ID A0A261BMB1_9PELO Unreviewed; 2717 AA.
AC A0A261BMB1;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE RecName: Full=DNA helicase {ECO:0008006|Google:ProtNLM};
DE Flags: Fragment;
GN ORFNames=FL83_14744 {ECO:0000313|EMBL:OZG10855.1};
OS Caenorhabditis latens.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=1503980 {ECO:0000313|EMBL:OZG10855.1, ECO:0000313|Proteomes:UP000216463};
RN [1] {ECO:0000313|EMBL:OZG10855.1, ECO:0000313|Proteomes:UP000216463}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PX534 {ECO:0000313|EMBL:OZG10855.1,
RC ECO:0000313|Proteomes:UP000216463};
RA Fierst J.L.;
RT "Caenorhabditis latens genome sequence.";
RL Submitted (JUL-2017) 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:OZG10855.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; NIPN01000116; OZG10855.1; -; Genomic_DNA.
DR STRING; 1503980.A0A261BMB1; -.
DR Proteomes; UP000216463; Unassembled WGS sequence.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0140658; F:ATP-dependent chromatin remodeler activity; IEA:InterPro.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR CDD; cd18659; CD2_tandem; 1.
DR CDD; cd00167; SANT; 1.
DR CDD; cd18793; SF2_C_SNF; 1.
DR Gene3D; 2.40.50.40; -; 2.
DR Gene3D; 3.40.5.120; -; 1.
DR Gene3D; 1.10.10.60; Homeodomain-like; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR Gene3D; 3.40.50.10810; Tandem AAA-ATPase domain; 2.
DR InterPro; IPR006576; BRK_domain.
DR InterPro; IPR037259; BRK_sf.
DR InterPro; IPR016197; Chromo-like_dom_sf.
DR InterPro; IPR000953; Chromo/chromo_shadow_dom.
DR InterPro; IPR023780; Chromo_domain.
DR InterPro; IPR001650; Helicase_C.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR001005; SANT/Myb.
DR InterPro; IPR038718; SNF2-like_sf.
DR InterPro; IPR049730; SNF2/RAD54-like_C.
DR InterPro; IPR000330; SNF2_N.
DR PANTHER; PTHR45623; CHROMODOMAIN-HELICASE-DNA-BINDING PROTEIN 3-RELATED-RELATED; 1.
DR PANTHER; PTHR45623:SF11; KISMET, ISOFORM C; 1.
DR Pfam; PF07533; BRK; 1.
DR Pfam; PF00385; Chromo; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR Pfam; PF00176; SNF2-rel_dom; 1.
DR SMART; SM00592; BRK; 1.
DR SMART; SM00298; CHROMO; 2.
DR SMART; SM00717; SANT; 1.
DR SUPFAM; SSF160481; BRK domain-like; 1.
DR SUPFAM; SSF54160; Chromo domain-like; 2.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR PROSITE; PS50013; CHROMO_2; 1.
DR PROSITE; PS51194; HELICASE_CTER; 1.
DR PROSITE; PS50090; MYB_LIKE; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Helicase {ECO:0000256|ARBA:ARBA00022806};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000216463};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT DOMAIN 1077..1144
FT /note="Chromo"
FT /evidence="ECO:0000259|PROSITE:PS50013"
FT DOMAIN 1336..1523
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT DOMAIN 1802..1865
FT /note="Myb-like"
FT /evidence="ECO:0000259|PROSITE:PS50090"
FT REGION 1..106
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 152..295
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 366..412
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 428..942
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 973..1014
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1530..1574
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2024..2060
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2184..2217
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2363..2391
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2458..2486
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2685..2717
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 301..351
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 2228..2262
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 35..72
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 73..92
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 190..208
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 209..240
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 279..295
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 381..412
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 435..449
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 459..475
