ID A0A0V0V7Q9_9BILA Unreviewed; 1579 AA.
AC A0A0V0V7Q9;
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:KRX59492.1};
GN Name=swp-1 {ECO:0000313|EMBL:KRX59492.1};
GN ORFNames=T09_15121 {ECO:0000313|EMBL:KRX59492.1};
OS Trichinella sp. T9.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Trichinellida; Trichinellidae; Trichinella.
OX NCBI_TaxID=181606 {ECO:0000313|EMBL:KRX59492.1, ECO:0000313|Proteomes:UP000054681};
RN [1] {ECO:0000313|EMBL:KRX59492.1, ECO:0000313|Proteomes:UP000054681}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ISS409 {ECO:0000313|EMBL:KRX59492.1};
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:KRX59492.1}.
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DR EMBL; JYDN01000071; KRX59492.1; -; Genomic_DNA.
DR Proteomes; UP000054681; 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:UP000054681};
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 168..210
FT /note="SURP motif"
FT /evidence="ECO:0000259|PROSITE:PS50128"
FT DOMAIN 327..367
FT /note="SURP motif"
FT /evidence="ECO:0000259|PROSITE:PS50128"
FT DOMAIN 933..961
FT /note="C3H1-type"
FT /evidence="ECO:0000259|PROSITE:PS50103"
FT ZN_FING 933..961
FT /note="C3H1-type"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00723"
FT REGION 121..147
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 227..264
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 581..626
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 639..700
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 809..939
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1010..1043
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1536..1579
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 1308..1345
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 1395..1422
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 124..146
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 227..245
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 589..606
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 612..626
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 643..681
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 813..849
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 872..894
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 895..916
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 925..939
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1014..1037
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1554..1579
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1579 AA; 178852 MW; E7021241B6978375 CRC64;
MHRNSLLQEE SSDEFLAFGY PCKLFDSRGG RDCADESADL IPLHCNRKIL VDRFDCRLQL
SNLEKYDASK VEQSLLIADR SLEALLDAER YRDFKLTCET PKVENEKRMG TEIYFNYDDL
ESKPQHGCQP KEEAEGTEDE QKEQFVPPAE LKVPVGVTLP KTVKEGIIIE KTAAFIAEQG
SQMEIIVNAK QKSNPQFRFL DWNHPLNKYY KHVLKMIKEK RYTPVVVKKD PAPESESDSD
DSSEHYLHPS LMGGAGKTAV AKDTEPLSLP KTSYRLGEEN DVYSELFNGL VAVCPQLAAA
VSTAKGKETG GSAEGLLLPP PPDLYPVVDR VAAYVARNGP QFEQILRERN DPRFSFIDPS
NKYNPYYMAL LQNYESVPMS LNYLSYYGFV PQPPPPPRST PPPPAVENQE ETLNLKKTKT
VYCSDHLTSA AASSSVSEKP TEMGSVGPVC FTIKAKNQEE TCSMMDKANL DAHQDETINL
SLQSDSDVLM SDCAEKFDCK FVDGSGDAAE STVKSVDEYM QREITTFPEV GKKEQKNVEE
DLNLKRARRY RAKKFVDEFA KKIRKREKSC VDEEKVKKHG HISEGELCDS ESSESTLIGT
SSNASYGSEK KKKRKKKEEE 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
//
