ID A0A0V1CP27_TRIBR Unreviewed; 2602 AA.
AC A0A0V1CP27;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE SubName: Full=Helicase ssl-1 {ECO:0000313|EMBL:KRY50966.1};
GN Name=ssl-1 {ECO:0000313|EMBL:KRY50966.1};
GN ORFNames=T03_15465 {ECO:0000313|EMBL:KRY50966.1};
OS Trichinella britovi (Parasitic roundworm).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Trichinellida; Trichinellidae; Trichinella.
OX NCBI_TaxID=45882 {ECO:0000313|EMBL:KRY50966.1, ECO:0000313|Proteomes:UP000054653};
RN [1] {ECO:0000313|EMBL:KRY50966.1, ECO:0000313|Proteomes:UP000054653}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ISS120 {ECO:0000313|EMBL:KRY50966.1};
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 -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC -!- SIMILARITY: Belongs to the SNF2/RAD54 helicase family. SWR1 subfamily.
CC {ECO:0000256|ARBA:ARBA00009220}.
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:KRY50966.1}.
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DR EMBL; JYDI01000136; KRY50966.1; -; Genomic_DNA.
DR Proteomes; UP000054653; Unassembled WGS sequence.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0140658; F:ATP-dependent chromatin remodeler activity; IEA:InterPro.
DR GO; GO:0004386; F:helicase activity; IEA:UniProtKB-KW.
DR CDD; cd18003; DEXQc_SRCAP; 1.
DR CDD; cd18793; SF2_C_SNF; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR Gene3D; 1.20.120.850; SWI2/SNF2 ATPases, N-terminal domain; 1.
DR Gene3D; 3.40.50.10810; Tandem AAA-ATPase domain; 1.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR001650; Helicase_C.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR038718; SNF2-like_sf.
DR InterPro; IPR049730; SNF2/RAD54-like_C.
DR InterPro; IPR000330; SNF2_N.
DR PANTHER; PTHR45685:SF1; HELICASE SRCAP; 1.
DR PANTHER; PTHR45685; HELICASE SRCAP-RELATED; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR Pfam; PF00176; SNF2-rel_dom; 1.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00490; HELICc; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 3.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR PROSITE; PS51194; HELICASE_CTER; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Helicase {ECO:0000313|EMBL:KRY50966.1};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000054653}.
FT DOMAIN 270..435
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 1301..1451
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 139..199
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 952..1036
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1050..1140
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1504..1544
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1769..1795
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1958..2013
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2177..2283
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2417..2441
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 165..182
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 965..1004
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1064..1080
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1088..1104
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1105..1124
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1126..1140
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1522..1536