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 476..505
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 506..575
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 585..620
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 630..648
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 673..722
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 723..746
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 757..780
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 794..811
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 812..837
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 838..875
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 884..904
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 973..1005
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1530..1571
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2024..2041
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2463..2486
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2685..2707
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:OZG10855.1"
SQ SEQUENCE 2717 AA; 300351 MW; 2C98FC59EA05011C CRC64;
MDEGDDYVPQ MSQMTDYTMM GGPPQQPPQA QPPVGVPQQQ RYPGQPMNPY EQQHHQQMMM
MQQQQHMHQM APPVPSQQPP PQSAQPQPPP AKKPRGKSKK AQAEAAAAAA AAAAQMDPMA
SMASMANNPM MRQNAYPVSL FFEICISNQM GMYGGAPPPH YQQGSNGPSQ QGYRPGPASG
GPPQGQYPQA PPQNYQQMYH QRGPPQQAQP QQGQPPGYPG YGYPPQASTG YPPPPSQQSP
YAPQAAHMRH QYPPQSQQQA PPGYWDGYQG YGGAPQVQGA PPVTSQPMQM GQQQDQWARQ
VNELMGVLAQ LEKTCSEYKA RMQQLFNLPR NAAADAEVQT LQVKLNQMQA DHYRYGQQLQ
HAQWQQQQAA AAAAASAGGH HQPPPTSSQS MTPNQNQQVP VHVNQSGSQV QLNITADKSR
TLISVYHEGY GGAGSGASST ESKESIVPPE PTPSMQPQEQ IPSIPSMSGY PTQQHPHQQP
PQPPQPHQQP ASVPMQHPPQ QPHPHQQQHP SGYGIGSTST APSSMKPEAM EQQRPQSQTH
QNQYPGYSDY PASSGYQDSV PSETTMNQQQ PSPAVSDPIM APPTQPMEQI QNQSLSHQNP
IPNHEQIQQQ QQQQIQDQLI QEEQKIDEPF EYPSQSQEPE NADSVVNPSE EFNDEMKDEI
FKETASSSSS YPQEELKEEK EEESYREEAD EVVEKKEEDV NEDEKDMTPE KHYNNGNTLN
EEEEEKDPLD DITLDPLDEI DDLKSEEPDE ERSQRGQISE SQSQSTLSPG ESNSQMEPEE
STPVLLEDIE NFAGVEETFG DDDEAQDDED LPEEGSSAKS SKDDIKEEDD DDMSTITKDM
SEAPSETNDG FTEPSTPATP MMSTPGTSTT KKKSYRRPVV VSKSKKKKSV DDSDDDDFYP
QRGRGKKKGG GGXRKKADVE ENGEGGEAEV DEDEEFLMKI DTPAPDPNAL IVEKILNVRM
EKIQVPVITE EDLEGKSDVK EGEDDAEMKE GPAEKSEDQK EAATSKENGT TEVPAEEVEV
EQFLIKWKGR AYCHCEWKTF PELLEIDKRV EAKIKRFKAK KLVSYIEDDE DFNSDFVIVD
RVVDMITEDD GQEFVLIKWK SLGYEEVTWE PIENIPEDKV ELWRQRQVID PAKVRDKNRP
EPNEWKNMST LKVWKNGNSL REYQFEGVDW LLYCYYNAQN CILADEMGLG KTVQTITFLS
QIYDYGIHGP FLVVVPLSTI QNWEILKPMM LRRLKEDVEK SLGPKEETII EVQLSDMQKK
FYRAILERNF SHLCKGTSAP SLMNVMMELR KCCNHPFLIN GAEETIMNDF RLAHPDWDDE
TLAQKALVQA SGKVVLIEKL LPKLRKDGHK VLIFSQMVKV LDLLEEFLIT MSYPFERIDG
NVRGDLRQAA IDRFSKESLD KAVLQSTTAL KAEGTALSKK DVEELLKKGA YGSIMDEENE
SAKFNEEDIE TILQRRTQTI TLEAGQKGSL FAKATFNSTH NKGDDIDIDD PEFWTKWAEK
AQVDVEKATA TPDGRELILE EPRKRTKRFE ENKIDEVDSD GSEESGKRKR GNGEKRKRRK
GDDEDGDYSG SYRPDELATS KAEYFKVEKV LAQYGWGRWE DIRKYGELEI DIQDIEHMCR
TLLLHCVREF RGDDRVRQFV FNLIKPQEFS DKKIGAGSMY SQGWAALPEF NPPSFALDSA
FQRHVHRHAN KLMQKIDMLK HLETHIIGDE RALVEDMSVK WSDIKLKEMP IVSETFVDGW
DSDCDKCFLI GCWRHGLENY EAIRADENLC FNDKNLPMWP GQAEFWVRFR RLLLTSQRSV
HDPVYDKLKW TKREEQEFIR VLRSFGVKNQ KTESAMEDWN SFRAFSPILE KKSDDECHEQ
FMCVLAMCRR AQGNNDLKPI DLKRAMSIDP MPHRKAIKML NRINVIRKVH LLAESLEVAD
LSICETTGMP SGWSSQHDKE LIEICDQCGL DQLAANVLNK PAFTKIVRPS ETTLLRRVIE
IVTTVEAGKW CGVGDVESVN DSDTEEKKDM ATVAAAQAQF LRLQQQQQAS VTPSSSASRK
GNRKRPNNDN DAKMRAMQQM LMGQGGANDY ASMLALMLMP QMMASTGTQN MTAAQQQTIS
QMLTMLIAGA VQQQQQAQQQ QQPSTSKASS QQAQAQAQAQ AAAIALAQAA AQSTSSASSS
AEQQQQQQIL EAILAMSMNP AALASLTGQS STGTSTPSTQ KKTKPSATPK ESTSSATAAA
SAQAAALAAA AAAAQQQQQQ QAQQAQQAQQ AAQQAAQAAQ AQQVVKSQEE LLILRILEIA
GVGMTELAKL NTMSKDAKIP MIHKSTKEPL PDSKRPQIRD LTVFAMSNPE WTIDLSLFNE
MTGTGTGSGA AVSGALAAAK AASSRPTPVA TPKPATPKVE LKSEPQTPGA SATCNIKVGN
SLQFEDMIAV FNRKTGEPLA ATRWPKTNEL SSWLDANPDY NVHSQSALLA HLTLGGKHSD
RIGGESTIQT PSVPSTPAPS LTPSTSAAAA NAQLMALAAA QQVQQQQTAA ATSSAKSRSA
TAAAQAAAQA AASQQDAMAK SQLEMMQMQL ILQQYQQAAA IQQIMYGGYG MQSNASSSST
ANAASMAAMI AAAQAAQTQA SVPSTPTTSK QKFQSVASTP STSTAATTSV AATSSTPSTS
SAAAQAATSS SSGSAEDINP LLLSALLQNP AVLQQMMVSD PNTLLLLTAA AQQQQQQQQQ
SQKKDGQQPA AKKSKHP
//
