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Database: UniProt
Entry: A0A0V1N073_9BILA
LinkDB: A0A0V1N073_9BILA
Original site: A0A0V1N073_9BILA 
ID   A0A0V1N073_9BILA        Unreviewed;      1541 AA.
AC   A0A0V1N073;
DT   16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT   16-MAR-2016, sequence version 1.
DT   27-MAR-2024, entry version 26.
DE   SubName: Full=RNA-binding protein 26 {ECO:0000313|EMBL:KRZ77338.1};
GN   Name=swp-1 {ECO:0000313|EMBL:KRZ77338.1};
GN   ORFNames=T10_9180 {ECO:0000313|EMBL:KRZ77338.1};
OS   Trichinella papuae.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC   Trichinellida; Trichinellidae; Trichinella.
OX   NCBI_TaxID=268474 {ECO:0000313|EMBL:KRZ77338.1, ECO:0000313|Proteomes:UP000054843};
RN   [1] {ECO:0000313|EMBL:KRZ77338.1, ECO:0000313|Proteomes:UP000054843}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ISS1980 {ECO:0000313|EMBL:KRZ77338.1};
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:KRZ77338.1}.
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DR   EMBL; JYDO01000020; KRZ77338.1; -; Genomic_DNA.
DR   STRING; 268474.A0A0V1N073; -.
DR   Proteomes; UP000054843; 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:UP000054843};
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          182..224
FT                   /note="SURP motif"
FT                   /evidence="ECO:0000259|PROSITE:PS50128"
FT   DOMAIN          340..380
FT                   /note="SURP motif"
FT                   /evidence="ECO:0000259|PROSITE:PS50128"
FT   DOMAIN          897..925
FT                   /note="C3H1-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50103"
FT   ZN_FING         897..925
FT                   /note="C3H1-type"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00723"
FT   REGION          136..161
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          772..903
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          974..1010
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1165..1229
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1514..1541
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          1271..1308
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          1358..1395
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        777..813
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        836..858
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        859..880
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        889..903
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        978..1001
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1193..1229
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1517..1541
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1541 AA;  174401 MW;  6CAF504C9F95986E CRC64;
     MHRNSSLQEE SLDEFLAFGY PCKLFDSRED RDCADESADL IPLHCNRKIL VDRIMSLFGY
     QMVFITEFDC RLQLSNLEKY DASKVEQSLL IADRSFEALL DAERYRDFKL TYETPKVENE
     KRMGTEIYFN YDNLESKPQQ GCQPKEEAEG EEDEQKEQFV PPAELKVPVG VTLPKTVKEG
     IIIEKTAIFI AEQGSQMEII VNAKQKSNPQ FRFLDWNHPL NKYYKHVLKM IKEKRYTPVV
     VKKDPTPDSE SDSDDSEHYL HPSLMGGAAK IAVAKDTEPL SLPKTSYRLG EENDVYSELF
     NGLVAVCPQL AAAVSTAKEK ETAGSAEGLL LPPPPDLYPV VDRVAAYVAR NGPQFEQILR
     ERNDPRFSFI DPSNKYNPYY MALLQNYESE DYIAHLQQNV QNQSVEGVPM SLNYLSYYGF
     VPQPPPPPRS TPPPPAVENQ EQTLNLNKTK TIYCSDHLTS AATTISSVSE KPTEMGSVGP
     VCFTIKAKNP EETCLIVDKA NLDADLDETI NLPLQSDSDV LSDCAEKFDR KFVDGGGDAE
     ESAVKSVDEY MHREITAFPE VGKKEQKNVE ENLNLKQARR YRAKKFVDEF AKKIHKREKS
     CVDEEKVKKH GHVSEGELCD SESSESTLIG TSSNACYGID VGDPSQHPAV DIEKVQKIVD
     EEEKEEEDQE KERLDHDHVP PLRIYCIITK MFVDQPEQLK NWLINTLSPL CDADPAALAK
     YVMALLKKDK TEADLKHFCL DQLDVFLQKE TKKFVDELFL ALKSKVYIVT DKESQPSSTK
     EVPKKRSLEP SRNEKPSADE HLKSRRVDSH SASRPVRRYA SSPKARSKSS ERSKGKNDTT
     SVTQNKASSS TVRDRVKAHW SPSNNKEQRK STHKDSNEAA GNAENDSVQS IRSEKEKRKK
     ARCRDYDEKG YCMLGDNCVY DHGPDPVVVE DVALSSMIPM KDGTGRSNKS LPTPPPNFSV
     PPPGYVPIPP PPPGVDSNFQ TEGYNPEAPS LTSASTGTAV PLPPPYTQPP PPIWAQPPPV
     LRPFGPRQMA NYAQLRVNFP RARQLITLSE DRPNFDNFPQ SSIRTQHKSV GQINMRKRVA
     VDQINRHNRT LEVRRIPQPL NTITKLNEHF SQFGHITNIE VCYEGDPQAA LITYMTRPQA
     LAAYKSTDPI LNNRFIRVFW HNQKDGPAAE DTGTDQSSRP ARIPIKDRLE LPVKSSSNGT
     SSHDEVTFKS ETAANAGNNT ISTTMNKDQQ QMDDDAFLTK SIRLHNADAE LKNAAATAVA
     TKGENTKRIL KKRLELQRAE TELFNRQLEQ EKLLLKKLEN CKDQTKKELI LKTLKKLEIS
     LMTTKKNLES RDFSKFVKRS KTEVQRDVLD AELELITKKK AGEDISEIAV RLQNLRREMQ
     QLNDAESNNK QCRNSTYRPE RNRRIPRSAV LDLRSRSILI TDFCMEHKDA LIEHLQQFGT
     LRDIDFYPLT DPTVGKVIAS FYDRKEAERA FTDGKVFKDQ LLNMTWAVED KDAMAAALTA
     GSKTDLSAKA LLKTLDSPDD DDDDDLFEEN EREEIEEEQL A
//
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