ID K2NWN9_TRYCR Unreviewed; 1077 AA.
AC K2NWN9;
DT 28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT 28-NOV-2012, sequence version 1.
DT 27-MAR-2024, entry version 34.
DE SubName: Full=Helicase-like protein, putative {ECO:0000313|EMBL:EKF39461.1};
GN ORFNames=MOQ_000315 {ECO:0000313|EMBL:EKF39461.1};
OS Trypanosoma cruzi marinkellei.
OC Eukaryota; Discoba; Euglenozoa; Kinetoplastea; Metakinetoplastina;
OC Trypanosomatida; Trypanosomatidae; Trypanosoma; Schizotrypanum.
OX NCBI_TaxID=85056 {ECO:0000313|EMBL:EKF39461.1, ECO:0000313|Proteomes:UP000007350};
RN [1] {ECO:0000313|EMBL:EKF39461.1, ECO:0000313|Proteomes:UP000007350}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=B7 {ECO:0000313|EMBL:EKF39461.1,
RC ECO:0000313|Proteomes:UP000007350};
RX PubMed=23035642; DOI=10.1186/1471-2164-13-531;
RA Franzen O., Talavera-Lopez C., Ochaya S., Butler C.E., Messenger L.A.,
RA Lewis M.D., Llewellyn M.S., Marinkelle C.J., Tyler K.M., Miles M.A.,
RA Andersson B.;
RT "Comparative genomic analysis of human infective Trypanosoma cruzi lineages
RT with the bat-restricted subspecies T. cruzi marinkellei.";
RL BMC Genomics 13:531-531(2012).
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
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:EKF39461.1}.
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DR EMBL; AHKC01001222; EKF39461.1; -; Genomic_DNA.
DR AlphaFoldDB; K2NWN9; -.
DR EnsemblProtists; EKF39461; EKF39461; MOQ_000315.
DR OrthoDB; 153190at2759; -.
DR Proteomes; UP000007350; Unassembled WGS sequence.
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:0051213; F:dioxygenase activity; IEA:UniProtKB-KW.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0004386; F:helicase activity; IEA:UniProtKB-KW.
DR CDD; cd18007; DEXHc_ATRX-like; 1.
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:SF1; HELICASE ARIP4; 1.
DR PANTHER; PTHR45797; 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 Dioxygenase {ECO:0000256|ARBA:ARBA00022964};
KW Helicase {ECO:0000313|EMBL:EKF39461.1};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000007350}.
FT DOMAIN 262..446
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 654..817
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 79..119
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 572..634
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 977..1002
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 80..112
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 574..593
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 604..619
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 984..1002
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1077 AA; 121187 MW; AABD351B250D6B31 CRC64;
MATVRRTDEP VLFVMSTSES EDGDGTDGEN VADVLALAED ARSTLSSRHC DVANMFIDEV
LFGDMDHRSA FLPDTGAGAI DADSSSSSSS SSSSSSGSDR SLSVQELVGE ETNQLSHGPG
VVEEKEALEP HEPLMSMAVL RGMTCADVRA VLEPFFQRKE AAKARFDTLQ NWLAEEMAAK
KTRVKESMLE RWRRLVNISN WGDGSSSRDD VLFPEALVPP AATLLGVLGP SVTTTVLPEL
QQLRPHQIDG IRFVWSILAE GPVGRVPAVG CILAHTMGLG KTCQVVIFLH LFLNERRGSL
GRSQRVLIVV PKSTRLGWQK EFSTWSQYFP LAQRILPIMI DERDGMKRRL DLYRSWWNEG
GVLLVGYEML LGLTKLSKEG TREDKKGCEF TDLLICDEAH RLKSTRLQIS AALRGLHPLR
RLLLTGTPLQ NHLQEYWAMV DFAVHKYFEK RRFQEFFINP IEASVAQEAS SREVATARMK
TFALIRELRH FVQRVDSTPL RDELPPLHEY VLVVPLSTLQ VRLYNRFLHL ARLEQSRFNF
LQAVTYANKI SAHPQLLFDR DPASPLREIM SDVESSPDDD EDDDDDDDDG NNNNNNNNED
AGDNVGKGNR RRGDRRRTAF SGPVSEGYSD LFQPPADYMA APEDGVKLYI SIRIIKAAML
RGERALFFSL STKLLTLFEG IIAEMNRRWQ QDGSLSRPIR FCRLDGNSSG AERESTLRSF
NSSRGADVLL LSIKAGGVGI NITSATRVIL ADSGFNPADD RQAIGRAYRY GQTRPVFVYR
LLCYQTLEHR MFQQKVAKEW LFHTIVEEAS LKRDALTGLR LQSMFQLLGR SLEVSNEVPA
LTDEQRDSTA RLFTEDAVLA ELADSIIYAE SHEVYLQHDE LVQYGKEERE FYEEYQKKGV
FNIDSYMDGV NIGNETEQRK RQREKHQENI GRQTKTLTAL VDDVIRGRAE QDPQLRHLLR
MMGITVDASG VVSVSSIQEA QRRTREPIAV DGEDGSDASD DRRIRHLSGE KVARTETTPP
LRPIVLNHSD DDDDDDSILF EGKKNNNVGL VIDPSIYEPY KPGRNASNAI LIDEDEV
//
