ID A0A0V0UA65_9BILA Unreviewed; 1589 AA.
AC A0A0V0UA65;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE SubName: Full=RNA-binding protein 26 {ECO:0000313|EMBL:KRX47651.1};
DE Flags: Fragment;
GN Name=swp-1 {ECO:0000313|EMBL:KRX47651.1};
GN ORFNames=T05_4719 {ECO:0000313|EMBL:KRX47651.1};
OS Trichinella murrelli.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Trichinellida; Trichinellidae; Trichinella.
OX NCBI_TaxID=144512 {ECO:0000313|EMBL:KRX47651.1, ECO:0000313|Proteomes:UP000055048};
RN [1] {ECO:0000313|EMBL:KRX47651.1, ECO:0000313|Proteomes:UP000055048}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ISS417 {ECO:0000313|EMBL:KRX47651.1};
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:KRX47651.1}.
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DR EMBL; JYDJ01000040; KRX47651.1; -; Genomic_DNA.
DR Proteomes; UP000055048; 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:UP000055048};
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 943..971
FT /note="C3H1-type"
FT /evidence="ECO:0000259|PROSITE:PS50103"
FT ZN_FING 943..971
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..636
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 649..710
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 819..949
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1020..1053
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1546..1589
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 1318..1355
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 1405..1432
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 618..636
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 653..691
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 823..859
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 882..904
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 905..926
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 935..949
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1024..1047
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1564..1589
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1589
FT /evidence="ECO:0000313|EMBL:KRX47651.1"
SQ SEQUENCE 1589 AA; 179967 MW; 5773A6CC0156CA2F 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 ETCLMMDKAN
LDAHQDETIN LSLQSDSDVL MSDCAEKFDC KFVDGSGDAA ESTVKSVDEY MQREITTFPE
VGKKEQKNVE EDLNLKRARR YRAKKFVDEF AKKIRKREKS CVDEEKVKKH GHISEGELCD
SESSESTLIG TSSNASYGSE KKKKRKKEEE SKGRLMNFDK LPLSYAKCMK LNERSRSRRR
RRSKSSSHSR HRKSTEDRRR RRRRSRKRTS GSRSSRSTTS TRRYYSSRHR RSRSITKMFV
DQPEQLKNWL INTLSPLYHL KLYTKYLVVI ELLCSRCDAD PAALAKYVMA LLKKDKTEAD
LKHFCLDQLD VFLQKETKKF VDELFLALKS KVYIVTDKES QSTSTKEVPK KRSLEPSRNE
KPSADEHLKS RRVDSHSGSR PVRRYGSSPK ARSKSSERSK GKGDATSISQ NKASSSTVRD
RVKTHWSPSN NKEQRKSTHK DSNEAVGNAE NDSVQSIRSE KEKRKKARCR DYDEKGYCML
GDNCVYDHGP DPVVVEDVAL SSMIPMKDGT GRSNKSLPTP PPNFSVPPPG YVPIPPPPPG
VDSNFQTEGY NPEAPSLTSA STGTAVPLPP PYTQPPPPIW AQLPPVLRPF GPRQIASYAQ
LRVSFPRARQ LITLSEDRTN FDNFSQSTMR TQHKSVGQIN LRKRAAVDQI NRQNRTLEVR
RIPQPLNTIT KLNEHFSQFG HITNIEVCYE GDPQAALITY MTRPQALAAY KSTDPILNNR
FIRVFWHNQK DGTAVDDTGT SDQSSRPARI PIRDRLELPV KSSSNGTSSH EEAIFKAETN
ATAANTGSDT ISTTMNKMDG DAFATKSVRL VHNADAEVKN PMANVAASKG ENTKRILKKR
LELQRAETEL FNRQLEQEKL LLKKLEDCKD QTTKELIIKT LKKLEISLMA TKKNLESRDF
SKFVKRSKTE VQRDVLDAEL ELITKKKAGE DITEIAVRLQ NLRKEMQHLN DTESNNKHCR
NSAYRPERNR RIPRSAVLDL RSRSILITDF CMEHKDALIE HLQQFGTLRD IDFYPLTDPA
VGKVIASFYD RKEAERAFTD GKLFKDQLLN MTWAVEDKDA MAAALSSGSK SDLSAKALLK
TLDPPDDDDD DDDLFEENEE VEEEEQQLT
//
