ID A0A0V0RWM9_9BILA Unreviewed; 1688 AA.
AC A0A0V0RWM9;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 22-FEB-2023, entry version 29.
DE SubName: Full=Dystonin {ECO:0000313|EMBL:KRX18889.1};
GN Name=DST {ECO:0000313|EMBL:KRX18889.1};
GN ORFNames=T07_3179 {ECO:0000313|EMBL:KRX18889.1};
OS Trichinella nelsoni.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Trichinellida; Trichinellidae; Trichinella.
OX NCBI_TaxID=6336 {ECO:0000313|EMBL:KRX18889.1, ECO:0000313|Proteomes:UP000054630};
RN [1] {ECO:0000313|EMBL:KRX18889.1, ECO:0000313|Proteomes:UP000054630}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ISS37 {ECO:0000313|EMBL:KRX18889.1};
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 -!- 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:KRX18889.1}.
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DR EMBL; JYDL01000066; KRX18889.1; -; Genomic_DNA.
DR Proteomes; UP000054630; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-KW.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0008017; F:microtubule binding; IEA:InterPro.
DR GO; GO:0045104; P:intermediate filament cytoskeleton organization; IEA:InterPro.
DR CDD; cd00051; EFh; 1.
DR CDD; cd00176; SPEC; 4.
DR Gene3D; 1.20.58.60; -; 8.
DR Gene3D; 1.10.238.10; EF-hand; 1.
DR Gene3D; 3.30.920.20; Gas2-like domain; 1.
DR InterPro; IPR011992; EF-hand-dom_pair.
DR InterPro; IPR018247; EF_Hand_1_Ca_BS.
DR InterPro; IPR002048; EF_hand_dom.
DR InterPro; IPR003108; GAR_dom.
DR InterPro; IPR036534; GAR_dom_sf.
DR InterPro; IPR043197; Plakin.
DR InterPro; IPR018159; Spectrin/alpha-actinin.
DR InterPro; IPR002017; Spectrin_repeat.
DR PANTHER; PTHR23169; ENVOPLAKIN; 1.
DR PANTHER; PTHR23169:SF23; SHORT STOP, ISOFORM H; 1.
DR Pfam; PF13499; EF-hand_7; 1.
DR Pfam; PF02187; GAS2; 1.
DR Pfam; PF00435; Spectrin; 2.
DR SMART; SM00054; EFh; 2.
DR SMART; SM00243; GAS2; 1.
DR SMART; SM00150; SPEC; 8.
DR SUPFAM; SSF47473; EF-hand; 1.
DR SUPFAM; SSF143575; GAS2 domain-like; 1.
DR SUPFAM; SSF46966; Spectrin repeat; 8.
DR PROSITE; PS00018; EF_HAND_1; 1.
DR PROSITE; PS50222; EF_HAND_2; 2.
DR PROSITE; PS51460; GAR; 1.
PE 4: Predicted;
KW Calcium {ECO:0000256|ARBA:ARBA00022837};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Cytoskeleton {ECO:0000256|ARBA:ARBA00023212};
KW Reference proteome {ECO:0000313|Proteomes:UP000054630}.
