ID A0A3Q7X333_CICAR Unreviewed; 1428 AA.
AC A0A3Q7X333;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE SubName: Full=CHD3-type chromatin-remodeling factor PICKLE-like isoform X3 {ECO:0000313|RefSeq:XP_027188139.1};
GN Name=LOC101506720 {ECO:0000313|RefSeq:XP_027188139.1};
OS Cicer arietinum (Chickpea) (Garbanzo).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC NPAAA clade; Hologalegina; IRL clade; Cicereae; Cicer.
OX NCBI_TaxID=3827 {ECO:0000313|Proteomes:UP000087171, ECO:0000313|RefSeq:XP_027188139.1};
RN [1] {ECO:0000313|RefSeq:XP_027188139.1}
RP IDENTIFICATION.
RC TISSUE=Etiolated seedlings {ECO:0000313|RefSeq:XP_027188139.1};
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
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DR RefSeq; XP_027188139.1; XM_027332338.1.
DR Proteomes; UP000087171; Chromosome Ca3.
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:0004386; F:helicase activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR Gene3D; 2.40.50.40; -; 2.
DR Gene3D; 6.10.250.1310; -; 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); 1.
DR InterPro; IPR016197; Chromo-like_dom_sf.
DR InterPro; IPR000953; Chromo/chromo_shadow_dom.
DR InterPro; IPR023780; Chromo_domain.
DR InterPro; IPR001650; Helicase_C.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR038718; SNF2-like_sf.
DR InterPro; IPR000330; SNF2_N.
DR InterPro; IPR019786; Zinc_finger_PHD-type_CS.
DR InterPro; IPR001965; Znf_PHD.
DR InterPro; IPR019787; Znf_PHD-finger.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR45623; CHROMODOMAIN-HELICASE-DNA-BINDING PROTEIN 3-RELATED-RELATED; 1.
DR PANTHER; PTHR45623:SF51; DNA HELICASE CHROMATIN REGULATOR PHD FAMILY-RELATED; 1.
DR Pfam; PF00385; Chromo; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR Pfam; PF00176; SNF2-rel_dom; 1.
DR SMART; SM00298; CHROMO; 2.
DR SMART; SM00249; PHD; 1.
DR SUPFAM; SSF54160; Chromo domain-like; 2.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR PROSITE; PS50013; CHROMO_2; 1.
DR PROSITE; PS01359; ZF_PHD_1; 1.
DR PROSITE; PS50016; ZF_PHD_2; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022806};
KW Helicase {ECO:0000256|ARBA:ARBA00022806};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022806};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022806};
KW Reference proteome {ECO:0000313|Proteomes:UP000087171};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00146}.
FT DOMAIN 41..90
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS50016"
FT DOMAIN 101..166
FT /note="Chromo"
FT /evidence="ECO:0000259|PROSITE:PS50013"
FT REGION 1..34
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 887..939
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1201..1234
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1247..1267
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1201..1220
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1428 AA; 162299 MW; 5B3D60B4311561EC CRC64;
MKARTLVTDD GGNSDSRHDK GLTEDNTQVD LRGENGKGDE EDVCFKCSHG GTLWRCCGRG
CQRGYHPSCL DPPLKFLPLG FWHCISCVEK KIKLGVHSVS KGVECILDSQ DVVSKGEVMR
REYFVKYQGL AHAHNRWITE KQMLTVAPKL LEKYKKKQQA VRWKKDWSMP HRLLMKRDII
LSKQNAHPFD GHDENDSICR YEWLVKWTGL GYDHVTWELD DTSFMTSSKG MKLVDNYESL
RMRSDGLSNP LEANEERKVF FTELSVIPYG DSPGLYNQHL SYVNRLRMCW HKGQSAVIVD
DQIDQERVRK VILFILSLSC NVKRPFLIIS TSTGISAWET EFLHLAPSAN VVVYKGNKDV
RCSIRALEFY NEDGGILFQI LLSSSEIIIE DLHALRYIQW EAIIIDECQR SKILGHIDNI
NILAAEMRLL LISGQIKEDR ADYIKLLSFL QSGHDELNIS MKETYLSASI SNLKSQLEQY
IAFKGNSGSS RFIEYWVPAQ LSSLQLEQYC SMLLSNSMLL CSGQKYDSVD ALRDLIISTR
KCCNHPFLLN QSLNSLLIRG LPVEEHLDIG IRASGKLQLL EKILFEAKTR ELRVIIIFQS
SGGSGSIGDI LDDVLCHKFG KDCYVRYGRG YIPSKKQAAL DTFNDRESGK FVFLIESRAC
LPSVKLSSVD TVILFDSDWD PQNDLKCVQK MSISSKFNEL TVLRLYSYFT VEERVLMLAK
EGVALDSNMQ LVNQSSTYHT LLKWGASYLF SKLDDFHGSD TSVSASDISD QSILNDVICE
LSSKLVCDRD GSDCHGQSFL SRVQQNGAEY AKSISLLGER EMKKLSNETH TFSWSDHLKG
RNPQWKFLPV SSQRIRKTVE YFHHIPEGSE YENDSIICKR RTESKDNVYP TRKKVSKDNV
DPEERKVTKD NVDPKRRKVS EDIVGTKRKE LSKGVADPKT RKLSKNIIDD AERRKASKEV
IDSKGRKVSV DTVGSKYLKK KWKNKKNGRA SKRERKLNGA AVMNKHIPKQ KKLPDMPKNT
KFLSKPDISG LCDVLHFSEN VKAVAMMILE YVFKHYDVNN CREVSTVQAF QISVCWLAAS
LLKHKIDKKH SVDLAKRHLN FNCKEEEASY VYNELQKYEK DFSSCLQNEL CVEKSNMNGG
SDSLTPELID LVEEEKQKGF QHPHVLNSMK FASNEPDLPR KSPKTVLFSQ DQIYTENFHN
GPFMAHENST SQQTPGSLPV EADATSKESD ADERMNAMSS VAAEVSSLEH RNKNPNSSND
LNDVNPDTCS LKRQCPIVSS EITQSDGKVS EDPQTLMIEV IDIDNSMNMS THPAQLHNVE
MDAVTCDSTA VPEVRYRFGI GSPVRGESTT SEFAEVQPSN ANLMPLLQIL QLQSDFKKEF
EELGEKYSML HQNLDIAVAL KNKELETQRN IVRMHMLLAE AWILPDSF
//
