ID H3APH3_LATCH Unreviewed; 2488 AA.
AC H3APH3;
DT 18-APR-2012, integrated into UniProtKB/TrEMBL.
DT 18-APR-2012, sequence version 1.
DT 27-MAR-2024, entry version 63.
DE RecName: Full=DNA helicase {ECO:0000256|ARBA:ARBA00012551};
DE EC=3.6.4.12 {ECO:0000256|ARBA:ARBA00012551};
DE AltName: Full=ATP-dependent helicase ATRX {ECO:0000256|ARBA:ARBA00031106};
GN Name=ATRX {ECO:0000313|Ensembl:ENSLACP00000011544.1};
OS Latimeria chalumnae (Coelacanth).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Coelacanthiformes; Coelacanthidae; Latimeria.
OX NCBI_TaxID=7897 {ECO:0000313|Ensembl:ENSLACP00000011544.1, ECO:0000313|Proteomes:UP000008672};
RN [1] {ECO:0000313|Proteomes:UP000008672}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Wild caught {ECO:0000313|Proteomes:UP000008672};
RA Di Palma F., Alfoldi J., Johnson J., Berlin A., Gnerre S., Jaffe D.,
RA MacCallum I., Young S., Walker B.J., Lander E., Lindblad-Toh K.;
RT "The draft genome of Latimeria chalumnae.";
RL Submitted (AUG-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSLACP00000011544.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.12;
CC Evidence={ECO:0000256|ARBA:ARBA00001665};
CC -!- SUBCELLULAR LOCATION: Chromosome, telomere
CC {ECO:0000256|ARBA:ARBA00004574}. Nucleus
CC {ECO:0000256|ARBA:ARBA00004123}.
CC -!- SIMILARITY: Belongs to the SNF2/RAD54 helicase family.
CC {ECO:0000256|ARBA:ARBA00007025}.
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DR EMBL; AFYH01109332; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AFYH01109333; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AFYH01109334; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AFYH01109335; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AFYH01109336; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AFYH01109337; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AFYH01109338; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AFYH01109339; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AFYH01109340; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AFYH01109341; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR STRING; 7897.ENSLACP00000011544; -.
DR Ensembl; ENSLACT00000011633.1; ENSLACP00000011544.1; ENSLACG00000010157.2.
DR eggNOG; KOG1015; Eukaryota.
DR GeneTree; ENSGT00940000155902; -.
DR InParanoid; H3APH3; -.
DR OMA; QEMGGVM; -.
DR TreeFam; TF313172; -.
DR Proteomes; UP000008672; Unassembled WGS sequence.
DR Bgee; ENSLACG00000010157; Expressed in muscle tissue and 6 other cell types or tissues.
DR GO; GO:0000781; C:chromosome, telomeric region; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
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:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006807; P:nitrogen compound metabolic process; IEA:UniProt.
DR GO; GO:0071704; P:organic substance metabolic process; IEA:UniProt.
DR GO; GO:0044238; P:primary metabolic process; IEA:UniProt.
DR CDD; cd11726; ADDz_ATRX; 1.
DR CDD; cd18068; DEXHc_ATRX; 1.
DR CDD; cd18793; SF2_C_SNF; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR Gene3D; 1.20.120.850; SWI2/SNF2 ATPases, N-terminal domain; 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); 1.
DR InterPro; IPR025766; ADD.
DR InterPro; IPR041430; ADD_ATRX.
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; IPR011011; Znf_FYVE_PHD.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR46357; TRANSCRIPTIONAL REGULATOR ATRX; 1.
DR PANTHER; PTHR46357:SF1; TRANSCRIPTIONAL REGULATOR ATRX; 1.
DR Pfam; PF17981; ADD_ATRX; 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; SSF57903; FYVE/PHD zinc finger; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR PROSITE; PS51533; ADD; 1.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR PROSITE; PS51194; HELICASE_CTER; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Chromosome {ECO:0000256|ARBA:ARBA00022895};
KW DNA damage {ECO:0000256|ARBA:ARBA00022763};
KW DNA repair {ECO:0000256|ARBA:ARBA00023204};
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000008672};
KW Telomere {ECO:0000256|ARBA:ARBA00022895};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771}.