FT DOMAIN 1372..1400
FT /note="EF-hand"
FT /evidence="ECO:0000259|PROSITE:PS50222"
FT DOMAIN 1401..1436
FT /note="EF-hand"
FT /evidence="ECO:0000259|PROSITE:PS50222"
FT DOMAIN 1438..1509
FT /note="GAR"
FT /evidence="ECO:0000259|PROSITE:PS51460"
FT REGION 1054..1074
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1545..1575
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1588..1688
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 448..475
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 1588..1638
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1639..1656
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1657..1672
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1673..1688
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1688 AA; 191818 MW; 63CC965A72B7BA26 CRC64;
MTFALAKVMA ALDGLIDWLE PVEKKIKQGA VFSADLNIAR DTLESHRMLQ ADIFSRRTRA
NDILLLGNKV SKLLNPDDRQ FLVEKMEKLR ALSDAVTDCS CSLLEHLEEL VATITCFDEA
YKELDAWLTS EESEVECMHL LQDDGMHDIV EVNKRIWKNI SDGYIMVEKL EKYRLEVKKL
ACEEDAARIA KLTSQLMSRY ENLKNTFKMR ADVIERTQVH SGKVIYQLDG IMESLNDCKE
RFNSICSRIS DRPELLSRQI EENMALVKDL ERKQSLCHSL INGIDCDDEV KMLSDKADLI
ELLSTELLNI ITSHTYKLHE TLRVAGSFWN LYAACMEKWK PIESQLSSSE SATCEALCLV
DMRDQLIRMK AQFSDKQASA EGCEKLGNQL LKLVGDEFKS NVVETVRQLK TTNQRITDLL
NKRDQEIEYK LTKADSMTQL SDHILIMLKN VEDQINNFQD ISDQLEQLNE QFQEVLCLKD
QLDAVTVLVE QLKQLCETFC SGSPVTDVSY ARHAYETISS HLKLLYSIAS SRHQDLEKAL
LQVGCAQVAL DQMINWIEKT TGTVHELRCS PGDTKSVDLQ LAVLRAIGND VAAHRATVAE
VTDAVTRNRQ FLPDQSSEQS SIVEKVEIMQ SKWDALMASI DVKLSELEYS KQETFRFLDM
FVEWQVWMSD VESAISNGRH VGGLPDTAKE QLEKFQLIVA DVASKKSTID SAIVDALDYT
RDNSALQSPL FAEVQAFETR WKLLQKRVEE HSQKLERALK QAIEFDSLVT ECSCWQQRAE
HYLNHLEPAS RLKAKLKTQM EQHLIFCEEI DTRRQQMLTL DSCGTRMKYT CRRPDATLIK
NQLATMLTSW SKILTRAADR SKQLDTVSRS CTSFFDQLEQ LNCKFDELQD QFQQLLVQQH
LSPGGSGGGG GGGFNVEHLV QALDQLSMFQ CQLSALSADL DRIAAQGRQL REHAIAEEQR
VIGDAVNAAR DKWNGLNGAL LERQARLEQA LLFNGQLEEA VDVLMVWLRQ AEELLGDDER
VGGDVDTLLE LDERLQTLRS GLQSRESSIA SIRGMRHECS STNEQRQRQQ QQQQLSDSIA
KKVDVMLELW DTVSRLVDQR QATLCKSRAD AERLKTDCGA LFEWLAQAET RARPTEQNCE
RRIAALEHLI EEIDSKRGSV DEVLELGRRI RAVCHPKAEK PLERCLTALE ARYAQTLQMV
KQRLLRLKSD LDQEKQLDVD LKLLLDWVQK MQAKIDSLQD NLPSYTPGTA DVLDEQHRKI
VELIERQLMF EVSLQERQRE VDEATADFRT VEAEQLGLVT PGAAASRPKN ARTAQLVAAW
RKLWLSCINY KNLLNERLHY IIEMKQLIGF SFDNWRRRYV RWMAERKCRA VDLFKRYDCD
GDGRLTCDQF RDAILNSRFK TSKAEMDLVV EAIDRNQDGF VDMTEFLHAL RADSEHITDD
KRITEEIAKQ LNLCSCKQKY RVEEVRPGRC YRLGERLKLV RIYRSTVMVR VGGGWQTFQE
FMSKNDPCRA KGRTNLELRE QFILPEGGSQ AVWLFRRKNI KPEKAAKLSS GTSYGPVTKI
REKTERSMPM CSTGGAVAGN ASSLSVAGNV SETSPAEPSS ITGELASTCD AGDHSSSQAN
LPTNTDASGG VTSSHRSSEQ EIDTAETSKR RKEQRTSSSA ASSLSSLHRK NNTTTGRGRR
GGRSRKNF
//
