ID F7AAN9_CALJA Unreviewed; 1405 AA.
AC F7AAN9;
DT 27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT 25-MAY-2022, sequence version 4.
DT 27-MAR-2024, entry version 54.
DE SubName: Full=RAD54 like 2 {ECO:0000313|Ensembl:ENSCJAP00000010313.4};
GN Name=RAD54L2 {ECO:0000313|Ensembl:ENSCJAP00000010313.4};
OS Callithrix jacchus (White-tufted-ear marmoset).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Platyrrhini; Cebidae;
OC Callitrichinae; Callithrix; Callithrix.
OX NCBI_TaxID=9483 {ECO:0000313|Ensembl:ENSCJAP00000010313.4, ECO:0000313|Proteomes:UP000008225};
RN [1] {ECO:0000313|Ensembl:ENSCJAP00000010313.4}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Warren W., Ye L., Minx P., Worley K., Gibbs R., Wilson R.K.;
RL Submitted (MAR-2009) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSCJAP00000010313.4}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
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DR Ensembl; ENSCJAT00000010902.4; ENSCJAP00000010313.4; ENSCJAG00000005575.4.
DR GeneTree; ENSGT00940000155763; -.
DR Proteomes; UP000008225; Chromosome 15.
DR Bgee; ENSCJAG00000005575; Expressed in testis and 6 other cell types or tissues.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0004386; F:helicase activity; IEA:UniProtKB-KW.
DR CDD; cd18069; DEXHc_ARIP4; 1.
DR CDD; cd18793; SF2_C_SNF; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR Gene3D; 3.20.80.10; Regulatory factor, effector binding domain; 1.
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 InterPro; IPR044574; ARIP4-like.
DR InterPro; IPR044573; ARIP4_DEXHc.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR001650; Helicase_C.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR011256; Reg_factor_effector_dom_sf.
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 SUPFAM; SSF55136; Probable bacterial effector-binding domain; 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 Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000008225};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 1187..1207
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1213..1233
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 181..401
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 617..785
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 75..127
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 539..561
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1009..1060
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1074..1109
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1139..1168
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 80..108
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 542..561
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1027..1043
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1076..1101
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1405 AA; 156457 MW; CC3A093444E23F05 CRC64;
MFRKLLREDQ LEPVTKAAQQ EELERRKRLE QQRKDYAAPI PTVPLEFLPE EIALRASDGH
QLPPRVLAQE VICLDSSSGS EDEKSSRDEV IELSSGEEDT LHIVDSSESV SEEDEEEEKG
GTHVNDVLNQ PDTLGRVLVN LNHPPEEENV FLAPQLARAV KPHQIGGIRF LYDNLVESLE
RFKTSSGFGC ILAHSMGLGK TLQVISFIDV LFRHTPAKTV LAIVPVNTLQ NWLAEFNMWL
PPPEALPADN KPEEVQPRFF KVHILNDEHK TMASRAKVMA DWVSEGGVLL MGYEMYRLLT
LKKSFATGRP KKTKKRSHPV IIDLDEEDRQ QEFRREFEKA LCRPGPDVVI CDEGHRIKNC
QASTSQALKN IRSRRRVVLT GYPLQNNLIE YWCMVDFVRP DFLGTRQEFS NMFERPILNG
QCIDSTPQDV RLMRYRSHVL HSLLEGFVQR RGHTVLKIHL PAKEENVILV RLSKIQRDLY
TQFMDRFRDC GTSGWLGLNP LKAFCVCCKI WNHPDVLYEA LQKESLANEQ DLDVEELGSA
GTSARCPTQG TKGKGEDSTL ASSMGEATNS KFLQGVGFNP FQERGNNIVT YEWAKDLLTN
YQTGVLENSP KMVLLFHLIE ESVKLGDKIL VFSQSLSTLA LIEEFLGKRE VPSPPGAEGQ
GAQKWVRNVS YFRLDGSTPA FERERLINQF NDPSNLTTWL FLLSTRAGCL GVNLIGANRV
VVFDASWNPC HDAQAVCRVY RYGQKKPCYI YRLVADYTLE KKIYDRQISK QGMSDRVVDD
LNPMLNFTRK EVENLLHFVE KEPAPQVSLN IKGIKESVLQ LACLKYPHLI TKEPFEHESL
LLNRKDHKLT KAEKKAAKKS YEEDKRTSVP YTRPSYAQYY PASDQSLTSI PAFSQRNWQP
TLKGDEKPVA SVRPVQSTPI PMMPRHVPLG GSVSSASSTN PSMNFPINYL QRAGVLVQKV
VTTTDIVIPG LNSTTDVQAR INAGESIHII RGTKGTYIRT SDGRIFAVRA TGKPKVPEDG
RMAASGSQGP SRESTSNGRH SASSPKAPDP EGLARPVSPD SPEIISELQQ YADVAAARES
RQSSPSINAT LPGQPAQLVD SSAVPGTALG TEPRLGGHCL NSSLLVTGQP CGDRHPVLDL
RGHKRKLATP PAAQESSRRR SRKGHLPAPV QPCLGVQCGG SRAMSDLLLL GLIGGLTLLL
LLTLLAFAGY SGLLAGVAVS AGSPPILNIT LAYKFHMGPY GETGRLFTES CSISPKLRSI
AVYYDNPHMV PPDKCRCAVG SILSEGEESP SPELIDLYQK FGFKVFSFPA PSHVVTATFP
YTTILSIWLA TRRVHPALDT YIKERKLCAH PRLEIYQQDQ IHFMCPLARQ GDFYVPEVKE
TEQKWRGLAE AIDAQVDGTG TEGGV
//
