ID A0A0L7K6Y6_PLAFX Unreviewed; 2728 AA.
AC A0A0L7K6Y6;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 27-MAR-2024, entry version 39.
DE RecName: Full=SNF2 helicase {ECO:0008006|Google:ProtNLM};
GN ORFNames=PFHG_00598 {ECO:0000313|EMBL:KOB58850.1};
OS Plasmodium falciparum (isolate HB3).
OC Eukaryota; Sar; Alveolata; Apicomplexa; Aconoidasida; Haemosporida;
OC Plasmodiidae; Plasmodium; Plasmodium (Laverania).
OX NCBI_TaxID=137071 {ECO:0000313|EMBL:KOB58850.1, ECO:0000313|Proteomes:UP000054289};
RN [1] {ECO:0000313|EMBL:KOB58850.1, ECO:0000313|Proteomes:UP000054289}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HB3 {ECO:0000313|EMBL:KOB58850.1};
RG The Broad Institute Genome Sequencing Platform;
RA Volkman S.K., Neafsey D.E., Dash A.P., Chitnis C.E., Hartl D.L.,
RA Young S.K., Zeng Q., Koehrsen M., Alvarado L., Berlin A., Borenstein D.,
RA Chapman S.B., Chen Z., Engels R., Freedman E., Gellesch M., Goldberg J.,
RA Griggs A., Gujja S., Heilman E.R., Heiman D.I., Howarth C., Jen D.,
RA Larson L., Mehta T., Neiman D., Park D., Pearson M., Roberts A., Saif S.,
RA Shea T., Shenoy N., Sisk P., Stolte C., Sykes S., Walk T., White J.,
RA Yandava C., Haas B., Henn M.R., Nusbaum C., Birren B.;
RT "Annotation of Plasmodium falciparum HB3.";
RL Submitted (MAR-2006) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000054289}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG The Broad Institute Genome Sequencing Platform;
RA Birren B., Lander E., Galagan J., Nusbaum C., Devon K., Henn M., Jaffe D.,
RA Butler J., Alvarez P., Gnerre S., Grabherr M., Kleber M., Mauceli E.,
RA Brockman W., MacCallum I.A., Rounsley S., Young S., LaButti K.,
RA Pushparaj V., DeCaprio D., Crawford M., Koehrsen M., Engels R.,
RA Montgomery P., Pearson M., Howarth C., Larson L., Luoma S., White J.,
RA Kodira C., Zeng Q., Oleary S., Yandava C., Alvarado L., Wirth D.,
RA Volkman S., Hartl D.;
RT "The genome sequence of the Plasmodium falciparum HB3.";
RL Submitted (MAR-2006) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; CH671926; KOB58850.1; -; Genomic_DNA.
DR EnsemblProtists; KOB58850; KOB58850; PFHG_00598.
DR VEuPathDB; PlasmoDB:PfHB3_060028800; -.
DR Proteomes; UP000054289; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0140658; F:ATP-dependent chromatin remodeler activity; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR CDD; cd17919; DEXHc_Snf; 1.
DR CDD; cd15489; PHD_SF; 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 Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 4.
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 InterPro; IPR019786; Zinc_finger_PHD-type_CS.
DR InterPro; IPR011011; Znf_FYVE_PHD.
DR InterPro; IPR001965; Znf_PHD.
DR InterPro; IPR019787; Znf_PHD-finger.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
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; PF00628; PHD; 1.
DR Pfam; PF00176; SNF2-rel_dom; 1.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00490; HELICc; 1.
DR SMART; SM00249; PHD; 5.
DR SMART; SM00184; RING; 4.
DR SUPFAM; SSF57903; FYVE/PHD zinc finger; 4.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR PROSITE; PS51194; HELICASE_CTER; 1.
DR PROSITE; PS01359; ZF_PHD_1; 2.
DR PROSITE; PS50016; ZF_PHD_2; 2.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000054289};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00175}.
FT DOMAIN 52..118
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS50016"
FT DOMAIN 72..116
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT DOMAIN 144..191
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS50016"
FT DOMAIN 349..516
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 1070..1236
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 263..283
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 533..576
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 850..961
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1312..1345
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1357..1403
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1578..1612
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1787..1940
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2056..2080
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2148..2187
