ID A0A1S3JB55_LINUN Unreviewed; 2094 AA.
AC A0A1S3JB55;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 36.
DE SubName: Full=Chromodomain-helicase-DNA-binding protein 4 isoform X1 {ECO:0000313|RefSeq:XP_013407632.1};
GN Name=LOC106171731 {ECO:0000313|RefSeq:XP_013407632.1};
OS Lingula unguis.
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Brachiopoda; Linguliformea;
OC Lingulata; Lingulida; Linguloidea; Lingulidae; Lingula.
OX NCBI_TaxID=7574 {ECO:0000313|Proteomes:UP000085678, ECO:0000313|RefSeq:XP_013407632.1};
RN [1] {ECO:0000313|RefSeq:XP_013407632.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=26383154;
RA Luo Y.J., Takeuchi T., Koyanagi R., Yamada L., Kanda M., Khalturina M.,
RA Fujie M., Yamasaki S.I., Endo K., Satoh N.;
RT "The Lingula genome provides insights into brachiopod evolution and the
RT origin of phosphate biomineralization.";
RL Nat. Commun. 6:8301-8301(2015).
RN [2] {ECO:0000313|RefSeq:XP_013407632.1}
RP IDENTIFICATION.
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
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DR RefSeq; XP_013407632.1; XM_013552178.1.
DR STRING; 7574.A0A1S3JB55; -.
DR EnsemblMetazoa; XM_013552178.1; XP_013407632.1; LOC106171731.
DR GeneID; 106171731; -.
DR KEGG; lak:106171731; -.
DR InParanoid; A0A1S3JB55; -.
DR OrthoDB; 2910821at2759; -.
DR Proteomes; UP000085678; Unplaced.
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:0004386; F:helicase activity; 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 CDD; cd18667; CD1_tandem_CHD3-4_like; 1.
DR CDD; cd18662; CD2_tandem_CHD3-4_like; 1.
DR CDD; cd15531; PHD1_CHD_II; 1.
DR CDD; cd15532; PHD2_CHD_II; 1.
DR CDD; cd18793; SF2_C_SNF; 1.
DR Gene3D; 2.40.50.40; -; 2.
DR Gene3D; 1.10.10.60; Homeodomain-like; 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); 2.
DR InterPro; IPR012957; CHD_C2.
DR InterPro; IPR009462; CHD_II_SANT-like.
DR InterPro; IPR012958; CHD_N.
DR InterPro; IPR016197; Chromo-like_dom_sf.
DR InterPro; IPR000953; Chromo/chromo_shadow_dom.
DR InterPro; IPR023780; Chromo_domain.
DR InterPro; IPR002464; DNA/RNA_helicase_DEAH_CS.
DR InterPro; IPR009463; DUF1087.
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; 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; PF08074; CHDCT2; 1.
DR Pfam; PF06461; CHDII_SANT-like; 1.
DR Pfam; PF08073; CHDNT; 1.
DR Pfam; PF00385; Chromo; 1.
DR Pfam; PF06465; DUF1087; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR Pfam; PF00628; PHD; 2.
DR Pfam; PF00176; SNF2-rel_dom; 1.
DR SMART; SM00298; CHROMO; 2.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM01146; DUF1086; 1.
DR SMART; SM01147; DUF1087; 1.
DR SMART; SM00490; HELICc; 1.
DR SMART; SM00249; PHD; 2.
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; PS00690; DEAH_ATP_HELICASE; 1.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR PROSITE; PS51194; HELICASE_CTER; 1.
