ID A0A022RCS1_ERYGU Unreviewed; 1754 AA.
AC A0A022RCS1;
DT 11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT 11-JUN-2014, sequence version 1.
DT 24-JAN-2024, entry version 46.
DE RecName: Full=Histone acetyltransferase {ECO:0008006|Google:ProtNLM};
GN ORFNames=MIMGU_mgv1a000112mg {ECO:0000313|EMBL:EYU37854.1};
OS Erythranthe guttata (Yellow monkey flower) (Mimulus guttatus).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; lamiids; Lamiales; Phrymaceae; Erythranthe.
OX NCBI_TaxID=4155 {ECO:0000313|EMBL:EYU37854.1, ECO:0000313|Proteomes:UP000030748};
RN [1] {ECO:0000313|EMBL:EYU37854.1, ECO:0000313|Proteomes:UP000030748}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. DUN x IM62 {ECO:0000313|Proteomes:UP000030748};
RX PubMed=24225854; DOI=10.1073/pnas.1319032110;
RA Hellsten U., Wright K.M., Jenkins J., Shu S., Yuan Y., Wessler S.R.,
RA Schmutz J., Willis J.H., Rokhsar D.S.;
RT "Fine-scale variation in meiotic recombination in Mimulus inferred from
RT population shotgun sequencing.";
RL Proc. Natl. Acad. Sci. U.S.A. 110:19478-19482(2013).
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DR EMBL; KI630513; EYU37854.1; -; Genomic_DNA.
DR STRING; 4155.A0A022RCS1; -.
DR eggNOG; KOG1081; Eukaryota.
DR eggNOG; KOG1862; Eukaryota.
DR eggNOG; KOG1946; Eukaryota.
DR Proteomes; UP000030748; Unassembled WGS sequence.
DR GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR CDD; cd19757; Bbox1; 1.
DR CDD; cd00072; GYF; 1.
DR CDD; cd15568; PHD5_NSD; 1.
DR CDD; cd10567; SWIB-MDM2_like; 1.
DR Gene3D; 3.30.1490.40; -; 1.
DR Gene3D; 3.90.70.200; Plus-3 domain; 1.
DR Gene3D; 1.10.245.10; SWIB/MDM2 domain; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR003169; GYF.
DR InterPro; IPR035445; GYF-like_dom_sf.
DR InterPro; IPR004343; Plus-3_dom.
DR InterPro; IPR036128; Plus3-like_sf.
DR InterPro; IPR019835; SWIB_domain.
DR InterPro; IPR036885; SWIB_MDM2_dom_sf.
DR InterPro; IPR003121; SWIB_MDM2_domain.
DR InterPro; IPR019786; Zinc_finger_PHD-type_CS.
DR InterPro; IPR000571; Znf_CCCH.
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; PTHR46695:SF5; RNA POLYMERASE-ASSOCIATED PROTEIN RTF1 HOMOLOG; 1.
DR PANTHER; PTHR46695; ZINC FINGER CCCH DOMAIN-CONTAINING PROTEIN 44-RELATED; 1.
DR Pfam; PF02213; GYF; 1.
DR Pfam; PF03126; Plus-3; 1.
DR Pfam; PF02201; SWIB; 1.
DR SMART; SM00444; GYF; 1.
DR SMART; SM00249; PHD; 1.
DR SMART; SM00719; Plus3; 1.
DR SMART; SM00151; SWIB; 1.
DR SUPFAM; SSF57903; FYVE/PHD zinc finger; 1.
DR SUPFAM; SSF55277; GYF domain; 1.
DR SUPFAM; SSF159042; Plus3-like; 1.
DR SUPFAM; SSF47592; SWIB/MDM2 domain; 1.
DR PROSITE; PS50829; GYF; 1.
DR PROSITE; PS51360; PLUS3; 1.
DR PROSITE; PS51925; SWIB_MDM2; 1.
DR PROSITE; PS50103; ZF_C3H1; 1.
DR PROSITE; PS01359; ZF_PHD_1; 1.
DR PROSITE; PS50016; ZF_PHD_2; 1.
PE 4: Predicted;
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|PROSITE-
KW ProRule:PRU00723}; Reference proteome {ECO:0000313|Proteomes:UP000030748};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|PROSITE-ProRule:PRU00723};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00723}.
