ID W1PK58_AMBTC Unreviewed; 2626 AA.
AC W1PK58;
DT 19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT 19-MAR-2014, sequence version 1.
DT 27-MAR-2024, entry version 58.
DE RecName: Full=PHD-type domain-containing protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=AMTR_s00148p00090060 {ECO:0000313|EMBL:ERN08403.1};
OS Amborella trichopoda.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Amborellales; Amborellaceae; Amborella.
OX NCBI_TaxID=13333 {ECO:0000313|EMBL:ERN08403.1, ECO:0000313|Proteomes:UP000017836};
RN [1] {ECO:0000313|Proteomes:UP000017836}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=24357323;
RG Amborella Genome Project;
RT "The Amborella genome and the evolution of flowering plants.";
RL Science 342:1241089-1241089(2013).
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DR EMBL; KI393463; ERN08403.1; -; Genomic_DNA.
DR STRING; 13333.W1PK58; -.
DR EnsemblPlants; ERN08403; ERN08403; AMTR_s00148p00090060.
DR Gramene; ERN08403; ERN08403; AMTR_s00148p00090060.
DR eggNOG; KOG0383; Eukaryota.
DR eggNOG; KOG0384; Eukaryota.
DR HOGENOM; CLU_227737_0_0_1; -.
DR OrthoDB; 357661at2759; -.
DR Proteomes; UP000017836; Unassembled WGS sequence.
DR GO; GO:0000785; C:chromatin; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IBA:GO_Central.
DR GO; GO:0140658; F:ATP-dependent chromatin remodeler activity; IBA:GO_Central.
DR GO; GO:0003682; F:chromatin binding; IBA:GO_Central.
DR GO; GO:0003677; F:DNA binding; IBA:GO_Central.
DR GO; GO:0004386; F:helicase activity; IEA:UniProtKB-KW.
DR GO; GO:0042393; F:histone binding; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006338; P:chromatin remodeling; IBA:GO_Central.
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; 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; IPR011011; Znf_FYVE_PHD.
DR InterPro; IPR001965; Znf_PHD.
DR InterPro; IPR019787; Znf_PHD-finger.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR45623:SF13; CHROMODOMAIN-HELICASE-DNA-BINDING PROTEIN 3-RELATED; 1.
DR PANTHER; PTHR45623; CHROMODOMAIN-HELICASE-DNA-BINDING PROTEIN 3-RELATED-RELATED; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR Pfam; PF00628; PHD; 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; SSF57903; FYVE/PHD zinc finger; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR PROSITE; PS50013; CHROMO_2; 2.
DR PROSITE; PS51194; HELICASE_CTER; 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 Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000017836};
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 603..652
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS50016"
FT DOMAIN 663..727
FT /note="Chromo"
FT /evidence="ECO:0000259|PROSITE:PS50013"
FT DOMAIN 750..816
FT /note="Chromo"
FT /evidence="ECO:0000259|PROSITE:PS50013"
FT DOMAIN 1147..1310
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 1..325
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 340..376
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 408..471
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1471..1494
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1511..1549
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1670..1737
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1879..1898
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2443..2545
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..20
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 56..78
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 118..157
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 158..174
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 175..191
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 265..287
