ID A0A1I7UEH8_9PELO Unreviewed; 1406 AA.
AC A0A1I7UEH8;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE SubName: Full=Helicase ATP-binding domain-containing protein {ECO:0000313|WBParaSite:Csp11.Scaffold629.g8508.t1};
OS Caenorhabditis tropicalis.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=1561998 {ECO:0000313|Proteomes:UP000095282, ECO:0000313|WBParaSite:Csp11.Scaffold629.g8508.t1};
RN [1] {ECO:0000313|WBParaSite:Csp11.Scaffold629.g8508.t1}
RP IDENTIFICATION.
RG WormBaseParasite;
RL Submitted (NOV-2016) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
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DR STRING; 1561998.A0A1I7UEH8; -.
DR WBParaSite; Csp11.Scaffold629.g8508.t1; Csp11.Scaffold629.g8508.t1; Csp11.Scaffold629.g8508.
DR eggNOG; KOG1015; Eukaryota.
DR Proteomes; UP000095282; Unplaced.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0140658; F:ATP-dependent chromatin remodeler activity; IEA:InterPro.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0004386; F:helicase activity; IEA:UniProtKB-KW.
DR CDD; cd18793; SF2_C_SNF; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR Gene3D; 3.40.50.10810; Tandem AAA-ATPase domain; 1.
DR InterPro; IPR044574; ARIP4-like.
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; PTHR45797; RAD54-LIKE; 1.
DR PANTHER; PTHR45797:SF3; RAD54-LIKE; 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; 2.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR PROSITE; PS51194; HELICASE_CTER; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741}.
FT DOMAIN 555..756
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 996..1179
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 27..478
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 887..969
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 27..53
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 80..133
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 140..158
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 198..214
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 221..239
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 271..328
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 342..415
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 449..478
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 888..906
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 941..965
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1406 AA; 162892 MW; 51298FF32F48D2D7 CRC64;
MKVVEDSEDD ADLQVIDDED LQLAAEIEKE RKEKRAQKLR EKREKEGKPV KKETRKRGKP
PTKKRRVDSS EEEDEDEDEE SPKKPVKKAR RRAKDSEDDD SEDEMPKKSS KKTKKRAESS
DEDDEEEERS RKKPTRKAGK RAKSSDEDED SEEDKRKKKK NEKKRKSRKQ KSESEESEES
DDDDDRRKSK NKKKKTSKKR AETSESEESD YPKRKKSQKK RRDSSSSESE SESEEDRKMK
KKKNKKKISK KRSVSSEPET TSKKKKSTSK KRGKESSDEE SEEEQRKTKK NGNKRGKSKS
SEEESDGEKK ETQKNKKQEK KDKKEVVDSK EEEEEEEIKE DKQSTSEEKE SVKSDSEDDI
VISPKRKTKK QEASDEQSEE SEEEVMPKKK SRGVVLVSDE EDSDYEQKKK NASGSEESDS
TGSEASEASD SDEKSTKKKS KKEEKSKKKK KGMIMDDSKL AKSTVDAEKA ERERRKRLEK
KQKEFNGIVL NEKAGLEQAL EGKQISWLKS VVLDPDANSD PPVPVEVHKS LVRILKPHQA
HGVQFMYDCA FESVDRLDSE GSGGILAHCM GLGKTLQVIT FLHTTMMHEK VGEKCRRVLV
VVPKNVIINW FKECQKWLED NDPELGTIEY DEMDRYKSIP ERLYALKQWH KTKTPSVMII
GYDMFRILTC EDDPKKKKTA AARKLAKAKE EFRKYLQDPG PDMVVCDEAH KLKNDESALS
KCMVKIATKR RICLTGTPLQ NNLMEYHCMV NFVKPGLLGT KTEFANRFSN IITRGRTKDA
SPLEVSFMKR RCHVLYEHLK KCVDRKDYSV LTEAIPPKQE YVVNVRMTEK QCSLYNLFLE
DVVGSQGLSK RLLPDYHMFS RIWTHPYQLI LHEQRLERER VLRDEEEEEA AFIDDEESEE
EDSYNSSSSE ESVVQSGSDS DDGKKRKRTR RTRRKRKGRR KQEEINGIRQ SRRLAGEDAL
ERDTDTPPEY TGWFAKSGLL SDDDRNDFTL SNKLVLLMEI IKKCEEIGDK LLVFSQSLES
LALIKRMLEH MAGTGQWFGG EHAALNAEGE EAWSWLEGTD YMTIDGSVQS VKRDSVQTEF
NDPQNLRARL MLISTRAGSL GTNMVAANRV VIFDACWNPS HDTQSLFRVY RFGQTKPVYI
YRFIAQGTME ERIYKRQVTK ESTSMRVVDE AQIQRHYLGN DLTELYQFTP SKYDPEIAIS
CAPPKDLLLA EVIHENPSAI VDYIEHDTLF ANQEQEKLTE QEMKDAWADY EKDKSGQQPP
PLPRVQYDVN AIRSGGVFVG PQLETALQNR FQETLRIDQL QNDPLYRELT RMRNKDLPTF
LKVVLLRNLL EQILPYIPDE MRGGMSEFNS HFIRLVHESD RKMEAPEELL RKALESFKTV
TRMVSGIPTC REPMERMRRT HPYLFE
//