FT DOMAIN 150..287
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS51533"
FT DOMAIN 1570..1757
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 2017..2196
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 16..107
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 437..510
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 541..574
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 594..910
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1067..1108
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1121..1208
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1226..1251
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1279..1501
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1902..1991
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2464..2488
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 22..56
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 63..77
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 78..99
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 437..468
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 541..567
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 597..643
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 661..717
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 751..800
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 807..831
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 845..866
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 883..907
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1076..1093
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1121..1135
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1136..1155
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1166..1197
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1290..1320
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1346..1385
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1399..1424
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1474..1501
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2488 AA; 281894 MW; BDFC7AB43748A047 CRC64;
SESKLNTLVQ KLHEFLAHSS EESEDPNSPL MEFSPENSAT SKKEISKLQQ MDNSKEEGCS
SSEKSKISGS TRSKRKPSIV TKYIESDEEK TKDEEMSNGN ASEGEVDVNC LPKGTVVVQP
EPVSNEDKDS FKGPEFRGRS SKTKIETYKK RGEEALHGIV SCTACGQQVN HFQKDSIFRH
PALHVLICKN CYKYYMSDDI NKDADGMDEQ CRWCAEGGNL ICCDFCHNVF CKKCILRNLG
RKELSSVMEE NRKWYCYICF PEPLLDLVTA CDSVFENLEQ LWQQSKKKAK SESDKGRMDE
HGIKNAQKEK SCSHCNGQDH CLNNVSSGTV TYSYKTLKVP KDLIKKTRKL VETTASLNAS
FVKFLKEKNE SLDTDKIVTQ RRLKAFKSVL GDLKKLHLAL EETLDKEILE LDKATKHVKT
KDNAAKDVDQ EVISEERENL STAAEKNDYE ELDSAGEVPE DSVVRELEDS VMDQSIPPTE
QQDTETKGSV TEEEECKDEP ANDPEALDKD IVSVPASVPE DIFENADSSM DAMSCLVEVE
NSSAVASQEP THEVESTCSP SNKPSKDNSS DTELKHVKVL KELYVKLTPV SFVEPSHKNI
KKQKGSEAGK EKNVISKKHK VDDCSLYEKQ NMSEGEELGG EKSELLCDSP NLRRSPRIKT
TPLRRPNDKN TLRSMPEEES SNDETPKRSS PQSKKQVKKG SMDEAYSKSK KSVSRSSETL
KTDGSSSDSD DVPEILKEAS KMNPSSSDAD SNDDTKSKNV RRKSLFGIKK ENEVTESGKR
KRKSSGSDSD WDEKTTKTSK SPAVAKKKRR NQSDSSNYDS DLEKELKNLS KIALVKKSSK
RAKKEKRHDN SSSKDEDDEK PKATERKKAS PKKRSIKKTS ISSSSSDEEE EAAKTSAADD
SSDEQKIKPV AENPVLPAAS GFCQSSVFFI KDTFIMKPSI SFFSPFKSSF LPFMPEKCKE
QSFDQISYQY LKGGEQEIEN SDSKLEEERG GKKYKINEEN QMQLRARMSK LGDDTKSTTT
EKIATKGMSL RQTNQTFLND HSRTKKKKKM KIKFILTKAQ KFKVEYSPGS KEFPGLESEG
GDEENAKSGL ASEVVDDDDD DDPENRYDSI CTDFKKIITH PRRGLKAKQR NSKWVKKSRT
GCSVKTRSQA ACKIEQVASK QRPETRNAKR RNKKKYTFEK KTKHISDKKK KKQTNKQKKK
QEVVISERLD SNSPQYSCLG GGVRSEIKFK PTRSGPSAIG GGGEKCSRPV PVCVKMTREQ
EDIERRIAKK MLLEEIKANL SSGGAGSSEE DSEDGEKKKS DKRNESKESS KCKTYDEEAS
ESDSDSLSDS DFEMKKPRYR HRLLRHKLSM SDGESGEEKK EGKTKDGSKE GKRRNRRKVS
SEDSDDSEFQ ESGVSEEVSD SDDDQRPRTR STKKLDAEEN QRSYKQKKKR RRIKVQDDSS
SENKSNSEEN DDEEENGDSK SPGKGRKKIR KILKNDKLRA ETQNALKEEE ERRKRIAERE
REREKMREVI VVEDASPVTC PITTKLVLDE DDETKEPLVQ VHRNLVTKLK PHQVDGVQFM
WDCCCESVKK TKKSQGSGCI LAHCMGLGKT LQVVSFLHTL LLCEKVDFRT ALVVCPLNTV
LNWLNEFDKW QEGLGDDEKL EVTELATVKR PQERSCLIQR WQEDGGIMII GYEMYRNLTQ
GRNVKSKKLK EVFQRTLVDP GPDFVICDEG HILKNEASAI SKSMNAIRTR RRIVLTGTPL
QNNLIEYHCM VNFIKENLLG SVKEFRNRFI NPIQNGQCAD STPVDVRIMK KRAHILYEML
AGCVQRRDYT SLTKFLPPKH EYVLAVRITP IQCKLYRYYL DHFTGIGTTV DGGRGRAGTK
LFQDFQMLSR IWTHPWCLQL DYISKENKGY FDEDSMEEFI ASDSEDTSIS LSSEEERKKK
KKSKGGKGSK RDSSSRSGSD NDVEVIKSWN SRSRGGGGGD GVVEERPSVV ENVKPEEGKS
GSGSNPASPQ PDWYKDFVSE ADAEIIEHSG KLSLLFEILR MAEELGEKVL VFSQSLISLD
LIEDFLELAN KAKDEEDKPL IYKGKGKWFR NIDYYRLDGS TSAQTRKKWA EEFNDDSNPR
GRLFIISTRA GSLGINLVAA NRVIIFDASW NPSYDVQSIF RVYRFGQVKP VFVYRFLAQG
TMEEKIYDRQ VAKQSLSFRV VDQQQIERHF TMNELTELYT FEPDLLDDPN SEKKSKRATP
MLPKDTILAE LLQNHKEYMV GYHEHDSLLD HKEEEELTEE ERKAAWTEYE AEKKGLNTRF
NVPNPNIAHL SAQLGINMGA NLGAQNPYFP FNFQGLSKMS TQQLEDVVKQ GREKVVEATS
SITAARLEPL EDIIGTAWKE NPNLSEAQVQ ALALSKQASQ ELELKRREAV YSDVLTKQQV
LVQYVQKILM SRRLQEVSQQ QQQQLAFQHQ AALNRYMFSK PPNLLTTPNF PQIDYTGMYR
PLTGGMPPPL QRGTNLMRGH SPGPSQGK
//
