ID A0A2H5N6X7_CITUN Unreviewed; 1067 AA.
AC A0A2H5N6X7;
DT 28-FEB-2018, integrated into UniProtKB/TrEMBL.
DT 28-FEB-2018, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE RecName: Full=Chromatin-remodeling complex ATPase {ECO:0008006|Google:ProtNLM};
GN ORFNames=CUMW_019680 {ECO:0000313|EMBL:GAY35988.1};
OS Citrus unshiu (Satsuma mandarin) (Citrus nobilis var. unshiu).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Sapindales; Rutaceae; Aurantioideae; Citrus.
OX NCBI_TaxID=55188 {ECO:0000313|EMBL:GAY35988.1};
RN [1] {ECO:0000313|EMBL:GAY35988.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=29259619; DOI=10.3389/fgene.2017.00180;
RA Shimizu T., Tanizawa Y., Mochizuki T., Nagasaki H., Yoshioka T., Toyoda A.,
RA Fujiyama A., Kaminuma E., Nakamura Y.;
RT "Draft sequencing of the heterozygous diploid genome of Satsuma (Citrus
RT unshiu Marc.) using a hybrid assembly approach.";
RL Front. Genet. 8:180-180(2017).
CC -!- SIMILARITY: Belongs to the SNF2/RAD54 helicase family. ISWI subfamily.
CC {ECO:0000256|ARBA:ARBA00009687}.
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:GAY35988.1}.
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DR EMBL; BDQV01000003; GAY35988.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2H5N6X7; -.
DR STRING; 55188.A0A2H5N6X7; -.
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:InterPro.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0031491; F:nucleosome binding; IEA:InterPro.
DR CDD; cd17997; DEXHc_SMARCA1_SMARCA5; 1.
DR CDD; cd00167; SANT; 1.
DR CDD; cd18793; SF2_C_SNF; 1.
DR Gene3D; 1.10.10.60; Homeodomain-like; 2.
DR Gene3D; 1.20.5.1190; iswi atpase; 1.
DR Gene3D; 1.10.1040.30; ISWI, HAND domain; 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; IPR044754; Isw1/2_DEXHc.
DR InterPro; IPR015194; ISWI_HAND-dom.
DR InterPro; IPR036306; ISWI_HAND-dom_sf.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR001005; SANT/Myb.
DR InterPro; IPR017884; SANT_dom.
DR InterPro; IPR015195; SLIDE.
DR InterPro; IPR038718; SNF2-like_sf.
DR InterPro; IPR049730; SNF2/RAD54-like_C.
DR InterPro; IPR000330; SNF2_N.
DR PANTHER; PTHR45623; CHROMODOMAIN-HELICASE-DNA-BINDING PROTEIN 3-RELATED-RELATED; 1.
DR PANTHER; PTHR45623:SF49; SWI_SNF RELATED, MATRIX ASSOCIATED, ACTIN DEPENDENT REGULATOR OF CHROMATIN, SUBFAMILY A, MEMBER 1; 1.
DR Pfam; PF09110; HAND; 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 SMART; SM00717; SANT; 2.
DR SUPFAM; SSF101224; HAND domain of the nucleosome remodeling ATPase ISWI; 1.
DR SUPFAM; SSF46689; Homeodomain-like; 2.
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; PS51293; SANT; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741}.
FT DOMAIN 203..368
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 496..647
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT DOMAIN 841..893
FT /note="SANT"
FT /evidence="ECO:0000259|PROSITE:PS51293"
FT REGION 1..90
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 137..175
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1013..1067
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 11..26
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 27..42
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 52..75
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 76..90
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1013..1030
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1035..1049
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1050..1067
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1067 AA; 123782 MW; 73B61EEBC31CEC1C CRC64;
MAKPSKARES SDDALSNGSS SSEEEQINDQ INEDDEEELE AVARSADADS DDDNSPASED
EAAADGDDVE EDDDSGANAD ISKREKQRLK EMQKLKKQKI QELLDKQNAA IDADMNNRGK
GRLKYLLQQT ELFSHFAKGD QSASQKKAKG RGRHASKLTE EEEDEEYLKE EEDGLSNTRL
VTQPSCIQGK MRDYQLAGLN WLIRLYENGI NGILADEMGL GKTLQTISLL GYLHEFRGIT
GPHMVVAPKS TLGNWMNEIR RFCPVLRAVK FLGNPEERRH IRENLLVAGK FDVCVTSFEM
AIKEKSALRR FSWRYIIIDE AHRIKNENSL LSKTMRLYNT NYRLLITGTP LQNNLHELWS
LLNFLLPEIF SSAETFDEWF QISGENDQQE VVQQLHKVLR PFLLRRLKSD VEKGLPPKKE
TILKVGMSQM QKQYYRALLQ KDLEVVNAGG ERKRLLNIAM QLRKCCNHPY LFQGAEPGPP
YTTGDHLITN AGKMVLLDKL LPKLKERDSR VLIFSQMTRL LDILEDYLMF RGYLYCRIDG
NTGGEDRDAS IEAFNKPGSE KFVFLLSTRA GGLGINLATA DVVILYDSDW NPQVDLQAQD
RAHRIGQKKE VQVFRFCTEY TIEEKVIERA YKKLALDALV IQQGRLAEQK TVNKDELLQM
VRFGAEMVFS SKDSTITDED IDRIIAKGEE ATAELDAKMK KFTEDAIKFK MDDTAELYDF
DDEKDENKFD FKKIVSDNWI EPPKRERKRN YSESEYFKQT MRQGGPAKPK EPRIPRMPQL
HDFQFFNTQR LSELYEKEVR YLMQTHQKNQ LKDTIDVDEP EDVGDPLTAE ELEEKERLLE
EGFSSWSRRD FNTFIRACEK YGRNDIKSIA SEMDGKSEEE VERYAKVFKE RYKELNDYDR
IIKNIERGEA RISRKDEIMK AIGKKLDRYK NPWLELKIQY GQNKGKLYNE ECDRFMICMV
HKLGYGNWDE LKAAFRTSPL FRFDWFVKSR TTQELARRCD TLIRLVEKEN QEYDERERQA
RKEKKLAKNM TPSKRGGGRQ PNESPSSLKK RKQLSMDDYV SSGKRRK
//
