ID A0A0V1NZ41_9BILA Unreviewed; 1590 AA.
AC A0A0V1NZ41;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE SubName: Full=RNA-binding protein 26 {ECO:0000313|EMBL:KRZ89173.1};
GN Name=swp-1 {ECO:0000313|EMBL:KRZ89173.1};
GN ORFNames=T08_3606 {ECO:0000313|EMBL:KRZ89173.1};
OS Trichinella sp. T8.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Trichinellida; Trichinellidae; Trichinella.
OX NCBI_TaxID=92180 {ECO:0000313|EMBL:KRZ89173.1, ECO:0000313|Proteomes:UP000054924};
RN [1] {ECO:0000313|EMBL:KRZ89173.1, ECO:0000313|Proteomes:UP000054924}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ISS272 {ECO:0000313|EMBL:KRZ89173.1};
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 -!- FUNCTION: May be involved in the turnover of nuclear polyadenylated
CC (pA+) RNA. {ECO:0000256|ARBA:ARBA00043866}.
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:KRZ89173.1}.
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DR EMBL; JYDM01000074; KRZ89173.1; -; Genomic_DNA.
DR Proteomes; UP000054924; Unassembled WGS sequence.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR GO; GO:0006397; P:mRNA processing; IEA:InterPro.
DR CDD; cd12257; RRM1_RBM26_like; 1.
DR Gene3D; 3.30.70.330; -; 1.
DR Gene3D; 1.10.10.790; Surp module; 2.
DR InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
DR InterPro; IPR002483; PWI_dom.
DR InterPro; IPR035979; RBD_domain_sf.
DR InterPro; IPR045137; RBM26/27.
DR InterPro; IPR000504; RRM_dom.
DR InterPro; IPR000061; Surp.
DR InterPro; IPR035967; SWAP/Surp_sf.
DR InterPro; IPR019147; SWAP_N_domain.
DR InterPro; IPR000571; Znf_CCCH.
DR InterPro; IPR036855; Znf_CCCH_sf.
DR PANTHER; PTHR14398; RNA RECOGNITION RRM/RNP DOMAIN; 1.
DR PANTHER; PTHR14398:SF0; ZINC FINGER PROTEIN SWM; 1.
DR Pfam; PF09750; DRY_EERY; 1.
DR Pfam; PF01480; PWI; 1.
DR Pfam; PF01805; Surp; 2.
DR Pfam; PF00642; zf-CCCH; 1.
DR SMART; SM01141; DRY_EERY; 1.
DR SMART; SM00360; RRM; 1.
DR SMART; SM00648; SWAP; 2.
DR SMART; SM00356; ZnF_C3H1; 1.
DR SUPFAM; SSF90229; CCCH zinc finger; 1.
DR SUPFAM; SSF54928; RNA-binding domain, RBD; 2.
DR SUPFAM; SSF109905; Surp module (SWAP domain); 2.
DR PROSITE; PS50128; SURP; 2.
DR PROSITE; PS50103; ZF_C3H1; 1.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|PROSITE-
KW ProRule:PRU00723}; Reference proteome {ECO:0000313|Proteomes:UP000054924};
KW RNA-binding {ECO:0000256|ARBA:ARBA00022884};
KW Transcription {ECO:0000256|ARBA:ARBA00023163};
KW Transcription regulation {ECO:0000256|ARBA:ARBA00023015};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|PROSITE-ProRule:PRU00723};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00723}.
