ID M2W1Y1_GALSU Unreviewed; 1139 AA.
AC M2W1Y1;
DT 01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 01-MAY-2013, sequence version 1.
DT 27-MAR-2024, entry version 46.
DE SubName: Full=DNA binding / methyl-CpG binding protein isoform 2 {ECO:0000313|EMBL:EME29691.1};
GN ORFNames=Gasu_29130 {ECO:0000313|EMBL:EME29691.1};
OS Galdieria sulphuraria (Red alga).
OC Eukaryota; Rhodophyta; Bangiophyceae; Galdieriales; Galdieriaceae;
OC Galdieria.
OX NCBI_TaxID=130081 {ECO:0000313|EMBL:EME29691.1, ECO:0000313|Proteomes:UP000030680};
RN [1] {ECO:0000313|Proteomes:UP000030680}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=074W {ECO:0000313|Proteomes:UP000030680};
RX PubMed=23471408; DOI=10.1126/science.1231707;
RA Schonknecht G., Chen W.H., Ternes C.M., Barbier G.G., Shrestha R.P.,
RA Stanke M., Brautigam A., Baker B.J., Banfield J.F., Garavito R.M., Carr K.,
RA Wilkerson C., Rensing S.A., Gagneul D., Dickenson N.E., Oesterhelt C.,
RA Lercher M.J., Weber A.P.;
RT "Gene transfer from bacteria and archaea facilitated evolution of an
RT extremophilic eukaryote.";
RL Science 339:1207-1210(2013).
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, spindle
CC {ECO:0000256|ARBA:ARBA00004186}. Nucleus
CC {ECO:0000256|ARBA:ARBA00004123}.
CC -!- SIMILARITY: Belongs to the INCENP family.
CC {ECO:0000256|ARBA:ARBA00010042}.
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DR EMBL; KB454506; EME29691.1; -; Genomic_DNA.
DR RefSeq; XP_005706211.1; XM_005706154.1.
DR AlphaFoldDB; M2W1Y1; -.
DR STRING; 130081.M2W1Y1; -.
DR EnsemblPlants; EME29691; EME29691; Gasu_29130.
DR GeneID; 17088468; -.
DR Gramene; EME29691; EME29691; Gasu_29130.
DR eggNOG; KOG1245; Eukaryota.
DR OrthoDB; 462469at2759; -.
DR Proteomes; UP000030680; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0005819; C:spindle; IEA:UniProtKB-SubCell.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0007059; P:chromosome segregation; IEA:UniProtKB-KW.
DR CDD; cd15543; PHD_RSF1; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR005635; Inner_centromere_prot_ARK-bd.
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; PTHR45915:SF2; IP14655P-RELATED; 1.
DR PANTHER; PTHR45915; TRANSCRIPTION INTERMEDIARY FACTOR; 1.
DR Pfam; PF03941; INCENP_ARK-bind; 1.
DR Pfam; PF00628; PHD; 1.
DR SMART; SM00249; PHD; 1.
DR SUPFAM; SSF57903; FYVE/PHD zinc finger; 1.
DR PROSITE; PS01359; ZF_PHD_1; 1.
DR PROSITE; PS50016; ZF_PHD_2; 1.
PE 3: Inferred from homology;
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Cytoskeleton {ECO:0000256|ARBA:ARBA00023212};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000030680};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00146}.
FT DOMAIN 209..259
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS50016"
FT REGION 81..188
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 287..391
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 457..522
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 618..1055
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 96..126
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 172..187
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 301..323
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 348..379
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 457..521
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 618..632
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 650..665
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 684..707
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 716..737
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 776..836
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 837..856
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 863..979
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1007..1055
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1139 AA; 129790 MW; 05FAA167438EBAB4 CRC64;
MESIPTEQRH SSPYLEQVLQ ALDAARKQAL EELQQQAEDI REWCTTTTQN TCKSLTEEYK
YMTLVGKRKN SYEKVTLGLL CPPSTKKKRS TSNNRKSKKV DKLHCLKDQE TAGREQDNHQ
QMEEDPYEFK EDEEEEEEAV KQRRKRRSKA SNQQKWEAPR QSRRSKRGHS KLSEHKITVE
KKSHGSVDLD SLSPYSRAIA QGRSPTKYET YCRVCKKTDY EDLLLLCDHC DDAFHTFCCN
PRLQSVPEGD WFCPKCTNNA TVDTTNRWNM DVDNSIQDKP VEVANSDVQQ EQQCGKNDIS
LETQVKDDDE KEATDKKELN HCEEPLTLNN SESSALQIRR PRKARKGSKR VEKTESSNKS
TKAVGKRGRP RKEQSQAKDL VTSHPKQEGS FSDYLDGIAA IMEGEISEQA SLNKNNSNNV
AISKQQESLQ VEKSGLTSSG DSVSSLHLGT IMKPLEEAHN SEQENNEKQL SPKYHSHRMS
SIEDDCKTPG RKPQENLSSR KERTQERYVN VHREDETEQS NTKENVAVVE KVWQMFNIDS
TGSVAVEETS KTPSSKAVGK GVQAVTKTSE RKLQSLTESI YKKKKKIGRV GDKSSGLVGL
ESISNLSTAL FSKLDNTTRD IQGEEKPLEV HGTEENPTQA VVDVDNATLS PAEKKGKEEK
VSNPNSRDLS EMQPLKLSSP PEEADDTHSQ PQVTSKPLSN NSRAAELRSK IQRLRSNQEE
VQPSSDPKSV GSSSKEDNSS AEKVKTPQVG IFKRIASLFG SPSPFKKASP PESKAVEGPT
QESTQLLVDP TSPNSRHHLT SVKSSPSKTS EKSGLPVAPS KGSNIVTSFS SFLSNNGREK
KNEDPNKKEV KSVGTNTKMV EEKLAQMDAK KKAIQEQKRR ENEEKLRRAE ERRKQQALEE
QRKEEERKKQ EEERERRRKE QALLLKKAKE EEEAKRKEES RKRHEELVAK QAMEAERRRK
ELEMKEHRLH HENNDLNSNK WKNEQRSLGL RPKAVTECNA QETEPLVLKD KNTESHVTPD
SKGHTEAHNS YQLTDEKQKH EDEDSDEEYE RRKRKRIPSW ARSHNLRELL QQQVNVNPEE
IFPCADTCDL EEIFGPNERK KRYRNRQRTS SGNWSASERS LLLSPDSTIN KSSELSHIR
//
