ID A0A2Y9DMC1_TRIMA Unreviewed; 1475 AA.
AC A0A2Y9DMC1;
DT 12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT 12-SEP-2018, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE SubName: Full=PR domain zinc finger protein 2 isoform X3 {ECO:0000313|RefSeq:XP_004377287.1};
GN Name=LOC101359888 {ECO:0000313|RefSeq:XP_004377287.1};
OS Trichechus manatus latirostris (Florida manatee).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Afrotheria; Sirenia; Trichechidae; Trichechus.
OX NCBI_TaxID=127582 {ECO:0000313|Proteomes:UP000248480, ECO:0000313|RefSeq:XP_004377287.1};
RN [1] {ECO:0000313|RefSeq:XP_004377287.1}
RP IDENTIFICATION.
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
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DR RefSeq; XP_004377287.1; XM_004377230.3.
DR GeneID; 101359888; -.
DR KEGG; tmu:101359888; -.
DR OrthoDB; 5399106at2759; -.
DR Proteomes; UP000248480; Unplaced.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-KW.
DR GO; GO:0042054; F:histone methyltransferase activity; IEA:InterPro.
DR Gene3D; 3.30.160.60; Classic Zinc Finger; 3.
DR InterPro; IPR009170; PRDM2.
DR InterPro; IPR036236; Znf_C2H2_sf.
DR InterPro; IPR013087; Znf_C2H2_type.
DR PANTHER; PTHR16515; PR DOMAIN ZINC FINGER PROTEIN; 1.
DR PANTHER; PTHR16515:SF37; PR DOMAIN ZINC FINGER PROTEIN 2; 1.
DR Pfam; PF00096; zf-C2H2; 2.
DR Pfam; PF13912; zf-C2H2_6; 2.
DR PIRSF; PIRSF002395; RIZ_SET; 1.
DR SMART; SM00355; ZnF_C2H2; 8.
DR SUPFAM; SSF57667; beta-beta-alpha zinc fingers; 2.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 6.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 7.
PE 4: Predicted;
KW Metal-binding {ECO:0000256|PROSITE-ProRule:PRU00042};
KW Reference proteome {ECO:0000313|Proteomes:UP000248480};
KW Zinc {ECO:0000256|PROSITE-ProRule:PRU00042};
KW Zinc-finger {ECO:0000256|PROSITE-ProRule:PRU00042}.
FT DOMAIN 151..173
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS50157"
FT DOMAIN 181..203
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS50157"
FT DOMAIN 274..297
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS50157"
FT DOMAIN 928..955
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS50157"
FT DOMAIN 956..979
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS50157"
FT DOMAIN 985..1008
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS50157"
FT DOMAIN 1249..1276
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS50157"
FT REGION 1..101
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 196..246
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 301..342
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 406..454
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 497..585
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 701..878
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1023..1060
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1273..1368
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1417..1475
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..18
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 62..89
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 211..246
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 420..434
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 517..543
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 566..580
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 726..758
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 759..800
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 801..878
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1337..1368
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1454..1475
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CROSSLNK 443
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000256|PIRSR:PIRSR002395-1"
FT CROSSLNK 567
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000256|PIRSR:PIRSR002395-1"
SQ SEQUENCE 1475 AA; 161904 MW; D54D945E87B1CA88 CRC64;
MRDSAEGPKE EEEKPSASAA EQTDVLQEVV SQDVLPELAV PSAVCEPQTE PDEKVEATNC
EVNDLEDEEE EEDDDEDDEL EEEGEEEADM PNESSVKEPE IRCDEKLEDL LEEPKHISRE
SLEDSPEVTP VIRIPKTKGE PNGDVFETFM FPCQHCERKF TTKQGLERHM HIHISTVNHA
FKCKYCGKAF GTQINRRRHE RRHETGLKRK PSLTLQPSED LTDGKVSGDN VTPQDESNPP
NLGQNSLILN SEKASQEAVN STVVEENGEV KELHPCKYCK KVFGTHTNMR RHQRRVHERH
LIPKGVRRKG GLLEEPQPPA EQAQPTQNVY VPSTEPEEEG EADDVYIMDI SSNISENLNY
YIDGKIQTNS STSNCDVIEM ESNSADLYGI NCLLTPVTVE ITQNIQTTPV PVTDDLPKEP
SSSTNRESKK RRTTSPPLLP KIKAETDSDP VAPSCSVSLP LSISATEAVS FHKEKSVYLS
SKLKQLLQTQ EKLTSPAGIS ATEMPKLGPP PVSAPASMLP VSSSRFKRRT SSPPSSPQHS
PALRDFGKQS DGKAVWTEPV LSSKKPKMES HSNSPAWSLS GRDERETVSP PCFDEYKISK
EWAASSTFSN VCNQQPLDLS SGVKQKAEGV GKTPVQWESV LDLSVHKKPC SDSEGKEFKE
NHLVPPACSA VKKKKPTTCM LQKVLLNEYN GIDLPVENAA DVTRSPSPCK SLEPQPDPDL
GPHSSLSAPT VESPPDVSPS SPALQTSSLS SGQLPPLLIP TNPSSPPRCP PVLTVATPPP
PLLPTIPLPL PAPSSDASPH PCPSPLSNAA AQSPLPVLSP TVSPSPSPIH SVEPLTSAAS
PGPPTLSSSS SSSSSSSSFS SSSSSSSPSP PPLSAVSSVV SSGDNLEVSL PMISFKQEEL
ENEDLKPREE PQSSVEQDVV QETFNKNFVC NVCESPFLSI KDLTKHLSIH AEEWPFKCEF
CVQLFKDKTD LSEHRFMLHG VGNIFVCSVC KKEFAFLCNL QQHQRDLHPD KVCTHHEFET
GTLRPQNFTD PSKAHAEHMQ SLPEDPSETS KEEEELNDSS EELYTTIKIM ASGVKTKDPD
VRLGLNQHYP SFKPPPFQYH HRNPMGIGVT ATNFTTHNIP QTFTTAIRCT KCGKGVDNMP
ELHKHILACA SASDKKRYTP KKNPVPLKQT VQPKNGVVVL DNSGKNAFRR MGQPKRLNFS
VELSKMSSNK LKLNALKRKN QLVQKAILQK NKAAKQKADL KNASESSSHI CPYCNREFTY
IGSLNKHAAF SCPQKPLSPS KKKVSHSSKK GGHSSPASSD KNSNGNHRRR TADAEIKMQS
TPAPLGKTRA RSSGPAPVPL PSSSFRSKQN VKFGTSVKSK KPNSSLRNSS PIRMAKITHV
EGKKPKAMAK NHPAQLASKA SRNLHVRVQK SKAVLQSKAT LASKRRTDRF NMKSRERSGG
PITRSLQLAA ATDVGENRRE DSSAKQELKD FRNFL
//
