ID A0A3Q0CPH9_MESAU Unreviewed; 1052 AA.
AC A0A3Q0CPH9;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE SubName: Full=MDS1 and EVI1 complex locus protein EVI1 isoform X3 {ECO:0000313|RefSeq:XP_021082586.1};
GN Name=Mecom {ECO:0000313|RefSeq:XP_021082586.1};
OS Mesocricetus auratus (Golden hamster).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea;
OC Cricetidae; Cricetinae; Mesocricetus.
OX NCBI_TaxID=10036 {ECO:0000313|Proteomes:UP000189706, ECO:0000313|RefSeq:XP_021082586.1};
RN [1] {ECO:0000313|RefSeq:XP_021082586.1}
RP IDENTIFICATION.
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR RefSeq; XP_021082586.1; XM_021226927.1.
DR AlphaFoldDB; A0A3Q0CPH9; -.
DR Proteomes; UP000189706; Unplaced.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-KW.
DR GO; GO:0008168; F:methyltransferase activity; IEA:UniProtKB-KW.
DR GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR Gene3D; 3.30.160.60; Classic Zinc Finger; 8.
DR Gene3D; 2.170.270.10; SET domain; 1.
DR InterPro; IPR001214; SET_dom.
DR InterPro; IPR046341; SET_dom_sf.
DR InterPro; IPR036236; Znf_C2H2_sf.
DR InterPro; IPR013087; Znf_C2H2_type.
DR PANTHER; PTHR24393:SF15; IP01201P-RELATED; 1.
DR PANTHER; PTHR24393; ZINC FINGER PROTEIN; 1.
DR Pfam; PF21549; PRDM2_PR; 1.
DR Pfam; PF00096; zf-C2H2; 8.
DR Pfam; PF13912; zf-C2H2_6; 1.
DR SMART; SM00317; SET; 1.
DR SMART; SM00355; ZnF_C2H2; 10.
DR SUPFAM; SSF57667; beta-beta-alpha zinc fingers; 5.
DR SUPFAM; SSF82199; SET domain; 1.
DR PROSITE; PS50280; SET; 1.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 7.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 10.
PE 4: Predicted;
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125};
KW Metal-binding {ECO:0000256|PROSITE-ProRule:PRU00042};
KW Methyltransferase {ECO:0000256|ARBA:ARBA00022603};
KW Reference proteome {ECO:0000313|Proteomes:UP000189706};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Zinc {ECO:0000256|PROSITE-ProRule:PRU00042};
KW Zinc-finger {ECO:0000256|PROSITE-ProRule:PRU00042}.
FT DOMAIN 1..104
FT /note="SET"
FT /evidence="ECO:0000259|PROSITE:PS50280"
FT DOMAIN 123..151
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS50157"
FT DOMAIN 177..204
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS50157"
FT DOMAIN 205..232
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS50157"
FT DOMAIN 233..262
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS50157"
FT DOMAIN 263..290
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS50157"
FT DOMAIN 291..318
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS50157"
FT DOMAIN 320..347
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS50157"
FT DOMAIN 836..863
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS50157"
FT DOMAIN 864..892
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS50157"
FT DOMAIN 893..920
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS50157"
FT REGION 461..533
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 633..734
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 955..975
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1000..1052
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 474..494
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 495..515
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 517..533
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 676..691
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 701..721
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 955..969
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1007..1024
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1052 AA; 118266 MW; 9931195E06F6EDDE CRC64;
MPGAGLGIWT KRKIEIGEKF GPYMGEQRSD LKDSSYGWEI LDEFCNVKFC IDASQPDVGS
WLKYIRFAGC YDQHNLVACQ INDQIFYRVV ADIAPGEELL LFMKSEDDPH EPMAPDIHEE
RQHRCEDCDQ LFESKAELAD HQKFPCSTPH SAFSMVEEDL QQNLESESDL REIHGNQDCK
ECDRVFPDIQ SLEKHMLSHS EEREYKCDQC PKAFNWKSNL IRHQMSHDSG KHYECENCAK
QVFTDPSNLQ RHIRSQHVGA RAHACPECGK TFATSSGLKQ HKHIHSSVKP FICEVCHKSY
TQFSNLCRHK RMHADCRTQI KCKDCGQMFS TTSSLNKHRR FCEGKNHFAA GGFFGQGISL
PGTPAMDKTS MVNMSHANPG LADYFGTNRH PAGLTFPTAP GFSFSFPGLF PSGLYHRPPL
IPASPPVKGL SSTEQSNKCQ SPLLTHPQIL PATQDILKAL SKHPPVGDNK PVELLPERSS
EERPLEKISD QSESSDLDDV STPSGSDLET TSGSDLESDL ESDKEKCKEN GKMFKDKVSP
LQNLASINNK KEYSNHSVFS ASVEEQTAVS GAVNDSIKAI ASIAEKYFGS TGLVGLQDKK
VGALPYPSMF PLPFFPAFSQ SMYPFPDRDL RSLPLKMEPQ SPSEVKKLQK GSSESPFDLT
TKRKDEKPLT SVPSKPPGTP ATSQDQPLDL SMGSRSRAGG TKLTEPRKNH VFGEKKGSNV
EARSTSDGSL QHARPTPFFM DPIYRVEKRK LTDPLEALKE KYLRPSPGFL FHPQFPLPDQ
RTWMSAIENM AEKLESFSAL KPEASELLQS VPSMFSFRAP PNALPESLLR KGKERYTCRY
CGKIFPRSAN LTRHLRTHTG EQPYRCKYCD RSFSISSNLQ RHVRNIHNKE KPFKCHLCDR
CFGQQTNLDR HLKKHENGNM SGTATSSPHS ELESTGAILD DKEDAYFTEI RNFIGNSNHG
SQSPRNMDER MNGSHFKDDK TLVTSQSSDL LDDEEVEDEV LLDEEDEDND IHGKSRKELG
TTNLDEEIPE DDYEEGGALE MSCKTSPVRH ML
//
