ID A0A0V0WQH6_9BILA Unreviewed; 1603 AA.
AC A0A0V0WQH6;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE SubName: Full=RNA-binding protein 26 {ECO:0000313|EMBL:KRX77959.1};
GN Name=swp-1 {ECO:0000313|EMBL:KRX77959.1};
GN ORFNames=T06_13998 {ECO:0000313|EMBL:KRX77959.1};
OS Trichinella sp. T6.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Trichinellida; Trichinellidae; Trichinella.
OX NCBI_TaxID=92179 {ECO:0000313|EMBL:KRX77959.1, ECO:0000313|Proteomes:UP000054673};
RN [1] {ECO:0000313|EMBL:KRX77959.1, ECO:0000313|Proteomes:UP000054673}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ISS34 {ECO:0000313|EMBL:KRX77959.1};
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:KRX77959.1}.
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DR EMBL; JYDK01000074; KRX77959.1; -; Genomic_DNA.
DR Proteomes; UP000054673; 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; 1.20.1390.10; PWI domain; 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:UP000054673};
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 193..235
FT /note="SURP motif"
FT /evidence="ECO:0000259|PROSITE:PS50128"
FT DOMAIN 352..392
FT /note="SURP motif"
FT /evidence="ECO:0000259|PROSITE:PS50128"
FT DOMAIN 957..985
FT /note="C3H1-type"
FT /evidence="ECO:0000259|PROSITE:PS50103"
FT ZN_FING 957..985
FT /note="C3H1-type"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00723"
FT REGION 146..172
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 252..289
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 635..669
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 682..743
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 832..963
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1035..1067
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1560..1603
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 1332..1369
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 1419..1446
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 149..171
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 252..270
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 635..649
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 655..669
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 686..724
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 837..873
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 896..918
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 919..940
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 949..963
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1038..1061
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1578..1603
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1603 AA; 181747 MW; BAA3138F0310B02E CRC64;
MIAIISKFIN KLQLSNLLRE ESSDEFLAFG YPCKLFDSRG GRDCADESAD LIPLHCNRKI
LVDRIMSLFG YQMDFITEFD CRLQLSNLEK YDASKVEQSL LIADRSLEAL LDAERYRDFK
LTCETPKVEN EKRMGTEIYF NYDDLESKPQ HGCQPKEEAE GTEDEQKEQF VPPAELKVPV
GVTLPKTVKE GIIIEKTAAF IAEQGSQMEI IVNAKQKSNP QFRFLDWNHP LNKYYKHVLK
MIKEKRYTPV VVKKDPAPES ESDSDDSSEH YLHPSLMGGA GKTAVAKDTE PLSLPKTSYR
LGEENDVYSE LFNGLVAVCP QLAAAVSTAK GKETGGSAEG LLLPPPPDLY PVVDRVAAYV
ARNGPQFEQI LRERNDPRFS FIDPSNKYNP YYMALLQNYE SENYIVRLQQ NVQNQFVEGV
PMSLNYLSYY GFVPQPPPPP RSTPPPPAVE NQEETLNLKK TKTVYCSDHL TSAAASSSVS
EKPTEMGSVG PVCFTIKAKN QEETYSMMDK ANLDAHQGET INLSLQSDSD VLMSDCAEKF
DCKFVDGSGD AAESTVKSVD EYMQREITTF PEVGKKEQKN VEKDLNLKRA RRYRAKKFVD
EFAKKIRKRE KSCVDEEKVK KHGHISEGEL CDSESSESTL FGTSSNASYG SEKKKKRKKK
EEESKRRLMN FDKLPLSYAK CMKLNERSRS RRRRRSKSSS HSRHRKSTED RRRRRRRSRK
RTSGSRSSRS TTSMRRYYSS RHRRSRSITK MFVDQPEQLK NWLINTLSPL CDADPAALAK
YVMALLKKDK TEADLKHFCL DQLDVFLQKE TKKFVDELFL ALKSKVYIVT DKESQSTSTK
EVPKKRSLEP SRNEKPSAEE HLKSRRVDSH SGSRPVRRYG SSPKARSKSS ERSKGKGDAT
SISQNKASSS TVRDRVKTHW SPSNNKEQRK STHKDSNEAV GNAENDSVQS IRSEKEKRKK
ARCRDYDEKG YCMLGDNCVY DHGPDPVVVE DVALSSMIPM KDGTGRSNKS LPTPPPNFSV
PPPGYVPIPP PPPGVDSNFQ TEGYNPEAPS LTSASTGTAV PLPPPYTQPP PPIWAQLPPV
LRPFGPRQIA SYAQLRVSFP RARQLITLSE DRTNFDNFSQ STMRTQHKSV GQINLRKRAA
VDQINRQSRT LEVRRIPQPL NTITKLNEHF SQFGHITNIE VCYEGDPQAA LITYMTRPQA
LAAYKSTDPI LNNRFIRVFW HNQKDGTAVD DTGTSDQSSR PARIPIRDRL ELPVKSSSNG
TSSHEEAIFK AETNATAANT GSDTISTTMN KMDGDAFATK SVRLVHNADA EVKSPMANVA
ASKGENTKRI LKKRLELQRA ETELFNRQLE QEKLLLKKLE DCKDQTTKEL IIKTLKKLEI
SLMATKKNLE SRDFSKFVKR SKTEVQRDVL DAELELITKK KAGEDITEIA VRLQNLRKEM
QHLNDTESNN KHCRNSAYRP ERNRRIPRSA VLDLRSRSIL ITDFRMEHKD ALIEHLQQFG
TLRDIDFYPL TDPAVGKVIA SFYDRKEAER AFTDGKLFKD QLLNMTWAVE DKDAMAAALS
SGSKSDLSAK ALLKTLDPPD DDDDDDDLFE ENEEVEEEEQ QLT
//