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1774..1791
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1958..1988
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1998..2012
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2189..2222
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2242..2258
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2259..2281
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2602 AA; 290760 MW; A53371B61C6F0B14 CRC64;
MIVLLFSIAE YKNERIVKSK RERAMGTHLN ILLDRSEKFK DGSNWNSNLG TRLNTTNTYK
CCYMGGISSS ASSDKESNDS DVDDDADSVE NTAEVVGVPE TSSWTETNNA ALKLSTETKE
NSISKPRVGK VKTLLEEQSE LDDNKAAGES NAAGNIYDTD RNVSTSSKKQ VEEEKAESST
SPFTADEEET VTELDDYTQS NETSSWINYQ KLQSENVEER REGLAHIAEE VERLQPKGYT
LETTTVNTRI PFLLKFSLRE YQHVGLDWLV MLDSRGLNGI LADEMGLGKT IQTIALLAHH
ACQNNIWGPH LIIVPTTVIL NWEMEFKKWC PAFKIFTYYG STKERKEKRK GWNRPNAFHV
CITSYKLVIR DYSTFRRKAW QYMILDEAQH IKNYKSERWQ MLLHFRARRR LLLTGTPLQN
SVMELWSLMH FLMPDIFCSD KDFREWFSNP LTGMVEGTME FNDQVIKRLH HVLRPFLLRR
LKSEVEKQLP KKYEHLIKCS LSKRQRYLYD EFMSRSNTKA QLATGSIFNI ISVLMQLRKV
CNHPNLFEQR PVMSPLVLDP IIYRPPSLVC DLPSKCNLEI LPLRLNVLRQ EFSSGFACNC
SGKLFSTKFE QPCKIESLPQ ISELPVGLFN FKSLFLNNRN TTAQLDNSRA VVKENSNVKD
SSDQKLAAVI PLKKRCSTSN GVVSRSASVD VSPKGAGSSV KSEEKPKVIY WRLNPIGGVN
ASGGRVGTTR VLRPIYTATT SRMPRPALAS RGPCAAGPSL VRLVRPSFGA VATRAPSVAA
TPATSQQCRS PAAVQSYHGG ALRPRVGTAS RPPMACRQSF LQQMARPNGG SPTKPLSARA
FLDYRLQTAG TVAASGRTTT GMIHVRLPAS NPISFSGQSS APSTASSLRV GAGAKVNIRC
SVPNQNILMP KGALIQLHAG KLCIPIRPVP PPASTASSSS GTAVVENVQL KKTPMAAALP
STTYERGRRK QQQQQPQQRQ QPHQHQQPTG QQRQMNSEES PAFLSPVENC NRRVTRRRKA
TSQVESSSFA DSPDDDFNVA AESKKIALRS GTTVGGGSKR RRSAAVVAST SSSSDSSKLR
RSTRSSFKAA VEKNSNIFAP STHSDDHHYN NEDEGEELPS RSGDVERMDG TSTQGTVSFD
PEAETSLEKA ILKLLNKQVN DLWSEITLSK AETKLRIQNN LINQNRERCL ARPMYGSDLR
MAFTIEKRSV PLSRTLEDMF QSVRFLLQQF LVYVPAALIS EPLFRPTYRS CAVEYAEVAM
RTSMNRLLKN KLDVFRAVEY AQRLCFPELR LIEYDCGKLQ SLSALLRRLQ AEGHRCLIFT
QMARMLDILE AFLSYHGYMY LRLDGATNIE RRQMLMERFN HDKKILCFIL STRSGGVGVN
LTGADTVIFY DSDWNPTMDA QAQDRCHRIG QTRDVHIYRL ICERTIEENI LLKATQKRKL
GELAIDEGGF KADFFHNTNI KELFDMEESV FVRDVSDADI QQAMSKVEDD NDAIAARIAV
DEAQAEERAD EEEDDENATS GQKKSDAVQD ANDNPVAESS DPDVLRVLEE MKDVLSKMSE
VERYALEYIE EERAFEFSEE LKGVDNEIEE RKMALMQAHY SEMRSARTMQ EAEAGEEFAI
TYDRRDAFAK VRDGDFNGES VKNSGKVSLL LTKEKGVTSV VAKSSTSSSV PATKCSLSNE
KFPIRTRRTR NNNSTMICIE DPSLEMPIWT PLSPPLSDDD SRGSLKPDHL LGELYERLPI
DQSILAKFPS SPSPDDDRSV EMPILRIPDK MPKLGGTTTT TNNNNRRASP FRGRSAVQVR
DKSVTETINS VARFPPPALS ISVNSPKSLF ELLSSKGRKE SSRSYNPSIM GMDMKNYEVF
PWNVIQDYAL IRSLLCGHCS LKSGNLPSRN QSLNWEYVSD FVRAHGSFYH SPRQCCLRYY
GWLHAQDEKT ASANMAANNP TPTPNATATA TGSVSLQTGG EASANVSGPS PSSGASSSST
GQGSKRDGSE CSTTKKQRKT GTHGSTAHSG KLVLKNISDR YKRDLNKTNT QRFRTISIMG
ASTFPESDSF TFTAGLLPTE LIDDEPAEQQ KDDVDINSED MKETFFESLF IPVMTSSNLE
EDGCQSDDDE DLESATVELQ ERMAATTQKM PTLRSTPSMD KLLFDNWLEE EKRNCQTKTD
FRKEVLPYFM TSLHMFDTDS DDETNNNNDV DDGNGNSNSN GNGNINRTSF FRTNSRDSSN
IINKGSESDE DIDDEKDDDD NNTNDGNVHP DVNDEHRRLQ QQQQQQQKQQ QQQQQQQQQK
HLHEHISLKE IIKQEDNRYY SGDFRPFSPV LLSTNNNNKG DNSAPPLPDV VTVKVESSPL
PTVKVEPVEF PPYRRYTVPP HFSANVTTTA TTTTFPTTNP SVTISSSPHT RLASFIHPIM
SSRQLTMPCS NLPTEVSALP RPTTIPSVRT TSSSSVPRQQ QQQMMHRAQT LKVLCPGRMR
IGNSRLRSLM GRAVPPSRII STSSGRPILR GQGITSSIGG RTIAIRTYRP RQPTPTTTTT
ISTPATVPST VVRPLPSSVA ANSSLAALIS DPPRIYTLSN RNPTTPVVRR RMPSVNVLAP
RGLIKREPTT FTAYRSSSNQ QH
//