FT DOMAIN 627..693
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS50016"
FT DOMAIN 844..927
FT /note="DM2"
FT /evidence="ECO:0000259|PROSITE:PS51925"
FT DOMAIN 985..1118
FT /note="Plus3"
FT /evidence="ECO:0000259|PROSITE:PS51360"
FT DOMAIN 1317..1371
FT /note="GYF"
FT /evidence="ECO:0000259|PROSITE:PS50829"
FT DOMAIN 1729..1754
FT /note="C3H1-type"
FT /evidence="ECO:0000259|PROSITE:PS50103"
FT ZN_FING 1729..1754
FT /note="C3H1-type"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00723"
FT REGION 23..50
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 324..350
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 407..442
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 456..620
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 771..845
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 950..981
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1160..1247
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1261..1282
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1396..1418
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1663..1736
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 36..50
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 422..442
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 456..493
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 506..543
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 553..574
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 575..600
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 780..797
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 826..845
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1160..1201
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1219..1247
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1262..1276
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1665..1679
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1682..1696
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1754 AA; 191329 MW; A49F4228BE5E8848 CRC64;
MEEEKLDFVG IESSEKCEAI PEFGESTLTV GGDRDPSPEN KPDADEKGEG ILVNHAEEQG
SEFIAEGLTD MVEQSVVAEE GGCEITAAQI EELPIEMEAE EEAKIDEAEE EAEIDAEGVA
AVTDTEPLFS ETQVISGGED EMLADPQIGL EAEQEFTPAV DSIVEGVVTD VSDAHNLADP
QIGSEAEQEF TPAVDPIVEG VVTDVSDAHN LADPQIVSEA EQEFTPAVDP IVEGVVTDAS
DAHNFSELQV DSNVDELHAT VEGIEAEDYK SEGDMDEGEN VKAVGGLDNE SADSLIEANT
ETVVKDDEIK DDEVDEPKVD FVENDSEVGA AEKPADVEEE KVDFINEEMP ITEVKRETEA
TTEINTFIGN TTEQEQVNES TGVKEFVSCD VSYDHAVDKE VAVEESLMSS NSELDESLTV
AENEDTIVKE EPSSGDIKTE TEALEELEST RKVVVEEEIQ LEGHEVETEM ESEVMADRIP
DDEDGKMETE EQMGSEVMAD QIPDDEDGKM ETEEQMGSEV MADEIQDDDG KMETEETTSD
VDETGQDIYD SPAALQDEED DTMAAEEDDT MPAEEDAGAH DTEIETETDI AEAEKTSGGK
RKRNKLSKST PISKATPKAS SRKTVGEDVC FICFDGGELV LCDRRGCPKA YHPSCVNRDE
AFFKSKGRWN CGWHLCSICE KNARYMCYTC TFSLCKSCTK DAVILCIQGN KGFCETCMRT
VMLIESNEQG DKDDQIDFDD KSSWEFLFKD YYTELKAKLS LSSDDIAQAK NPWKGADMSG
PSKQESSEAQ ADGNDGGSGS EDSIEKLETV RPKRRKIRKQ SKSRSKGEGS VSTSTAAGDK
ANNLSDNSEW ASKELLEFVS HMKDGDTSIL SQFDVQALLL EYIQRNKLRD PRKKSQIVCD
GRLENLFGKS RVGHFEMLKL LESHFFVRDE HNDDLQGSVV DTENSLLDID GSGEPLTKGV
KDKKRKPRRK GDSRGPQSNL DDYAAIDMHN IGLIYLRRKL IEDLLEDDET FHDKAVGTFV
RIRISGSTQK QDMYRLVQVV GTSKAPEPYK IGKKSTDTMV EILNLDKTEI ISIDTISNQE
FTEEECTRLR QSIKCRLLSP LTVGEILDKT TEIQTARVND WLEAEVLRLS HLRDRASDLG
RRKELRECVE KLQLLKTPEE RRRRLEETPK IHSDPKMDPS YESEDNSENE NNRREAFMRS
RGSGFSRRGR GPISPGSEHS VKDSWSSPGN ITNKNSELSR ASPGNNFSVN ASHISEIANE
NSWNLEREKE KQESNYSEKL NAPTYPESYG GVTSVISQAS LSSAVLETAA VKINESEKMW
HYKDPSGKVQ GPFSMVQLRK WNNTGYFPTG LQIWRNTDNQ DNSVLLADAL AGKFPIPSAT
AGNIISQADK LAGHSGKTSG TFLNQDNQNS GPRSKTSAEK WAVNDMTNMP SPTPTQRGHL
INGAVPSPII GTHSSTPASV LSAIIETATF SPTPNSQLGG SSAVSRHSHS TTVTEQHEVP
MQGWGQSGQV QAYNWGTPSN VQNPSGSFQN SGSTVGIQQD MWRPTQGSVP NMIPPTQGSV
PNMIPPTTPN ASIGVRPENP NMGWGGTNTM QANPNMGWVN PAPVNANANW MPAMQVPVPQ
PGSYVAPPAG NAAAANIQGW GAPAQGWGAP PVQGGPVPGN GWAPPGGNVG PPPPPAVNQG
WGGPQAGNQG SWGGEQMPSG GQFMGGQRGP WNRQSSFGGG GGGGGGSRSK RDTLCPFNLN
GRCKKGSRCD YMHS
//
