ID A0A3R7N5I9_9TRYP Unreviewed; 1113 AA.
AC A0A3R7N5I9;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE SubName: Full=Putative DNA-dependent ATPase {ECO:0000313|EMBL:RNF13152.1};
DE EC=3.6.1.- {ECO:0000313|EMBL:RNF13152.1};
GN ORFNames=Tco025E_06271 {ECO:0000313|EMBL:RNF13152.1};
OS Trypanosoma conorhini.
OC Eukaryota; Discoba; Euglenozoa; Kinetoplastea; Metakinetoplastina;
OC Trypanosomatida; Trypanosomatidae; Trypanosoma.
OX NCBI_TaxID=83891 {ECO:0000313|EMBL:RNF13152.1, ECO:0000313|Proteomes:UP000284403};
RN [1] {ECO:0000313|EMBL:RNF13152.1, ECO:0000313|Proteomes:UP000284403}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=025E {ECO:0000313|EMBL:RNF13152.1,
RC ECO:0000313|Proteomes:UP000284403};
RX PubMed=30355302; DOI=10.1186/s12864-018-5112-0;
RA Bradwell K.R., Koparde V.N., Matveyev A.V., Serrano M.G., Alves J.M.,
RA Parikh H., Huang B., Lee V., Espinosa-Alvarez O., Ortiz P.A.,
RA Costa-Martins A.G., Teixeira M.M., Buck G.A.;
RT "Genomic comparison of Trypanosoma conorhini and Trypanosoma rangeli to
RT Trypanosoma cruzi strains of high and low virulence.";
RL BMC Genomics 19:770-770(2018).
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:RNF13152.1}.
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DR EMBL; MKKU01000420; RNF13152.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3R7N5I9; -.
DR OrthoDB; 5482994at2759; -.
DR Proteomes; UP000284403; Unassembled WGS sequence.
DR GO; GO:0005634; C:nucleus; IEA:InterPro.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0140658; F:ATP-dependent chromatin remodeler activity; IEA:InterPro.
DR GO; GO:0051213; F:dioxygenase activity; IEA:UniProtKB-KW.
DR GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0031491; F:nucleosome binding; IEA:InterPro.
DR CDD; cd18793; SF2_C_SNF; 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; 1.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR001650; Helicase_C.
DR InterPro; IPR009057; Homeobox-like_sf.
DR InterPro; IPR036306; ISWI_HAND-dom_sf.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR035979; RBD_domain_sf.
DR InterPro; IPR015195; SLIDE.
DR InterPro; IPR038718; SNF2-like_sf.
DR InterPro; IPR049730; SNF2/RAD54-like_C.
DR InterPro; IPR000330; SNF2_N.
DR PANTHER; PTHR10799:SF879; CHROMATIN-REMODELING COMPLEX ATPASE CHAIN ISWI; 1.
DR PANTHER; PTHR10799; SNF2/RAD54 HELICASE FAMILY; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR Pfam; PF09111; SLIDE; 1.
DR Pfam; PF00176; SNF2-rel_dom; 1.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00490; HELICc; 1.
DR SUPFAM; SSF101224; HAND domain of the nucleosome remodeling ATPase ISWI; 1.
DR SUPFAM; SSF46689; Homeodomain-like; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR SUPFAM; SSF54928; RNA-binding domain, RBD; 1.
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 Coiled coil {ECO:0000256|SAM:Coils};
KW Dioxygenase {ECO:0000256|ARBA:ARBA00022964};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:RNF13152.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000284403}.
FT DOMAIN 179..347
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 477..636
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 873..910
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1092..1113
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 985..1012
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 874..900
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1113 AA; 127215 MW; E4FE473049F95966 CRC64;
MTTMHPSRTE RQRQDLHTAS DLDRRMNDLA AAELYEQILL GCVRAGMNPN EKSEEEEYEG
YVAPTFDPVQ GARVAAAKRS QLAKTYHERE SIIRNLRSSP QHQQLGSFDR LLTETEYWTG
VREWGGENGG GNSKRLRSRH GGNADEDSVG FDLLHLTETP SYIRGKLRPY QIEGVNWLLG
LFSCNINGIL ADEMGLGKTL QTIATLGYLK FTYGLPGPHL VVCPKSVMGN WYRELKHWCP
ALNAFKFHGS SEIRPQLIKS HLQPYEKLKY DIVVTTFEMV LEELPTFKRI HWQYLIVDEA
HKLKNEEGRA HTALDSLCTN HRLIITGTPL QNNLKELWAL LHFLAPRLFD NAEAFEAWFD
TSSGQQDSNA MSNMHKILAP LMIRRVKSEV STGIPPKREI YVACKLTKTQ RKWYMHVLAK
DAEALNKASG GSMSSLTNIL MNLRKVINHP YMMNGGEEGP PFITDERIVK YSGKMLILDK
LLFRLKREGE AKHKVLIFSQ FTTMLDILED YCAMRGFRVC RIDGNTSGYD RDAQMAAFNS
PNSDYFIFLL STRAGGLGIN LQAANHVVIY DSDWNPQMDL QAQDRAHRIG QKRVVRIYRF
ITEGTVEEKI YRRALKKLYL DAMVVQHGRM QRRGGNNVSK EELLSMIKFG AEEIFKTKDE
DITEADIDQL FDGEEKSKQI NSAMKEQVQM SLASFQLGAE EANVYDFEGV SFKAGVESRM
LHLSLPSQVS QDELHRQCSR HGEVIKVVLH PNLSEALVFF RSTSGAIEAK DNLPYECQFA
AKDAQMVVPT EVITEYLSVG EKLGRGHRLR EAIRHYTEED VERMQSRATK APPLRLPRCP
KFPPHQLYNA KRLQELHATE LALMVQNWKR KYEPSGDGAA EQQEHQEGLE AEATDRNTGK
EEVEEEDETL TIVEQEERER LLNEGFSNWS LQEYRRLVGA LTSGAYDVTD YPALASAIAS
GKTVGEVRDY LTALLERGAQ CIKGFLHVEQ RIRNAQEKRK RKEDELRAAT WKVESYDHPE
SQLTFRGRGA HEFDRRLFLM AYDTGFRVKN IGSVVKGMPE YRFDVWCQSR SDTYFERRVG
ILMKAVRREW DKPNGEALDP PPRRPKLDAA ANN
//