DR PROSITE; PS50016; ZF_PHD_2; 2.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Helicase {ECO:0000256|ARBA:ARBA00022806};
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:UP000085678};
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 392..439
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS50016"
FT DOMAIN 450..497
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS50016"
FT DOMAIN 526..583
FT /note="Chromo"
FT /evidence="ECO:0000259|PROSITE:PS50013"
FT DOMAIN 616..677
FT /note="Chromo"
FT /evidence="ECO:0000259|PROSITE:PS50013"
FT DOMAIN 766..950
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 1081..1230
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 1..133
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 205..361
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 669..724
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1366..1428
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1558..1750
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1960..2094
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 1278..1331
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 51..67
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 108..133
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 236..259
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 289..305
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 306..322
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 336..352
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1380..1405
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1406..1422
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1573..1750
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1960..1981
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2008..2034
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2042..2074
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2075..2094
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2094 AA; 236943 MW; 0F9D07510790073A CRC64;
MTAPSETDTS PNDFLEPAVP ELDTQVSQNY DDDNEGALEI VLENKKGKKR KMKDGSEKKK
KAKKKKKGKS ASEEVDIGDG GNESVASMDV TLEESQGEDP ALEDDRNDDD YIPEKPAKEK
KKRPPKVDKD QKTAEEICQE HGLLNVELEY SDEDFVNLTT YKAYSAHIRP LLAKENPKCP
MTKMTSLVAA KWREFLALGA LPELQKEADP DISVEGSNDG DLGDVDSTPG TPSKQKGKKG
KGKGKSVAPL KIKLTKKKKR KKGSDEELEE GGGFNTSDEE FERQLEEASI ISEVQSESSN
MSAPKKSKVK KGRGRNAKKA KVKKGSFLSE AEAEGYEASP SNSLSQEPQG TPTVRKCKMK
KGRGRNASKK IKRTSTFPAN LNDADGYETD HQDYCEVCQQ GGEIILCDTC PRAYHLVCLD
PELEEAPEGK WSCPHCEAEG AQEQEEDEHM EFCRACKDGG DLLCCDSCPS AYHMHCLNPP
MKEIPDGEWH CPRCGCEPLK GKVQKVLTWR WVEPPKMADE LDHTHSPTKK KFDHKPTREF
FVKWHDMSYW HCSWITELQY DVYHPAMYRN YIRKNDMDEP PPLEDGSSFG MKDYKEEDPH
NLEGRFYRYG VRPEWLTINR IINHRQTRDG RTWYLVKWRD LPYEQATWEN EESGIAEFDK
EVERYHQLRE QMSKPRNRRS MMLGQTGSAK GGKKGGKGKK GKGKGKGKDR EDEEETEEEA
SKQMFKLPPE VPVVDLKRKL DQQPDYIDIT GGTLHPYQLE GLNWLRYSWC HGIHTILADE
MGLGKTIQTI VFLYSLYKEG HSKGPFLVSA PLSTIINWER EFEFWAPDFY VVTYVGDKDS
RAVIREHEFS FEEGAIRGGT KASKMRKECP VKFHVLLTSY ELISIDQATL GSVDWGVLVV
DEAHRLKNNQ SKFFKVLSAY KIGYKLLLTG TPLQNNLEEL FHLLNFMSPD DFRNLQVFLD
EFADIGKEEQ VKKLHDMLGP HLLRRLKADV LKGIPSKSEF IVRVELSPMQ KKYYKYILTR
NFEALNARGG NNVSLLNIMM DLKKCCNHPY LFPTAADEAP KLPNGMFEGS ALIKACGKLE
LLSKMLNILK EEGHRVLIFS QMTKMLDILE DFLECEGYKY ERIDGGVTGT LRQDAIDRFN
MNGSPSMVFL LSTRAGGLGI NLATADTVII YDSDWNPHND IQAFSRAHRI GQANKVMIYR
FVTRASVEER ITQVAKKKMM LTHLVVRPGL GGKGGSMSKQ EVDDILKFGT EELFKDEFKT
EDSSQANESR IVYDDAAVKE LLDRTQQGQE EKEMAMNEYF TSFKVASYAF KEEEEEEEEE
KEILKQEVEH ADPAYWEKLL RHHYEQQQED LARTLGKGKR VRKQVNYNDA MGGTNEDNWD
ENMSDFDSDF DQTGNGDDED DDFEEKSELG RGGRRRGGVP EKDRPLPPLL ARVNGQIEVL
GFNARQRKAF LNAVMRWGMP PQDAFNSHCR LVRDLRGKSE KVFKAYVSLF MRHLCEPGAD
NADTFADGVP REGLSRQHVL TRIGIMSLVR KKVQEFEAIN GTESMPYKTA SECIEKFSKS
RSSSAVPSPA PSTKEEKTEE KGETKEDQKE IKEEKTEEDK EGSGDKKDKD EGKETTEEAM
ETDQKGNEPS EKEDSKDAAQ EVKMETDEVK EEKKETDEKP TQATEESKDS EESKADVNEE
SKEEDVKDEK EEQKTDSLEE KKELKKEEAE GEKDEKKDDA KVKEEKDSDG TTKKSSKEEE
AKKSDEKEEE FKKEEAKQKF MFNIADGGFT ELHTLWQNEQ RALTVGREHE VWHRRHDYWL
LAGIVTHGYG RWQDIQNDVR FAIINEPFKG EVGKGNFLEI KNKFLARRFK LLEQALVIEE
QLRRAAYLNL TQDPNHPAMA LNARFAELEC LAESHQHLSK ESLAGNKPAN AVLHKVLNQL
EELLSDMKQD VSRLPSTLSR IPPVTQRLQM SERNILNRLV NPGQGSAQPS ASGTPSHTPS
STPTPSAQPS PAPPSGQQMA GLPQNPFSAL PPGFPPMGVR PPFGMPPVGF PPQGQLPQAS
PVAAVGKQTT TLPPAHKTTT PATASSGQAE DLSSKKTEGG SEGRKKDVIM LDDD
//