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 288..325
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 410..432
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 440..456
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 457..471
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1513..1535
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1676..1693
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1702..1718
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1720..1737
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2457..2481
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2482..2513
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2521..2535
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2626 AA; 289156 MW; 16A9171183C379DB CRC64;
MSKVNRSARK LRDEDLTSSS GSFSRKRMGL RPKGSDIRGS LTNSSGLRRS AREVLSKKRK
SLSSSSQKKL DKADKSGSPS HLSPKTSKKK TKKIGVLSLL KGKKVDKSGK KVSLSPSSKK
VKKTDKHVAS KSGKGEKKRA STSASSKKSE KNEKKVGSSS SNKSGNGGTQ ETTSSKESGH
KENGADKNAL KPRRKFLHRH VYREYFITRP PKVEDANASG TDAGKSAHSE GKDDNQVSLG
GTKLHSKFER VVAGSGSNSK KDANGITNGK ERDVIHPNKK QKFDTEEGHL MSNSQSTPAS
QSQSEDSRSK NQSTDSQTSL DSPTIKEVFN DVDFEKTQLQ GSVTKGKAAL VDSVSSDKGA
EMVGSTNEDH GEKDNISLQE NVESAFSEAK YEAVDTNKDA DYLAQNACKD KVSQRKRKTA
DRDDDTKVTA HKDLCGLESS SGDAASSSPP KSKRNKVSGT SEVRDGSVSE DHCATNLELQ
RVNDDSRNLV FMANVKASFT AVSTSEEVSE RVSRSSPEIG VVVSCPQEEK AVKIFKFDAS
GKPDECRKKN INGLIGSCTT PNGALSLEED RVRLQVSASR EIFEENADSS QHKDLNDHAN
RQINACIICN RGGKLLCCEG KGCSKSYHLQ CLDPPLEHVP PGVWHCLSCV KKKIELGLHS
VSEGIESIWD VRDAKISNDG SMVSKEQLQE FFVKYKGLAH VHNRWVPKSQ LLSEAPAVLA
KYNKNNQKGK FVKWNSEWTK PHRLLQKRFL MPPNIFFRCR SHLFGCNTEW LVKWRGLDYE
HITWELESAT FFSSPEAKCL FRDYESRLEK AKKVSDPSIT EKIQKQRVST FLRLQKMTGG
ALAGQEGLHL SSVNKLREMW HKGSNALVID DQERIARVIS FILSLQSDIC CPVLIVTTSS
EVSVWESEFM RLASSVNVVV YSGSKDVRES IRTLEFYSQN GCVLFEVLVS ASDAIVEDLE
ALDCLRWEAI IVDECHRSRV SRNLQQLGKL VTDFRLLLFR DQVKDSLTDY RNLLSFLEAK
VETVSGKSSP NDSNNNSAVE LKERFSRYLA YENKSDSSKF IEYWVPVPLS DVQLEQYCTI
LVSNAISLRS NLRNDQVGAL QGILISTRKC CDHPYLVNTS LQGLLTEGLP PVEFLDVGVN
ASGKLQLLDK VLTRMKSHGQ RVLILFQLIG GSGPHSIGDI LDDYLRQRFG AESYERIDSG
LLSSKKQAVL QMFNNKEKGR FVFLLENRAC LPSIKLSSVD NIIIFDSDMN PLNDLRALQK
ITIDSPHDKL KVFRFYSPYT MEERVLCFAK QDMVLESNVQ NISRGMNHLL LMWGATYLFN
KLEELRNMKS SSMGTMHSCD QKFLKDVASE LLNKMLVGNE TSDGNDSNVV LRVLRGGLGY
NRLNSLLGES EMNSVGGELP QAFWSKLLQG KSPEWSHLTG TLQRTRKKVQ HFDGSTKKLE
PENVNLEAKK KRKKQLSTID PATLTPWLQD KKKAVAEGKK ESIGLHGSAP PSATKNTAYC
SNIAEETGGM SGVPEATTAS NHGVPGLSTS RTKPNPEIPG IHRTESEDGR SIRVAQRSLH
LLMKPELSKL SETLHLPENV KSIAAEFLDY VMNNHNVPRE PETILQAFQI SLCWIAASVL
KYKMDRDASL ALARCELKFE CKKEEAESVY LKLKQLRPFL KDITRGQVFS GEADSGSQDD
RSRSSRGTDA HELEEAEICE DGEIREESRE RDMRVPTEKV NPHPNTNESV KDNGPHTNAS
LIAKLNAVKH SRMQYVLQKQ KDEVAEIISF WKREKQKLER AKEIEGTRIF DKYKNSSSLL
KEKSKSLKDI YAEKMDALDK RVEKYQQNLF ERQHGIRNEE NHLYSVWTEV VKSGKLKKPC
FDHPLPKFGL RLEDLGSFSN SHSGENDSRN GRPVLGSPIE SKIDMQALGG LAKSRSLNLM
AEAEESNLVI EQRVSAGNIA METVTVAADT GANCLDGRDV EVVTVGEISQ DSARNQFQPG
PGLGDLQPSH EITVDHNRHA VNAVRESVYG TAPEPLSIPM VQRDDATLLQ PESSDHIASP
SRPIIETHNE SAVCDVAKRQ NGPAISDREN GPAACSTVDG QNGPAVGAIE ERENGVAACS
NVEGENGPAV GVITEGGLGP AVGAITGREN GLAIGAITDR ENGLAVRTIA EREHGPSIAE
RESCQAVVAP VEKETGPVGA IVDGENLPAV GAIVDRENGP TVVTIAERAV CVTSERENGL
GVGLAENQNG PELGPTLERE NGPAVCTIIE RENNHAACAI TGRESGLTPE PRAPSTQPQL
EDLNLIASPS RPVMELQQES LGITLHTEVP STSGSGSGSA LLASIMQPVQ TAPSASRSLQ
PGQSDPLFNE IIRISKEQEM ATKKYEDDKL RLKLECEREI EEVKRKYGAL LQDTETAFSR
KKTVFEANLS KVNMNRWLAE AFKLRLHDLK MSPLLVQAPL PGNPSSLLHS HQPVPRPMHP
LATPSVPHPS NPNPSGPYHS SPQPSVDPTN QLFPQHQWPH QALDQRATRP QSPSLLRPPS
PNPNILSSSG TGQLPPFNPV PFPSQLDSTH LGAQIPVMMG MPHLVSPQFR VLSTVGSTQA
MDPSSLANVD LPGTNSQDLS SFLDTNLAFD MGVSSQPQVV YLSDDD
//
