ID G4ZBD5_PHYSP Unreviewed; 1020 AA.
AC G4ZBD5;
DT 14-DEC-2011, integrated into UniProtKB/TrEMBL.
DT 14-DEC-2011, sequence version 1.
DT 27-MAR-2024, entry version 54.
DE RecName: Full=Chromodomain protein {ECO:0008006|Google:ProtNLM};
DE Flags: Fragment;
GN ORFNames=PHYSODRAFT_388148 {ECO:0000313|EMBL:EGZ22731.1};
OS Phytophthora sojae (strain P6497) (Soybean stem and root rot agent)
OS (Phytophthora megasperma f. sp. glycines).
OC Eukaryota; Sar; Stramenopiles; Oomycota; Peronosporales; Peronosporaceae;
OC Phytophthora.
OX NCBI_TaxID=1094619 {ECO:0000313|EMBL:EGZ22731.1, ECO:0000313|Proteomes:UP000002640};
RN [1] {ECO:0000313|EMBL:EGZ22731.1, ECO:0000313|Proteomes:UP000002640}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=P6497 {ECO:0000313|EMBL:EGZ22731.1,
RC ECO:0000313|Proteomes:UP000002640};
RX PubMed=16946064; DOI=10.1126/science.1128796;
RA Tyler B.M., Tripathy S., Zhang X., Dehal P., Jiang R.H., Aerts A.,
RA Arredondo F.D., Baxter L., Bensasson D., Beynon J.L., Chapman J.,
RA Damasceno C.M., Dorrance A.E., Dou D., Dickerman A.W., Dubchak I.L.,
RA Garbelotto M., Gijzen M., Gordon S.G., Govers F., Grunwald N.J., Huang W.,
RA Ivors K.L., Jones R.W., Kamoun S., Krampis K., Lamour K.H., Lee M.K.,
RA McDonald W.H., Medina M., Meijer H.J., Nordberg E.K., Maclean D.J.,
RA Ospina-Giraldo M.D., Morris P.F., Phuntumart V., Putnam N.H., Rash S.,
RA Rose J.K., Sakihama Y., Salamov A.A., Savidor A., Scheuring C.F.,
RA Smith B.M., Sobral B.W., Terry A., Torto-Alalibo T.A., Win J., Xu Z.,
RA Zhang H., Grigoriev I.V., Rokhsar D.S., Boore J.L.;
RT "Phytophthora genome sequences uncover evolutionary origins and mechanisms
RT of pathogenesis.";
RL Science 313:1261-1266(2006).
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DR EMBL; JH159153; EGZ22731.1; -; Genomic_DNA.
DR RefSeq; XP_009525448.1; XM_009527153.1.
DR AlphaFoldDB; G4ZBD5; -.
DR STRING; 1094619.G4ZBD5; -.
DR EnsemblProtists; EGZ22731; EGZ22731; PHYSODRAFT_388148.
DR GeneID; 20650996; -.
DR KEGG; psoj:PHYSODRAFT_388148; -.
DR InParanoid; G4ZBD5; -.
DR OMA; DDDKAFM; -.
DR Proteomes; UP000002640; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0140658; F:ATP-dependent chromatin remodeler activity; IEA:InterPro.
DR CDD; cd17995; DEXHc_CHD6_7_8_9; 1.
DR CDD; cd18793; SF2_C_SNF; 1.
DR Gene3D; 2.40.50.40; -; 2.
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; IPR016197; Chromo-like_dom_sf.
DR InterPro; IPR000953; Chromo/chromo_shadow_dom.
DR InterPro; IPR023780; Chromo_domain.
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 PANTHER; PTHR45623; CHROMODOMAIN-HELICASE-DNA-BINDING PROTEIN 3-RELATED-RELATED; 1.
DR PANTHER; PTHR45623:SF11; KISMET, ISOFORM C; 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; SM00487; DEXDc; 1.
DR SMART; SM00490; HELICc; 1.
DR SUPFAM; SSF54160; Chromo domain-like; 2.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR PROSITE; PS50013; CHROMO_2; 2.
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 Helicase {ECO:0000256|ARBA:ARBA00022806};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000002640};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT DOMAIN 125..200
FT /note="Chromo"
FT /evidence="ECO:0000259|PROSITE:PS50013"
FT DOMAIN 212..275
FT /note="Chromo"
FT /evidence="ECO:0000259|PROSITE:PS50013"
FT DOMAIN 331..527
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 670..822
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 1..64
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 102..148
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 996..1020
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 15..32
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 49..64
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 102..127
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 997..1020
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1020
FT /evidence="ECO:0000313|EMBL:EGZ22731.1"
SQ SEQUENCE 1020 AA; 117506 MW; 1FC19EFB44912DC0 CRC64;
MSSDEEEEKP KPKPKPKKKA PTKGKAKGKG KRKRSSSESS ENLSGEDSEV EVVETRPKPD
SDGFIIDKVL GREVHTLKEW KKMCWNKNTR FLTHCSIFLP NEEDDKPEEM QEQKEKEDGD
KPDSEAVESA AETASTPKAS TDDDEVEDAG EERFLIKWKT LSYLHTSWQT EDELMETDKN
AKGKIQRFSE KEHRALYTQE VQGDEYFNPE FRSVDRILEI RDRPLDDFAP DDAEDGEQKF
QYFLVKWKAL SYDDITWERE DDVGDDAAVQ QYNDRIVRAA KRFRKIALAK HLPNSKRKNF
RGYTAEAPPP RRKEQSFQLR DYQLTGVNWM LFNWYQKRNS MLADEMGLGK TVQTVMYINH
LAVVERTPNP FIIVAPLSTL GHWQREFECW TNLNAVVYHG SAAARDILQN YEFFLTEDEL
LRADGLSGKT NSNGKKAPPR PKRNCYRFDV LITTYEMASA TDLYKLAQIN WQLMVVDEAH
RLKNRNSKLS NLLHTRFTFE NMLLLTGTPL QNNVEELWVL LNFLDDKKFN SKEDFLESFG
ELTDSAQVER LHSELKPYLL RRMKEDVEKS LAPKEETIIE VELTVLQKQY YRAIYEKNTE
FLSRGGKKGD TPSLMNVLME LRKCCNHPFL VKGVEEREVK RLAKQTSVSK EDIQRQIRES
LVDTSGKLVL LDKLLPRLKE TGHRVLIFSQ FKIMLDIIQD YLALRRYNCE RIDGNITGNE
RQSAIDRFCR KDSTSFIMLL STRAGGVGIN LTAADTVIIY DSDWNPQNDL QAQARCHRIG
QKKSVKIYRL LTSKTYELHM FHKASLKLGL DQAVLGGIKN DDPVAKLKGS AKTSKPNDRM
SKEEIENLLK HGAYEMFKEQ ESEAEAASKK FGEESIDQIL SRSTTIVHDP TRDADGNEKK
NAMSSFSKAT FVSSTNPDEE VDIDDPNFWT KVIGLNGVEE QKKEEPSPLQ KRRCRRKVKS
YLIDDDKAFM MDDSGDEASS SRKKIFRELG VQKDEEFVIS DDDDDDDDDS SDVAMAKDDL
//