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2237..2298
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2602..2682
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 1970..2007
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 269..283
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 533..550
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 850..867
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 881..898
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 910..930
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 931..961
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1361..1403
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1787..1869
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1870..1886
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1912..1940
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2056..2072
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2159..2175
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2618..2644
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2651..2682
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2728 AA; 316728 MW; 0DE648266B986D3A CRC64;
MRIRKTWCTL CRENFEEGDE CIQCKQCKKK FHRECLQAEG LMDNEQLKDI KNYVCYQCIN
EDDDIPENED RCKICREKSA NLILLLCDGC PNSYHVSCLG LAAEPESEKW YCPICKPDDH
KNLDVRRMRK GFVLDNMNGE HVNSSTCYVC QRPGKLLGCD FCPNSFHPTC LPDLDFDNIS
DQWECPCCKN EDPLLNQGHK RWTKNEIQEI MKKRQRELGF WRSKIIKYRN RFLLAHRKDL
QPFVNPRVFS NLTKTFKNDY FHTKGSSNNK KSNKYDNDKY NSKKDVDMDS KEFNEFISSL
EDEAHQNACK FIESVFLSVY YPNGRKIERR PLVDNVQLKP HQEDGVEWLL KSFLTGGAIL
ADEMGLGKTI QTLCFLSYLK CNKIDGPHLI VVPLSTVGNW LREIHRFTPH LTCIKICGSK
NERTHAKEDR LAEKGLYDLY VTTYETVKNE EEFFVETIPK WQCIVLDEAH RIKNQSGAIR
HSMDRVVGNM RLLLTGTPLQ NNSAELFTLI NFMFPDIFKN SEIIEQAFMN ASQNNKNKSN
NNNNNNNNKD EKNNNNDDDD DGGGGGGGAN TSGNNTSKVN VNIGNIDLKS AIKEEDLKSI
RCLLDKIMLR RLKEQAITLP KKIFHDVWLP LGTLSAHWYK RLLDIRSMVE EKVSVKKLLG
LVIKMRIICG HPKGIVSRPS QMEKLFAFFE EESEDIKEQV KNDALKLKNI SGEEHIESSS
KLIFIDKLLC QLHYENCKYV KNYASSYEKH KKEVAAYNYH KIQEQTNAQK KKREHSGKFK
KIEALENSPL FMEIYNKGKF DLKPTSQKED MLKSFMHSVP VDNECPYKKK RCIYDKVKEY
VKNNSNIKHK GRARLISDNN KNNKNDDNSD DEDDDEEEDE VNYYNKRKDK KKKVISDDDD
DDDENSNDDN KSEDNNNDDN NNDDNKDITK NDNNGNFSDN NNNNNNNNIN DDQNDDNIFS
LHDSSKINNN IKEFLKSEKM EMSNNTDKIN EDSTVGVTDK GDNKLDDFDM LKREEKEKND
AYMKEEGEEY DEEDVITHKN GTQLNIDNNN NNNNNNNNIN NVTDLKLQTD EKKVVINIKN
EMNDNDENGE KLGEAKMHKV LIFTQFQLVL DELEEYCKYR CWKYMRLDGS TNKLIRELDI
REFNLSDSIY FIYLISTRAG GLGINLTAAN HVIMYDEDWN PFIDLQAIDR AHRIGQKREV
NVWKLMTEWT VEERMAFRRE QKLKLDKLVV QTQDDEDMLD NFEEKLSSDE IRKLMLHGKA
AIQNMDVEST NNFPLEFFIE RGRQKLPIIN GVDLEREEKC AIEEEINKKD DGDDILVSKN
DEDDDDDDNS VDAKYNNNND DDNAIDIDEV MMDEAEELES RNNNTNNNNN NNDGTGGSGE
MINGQFSSSN NQNNNNNNNN NNDISLWRSV RERKKPQILY TPEYWGRKQE VKQIKHEYRC
FICNNTKNHK AIVKDRNGND IEIDYGDMIN CFRCPKTYHK LCEGIKDENV KKTWTCSWHE
CCLCFRKSSQ CGNLLIHCAT CPTSFCYNCF PPDYVRYYVG EEYYHNLRQR GVNFTPQNWV
CFLCSKCKAV EEQKKRRKMT KEERENEKQL QKELRSQLHD SKQEELEAKK RKRAQQLERD
KFIIENRKRI DALDQQYEDQ LRKAYENVFP NNFVKELVNR IEHAKMLKQK GIVEDNNNNN
NNNKETNKKK STTFLHTKLP SKLLVLCENC KLPCHANYKY PGKCCYPPEL DKSYYMSNTS
FSQMGRDGFE KRVSEGKNDS CSSHIHFKDK VGEDSNNMKN ITNIVDGNKI MNSSPHKGGT
KCEPNEGSTT PSRNDGIKKD LMVTSTINNN NSNNNNNNSN NNNNNNNSYN FNENKENSSS
TNKLMSNKGI EYNKNDDEDY NNNESKDKIM KGVGTTFLSD GSMRFEKDSP ENNMNENNNM
NNNNNNEKDS PQNNNDNTSK SKTRKFLRAV CSKCGTVQLG KLAHFRKHCD KLTEEEKKEY
DEKREKLKEL INLLNKKKIK EEHTEEEYKN MSVFKFKSLY SNYQDKADDI LEDCIRSMKW
DILIADKKKI IKKEKEKENK KIYSKNDDDN NNNNNKKNNN ITSMSLKAKL THFLSNQPLT
ISSDYSDTKD IIEIRSDLTD DMKEKINDEL CTISGKRKKC IVKNIKKVKK KKGNDDNDEN
NNNSNNNVDG DKKNNNKSNT SSKKKDDKDL KKLNLLINPF HEKLIKDTHN ANFIRDSFNE
DFLNKAKEFL RVTKSNLINN GNNNNNNKNK KSSSNSKNIN KNSSNTKNSS NTKSSSNTKS
SSSNTKNKNN KNNHNNSFLE SATTAEDFLR GITTGNNNIF NLVSSSNSPY DKNKKLKDDE
FEKSIIQNYL NKMKNSLKNS SHLDKNTIKE KLKELNYVNS RSNSNTKNNM NTNIINNNNN
NNNQHTISAQ ENSLRFAKEI FKNGAFDKNG NFKLYANKGN LCNTNKDIVH LLKSNEQIEN
MNKNSGYSIN DFNLDIFNID KNIKCEDLEK KLLNLCASTN LMNKKNIQHD NNKKEDNKNY
MLDSKNKNKQ FLFKKDNTQQ QEAFLSNISK AKKESSNSRK RVVEDVNVDY DIKKITNTSE
NSGPNKVQEY ILYRRNTSSV MSNVINNNDK SKNVRNDDED DDDDEDDYRD DDEDDDEEDD
EDKNESSNYN NNKKKKTNTS SRNSSNNNSS NKNKNNKSGN DIHQASNLLY QNLLNNPQSL
LQHLNLEDVK NFLKAADRSN NDNLPEIN
//
