593.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0V1HYB2; -.
DR STRING; 268475.A0A0V1HYB2; -.
DR Proteomes; UP000055024; 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; cd03039; GST_N_Sigma_like; 1.
DR CDD; cd12259; RRM_SRSF11_SREK1; 1.
DR Gene3D; 1.20.1050.10; -; 2.
DR Gene3D; 3.30.70.330; -; 2.
DR Gene3D; 3.40.30.10; Glutaredoxin; 2.
DR InterPro; IPR010987; Glutathione-S-Trfase_C-like.
DR InterPro; IPR036282; Glutathione-S-Trfase_C_sf.
DR InterPro; IPR040079; Glutathione_S-Trfase.
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; 2.
DR Pfam; PF02798; GST_N; 2.
DR Pfam; PF00076; RRM_1; 1.
DR SFLD; SFLDG01205; AMPS.1; 1.
DR SFLD; SFLDG00363; AMPS_(cytGST):_Alpha-__Mu-__Pi; 1.
DR SFLD; SFLDS00019; Glutathione_Transferase_(cytos; 1.
DR SMART; SM00360; RRM; 2.
DR SUPFAM; SSF47616; GST C-terminal domain-like; 2.
DR SUPFAM; SSF54928; RNA-binding domain, RBD; 2.
DR SUPFAM; SSF52833; Thioredoxin-like; 2.
DR PROSITE; PS50405; GST_CTER; 2.
DR PROSITE; PS50404; GST_NTER; 2.
DR PROSITE; PS50102; RRM; 1.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000055024};
KW RNA-binding {ECO:0000256|PROSITE-ProRule:PRU00176}.
FT DOMAIN 3..81
FT /note="GST N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS50404"
FT DOMAIN 101..194
FT /note="GST C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS50405"
FT DOMAIN 206..283
FT /note="GST N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS50404"
FT DOMAIN 284..403
FT /note="GST C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS50405"
FT DOMAIN 561..637
FT /note="RRM"
FT /evidence="ECO:0000259|PROSITE:PS50102"
FT REGION 681..805
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 817..950
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1012..1208
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 686..709
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 718..752
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 754..779
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 817..850
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 862..885
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 886..907
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 908..942
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1041..1063
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1075..1106
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1113..1167
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1168..1190
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1191..1208
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1208 AA; 139397 MW; 0E0E957EBB3E0597 CRC64;
MAPIYKLSYF DVRGLAEPIR LLLHDQKIEF IDHRFDRNEW TKIKPTILKF GQVPCLYENG
NAIVQSGAIM RHLGRRFGRK CGNSFDNFNE ITISALDLYG NANEMTYVDE IYDGICDLRK
KYAPFIYTEC SEGEVEKFTK EVLLVELQKF ENLLKGKKYI LNDKISFADY SLFDMLDTLL
TLSPACLFSF PSLKNNLKVA TFAMAPKYKL TYFAIRGLAE PIRLLLHDQK VNFDDERIEK
KDWPEIKPKM LFGQLPCLYE DDKPIVQSGA IMRHLGRRFG LYGNADEMTY VDVVYEGIVD
LRLKYARLIY GDFCNESKCK FVNEVLPVEL ARFEKLLTGK KYILNDEITF ADYALVEILD
VLLVLSSTCL EKFPALKTFH AHFMDRPNLK KYLSSDFQSE RKWNEKVHLV QISSISPLLT
REQIYHMFSY FGRIEEFRMY PSDTNPSNFI GQTKLCYIRY VRSSSADTAQ HMTNTVFIDR
ALICVPVPEG KIPEEDVALM LGGPTLPGQR QLPLGVVSEA RHVDGRDLIV TIDPKLTQLG
LPAYPPLSGS LPMSTVEEIR RTVFISGLAA DVDKYDLMMF LNDNIGEVMY LRMAGRRDAA
QRCAYVEFSS QLSVVNALQK NGLLYKGQKL RMWHSNTSIA KPLAKTLDMA KKEVEEAVRQ
SGILATATPF NEDEVDRLIQ RANSPLYHHR SRRHSRRRSR SRRRYSRSRD RSPRTPPRRY
HIRSSTPPHL RPRRRSRRRD RRRRRSNSSS GSLHRHRSRL DKSTARRNAS RERKSPKKDV
LGSSSSFKRS RGSRSPAEAG SKELKKRIEM ESKFVENEAD LVDVQPNEER AKEKKHDKND
SPKHSSRSNV NEEVRSLFLK AKNSNSHRRH HYRHHHRHRH HRQQQQPQPQ HCSDSKQDPS
VMKSIKQIDK SNDSKSSKEC KENKNKSYID DSDLKERKAE LSSTLTPESL SKKKFIDGLD
ELLVKDSNID SMKANTTDEQ EELLSPENKR HRSEYSCAEV IECSQWKDKR QTFSSPMAKL
KSETGEKDGA TMATAAEAEV EAVDLEEKKN SQNDERSAID EDHLLEVNLS GGQSRVEDID
DKQQSKESSS KKYRSSEKKI RSVELSKSFE EGSSSSSRRK PKKKSDRSPT PERKEDRHRR
RKHQQDAVEL LKRSSKVDTS GQQYRKEKYS KRGKRKSKHR SSKHGRSTRR VHSSSSSSAT
TSSTVSHC
//