FT DOMAIN 179..221
FT /note="SURP motif"
FT /evidence="ECO:0000259|PROSITE:PS50128"
FT DOMAIN 338..378
FT /note="SURP motif"
FT /evidence="ECO:0000259|PROSITE:PS50128"
FT DOMAIN 944..972
FT /note="C3H1-type"
FT /evidence="ECO:0000259|PROSITE:PS50103"
FT ZN_FING 944..972
FT /note="C3H1-type"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00723"
FT REGION 132..158
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 238..275
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 592..637
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 650..711
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 820..950
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1021..1054
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1547..1590
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 1319..1356
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 1406..1433
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 135..157
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 238..256
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 600..617
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 623..637
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 654..692
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 824..860
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 883..905
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 906..927
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 936..950
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1025..1048
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1565..1590
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1590 AA; 180077 MW; 996FA2332750373A CRC64;
MIAIISKFIN KLQLSNLLRE ESSDEFLAFG YPCKLFDSRG GRDCADESAD LIPLHCNRKI
LVDRFDCRLQ LSNLEKYDAS KVEQSLLIAD RSLEALLDAE RYRDFKLTCE TPKVENEKRM
GTEIYFNYDD LESKPQHGCQ PKEEAEGTED EQKEQFVPPA ELKVPVGVTL PKTVKEGIII
EKTAAFIAEQ GSQMEIIVNA KQKSNPQFRF LDWNHPLNKY YKHVLKMIKE KRYTPVVVKK
DPAPESESDS DDSSEHYLHP SLMGGAGKTA VAKDTEPLSL PKTSYRLGEE NDVYSELFNG
LVAVCPQLAA AVSTAKGKET GGSAEGLLLP PPPDLYPVVD RVAAYVARNG PQFEQILRER
NDPRFSFIDP SNKYNPYYMA LLQNYESVPM SLNYLSYYGF VPQPPPPPRS TPPPPAVENQ
EETLNLKKTK TVYCSDHLTS AAASSSVSEK PTEMGSVGPV CFTIKAKNQE ETCSMMDKAN
LDAHQDETIN LSLQSDSDVL MSDCAEKFDC KFVDGSGDAA ESTVKSVDEY MQREITTFPE
VGKKEQKNVE EDLKLKRARR YRAKKFVDEF AKKIRKREKS CVDEEKVKKH GHISEGELCD
SESSESTLIG TSSNASYGSE KKKKRKKKEE ESKGRLMNFD KLPLSYAKCM KLNERSRSRR
RRRSKSSSHS RHRKSTEDRR RRRRRSRKRT SGSRSSRSTT STRRYYSSRH RRSRSITKMF
VDQPEQLKNW LINTLSPLYH LKLYTKYLVV IELLCSRCDA DPAALAKYVM ALLKKDKTEA
DLKHFCLDQL DVFLQKETKK FVDELFLALK SKVYIVTDKE SQSTSTKEVP KKRSLEPSRN
EKPSADEHLK SRRVDSHSGS RPVRRYGSSP KARSKSSERS KGKGDATSVS QNKASSSTVR
DRVKAHWSPS NNKEQRKSTH KDSNEAVGNA ENDSVQSIRS EKEKRKKARC RDYDEKGYCM
LGDNCVYDHG PDPVVVEDVA LSSMIPMKDG TGRSNKSLPT PPPNFSVPPP GYVPIPPPPP
GVDSNFQTEG YNPEAPSLTS ASTGTAVPLP PPYTQPPPPI WAQLPPVLRP FGPRQIASYA
QLRVSFPRAR QLITLSEDRT NFDNFSQSTM RTQHKSVGQI NLRKRAAVDQ INRQNRTLEV
RRIPQPLNTI TKLNEHFSQF GHITNIEVCY EGDPQAALIT YMTRPQALAA YKSTDPILNN
RFIRVFWHNQ KDGTAVDDTG TPDQSSRPAR IPIRDRLELP VKSSSNGTSS HEEAIFKAET
NATAANTGSD TISTTMNKMD GDAFATKSVR LVHNADAEVK NPMANVTSSK GENTKRILKK
RLELQRAETE LFNRQLEQEK LLLKKLEDCK DQTTKELIIK TLKKLEISLI ATKKNLESRD
FSKFVKRSKT EVQRDVLDAE LELITKKKAG EDITEIAVRL QNLRKEMQHL NDTESNNKHC
RNSAYRPERN RRIPRSAVLD LRSRSILITD FCMEHKDALI EHLQQFGTLR DIDFYPLTDP
AVGKVIASFY DRKEAERAFT DGKLFKDQLL NMTWAVEDKD AMAAALSSGS KSDLSAKALL
KTLDPPDDDD DDDDLFEENE EVEEEEQQLT
//
