ID A0A151NZC1_ALLMI Unreviewed; 492 AA.
AC A0A151NZC1;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE SubName: Full=Histone-lysine N-methyltransferase 2D-like {ECO:0000313|EMBL:KYO41939.1};
GN ORFNames=Y1Q_0003629 {ECO:0000313|EMBL:KYO41939.1};
OS Alligator mississippiensis (American alligator).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Crocodylia; Alligatoridae; Alligatorinae;
OC Alligator.
OX NCBI_TaxID=8496 {ECO:0000313|EMBL:KYO41939.1};
RN [1] {ECO:0000313|EMBL:KYO41939.1, ECO:0000313|Proteomes:UP000050525}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KSC_2009_1 {ECO:0000313|EMBL:KYO41939.1};
RX PubMed=22293439; DOI=10.1186/gb-2012-13-1-415;
RA St John J.A., Braun E.L., Isberg S.R., Miles L.G., Chong A.Y., Gongora J.,
RA Dalzell P., Moran C., Bed'hom B., Abzhanov A., Burgess S.C., Cooksey A.M.,
RA Castoe T.A., Crawford N.G., Densmore L.D., Drew J.C., Edwards S.V.,
RA Faircloth B.C., Fujita M.K., Greenwold M.J., Hoffmann F.G., Howard J.M.,
RA Iguchi T., Janes D.E., Khan S.Y., Kohno S., de Koning A.J., Lance S.L.,
RA McCarthy F.M., McCormack J.E., Merchant M.E., Peterson D.G., Pollock D.D.,
RA Pourmand N., Raney B.J., Roessler K.A., Sanford J.R., Sawyer R.H.,
RA Schmidt C.J., Triplett E.W., Tuberville T.D., Venegas-Anaya M.,
RA Howard J.T., Jarvis E.D., Guillette L.J.Jr., Glenn T.C., Green R.E.,
RA Ray D.A.;
RT "Sequencing three crocodilian genomes to illuminate the evolution of
RT archosaurs and amniotes.";
RL Genome Biol. 13:415-415(2012).
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KYO41939.1}.
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 EMBL; AKHW03001491; KYO41939.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A151NZC1; -.
DR STRING; 8496.A0A151NZC1; -.
DR Proteomes; UP000050525; Unassembled WGS sequence.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0008168; F:methyltransferase activity; IEA:UniProtKB-KW.
DR GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR CDD; cd15509; PHD1_KMT2C_like; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 2.
DR InterPro; IPR034732; EPHD.
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; PTHR45888:SF2; HISTONE-LYSINE N-METHYLTRANSFERASE 2D; 1.
DR PANTHER; PTHR45888; HL01030P-RELATED; 1.
DR Pfam; PF00628; PHD; 2.
DR Pfam; PF13771; zf-HC5HC2H; 1.
DR SMART; SM00249; PHD; 3.
DR SUPFAM; SSF57903; FYVE/PHD zinc finger; 2.
DR PROSITE; PS51805; EPHD; 1.
DR PROSITE; PS50016; ZF_PHD_2; 2.
PE 4: Predicted;
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Methyltransferase {ECO:0000313|EMBL:KYO41939.1};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000050525};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transferase {ECO:0000313|EMBL:KYO41939.1};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00146}.
FT DOMAIN 108..213
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS51805"
FT DOMAIN 221..271
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS50016"
FT DOMAIN 268..318
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS50016"
FT REGION 1..58
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 85..106
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 352..492
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 377..402
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 412..433
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 455..469
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 492 AA; 52962 MW; 6FCB7F13524B3035 CRC64;
MDEQKPPSED KDSEAPADGA ASSEEQGSAE GDPLKPPEVV PATREPGSTE TKRPPQPCST
LPWRCALCNC GDWSRLGQRE LQRFEPGPNW TEQPQGQEGP GEVPAAEDDL SQIGFTEGVT
LRQISEPTGH CWVHHWCAAW SAGVQRQDGA GLNDVDKAVF SGISQKCERC QRMGATLQCH
SEGCPRRYHF PCAAASGSFQ SMKTLRLLCP EHLAEAAQME DSRCVVCDGP GELRDLLFCT
SCGLHYHGAC LEITVTPRKR AGWQCPECKV CQTCRQPGED SMMLVCEACD KGYHTFCMKP
AIESLPTDSW KCKNCRVCSD CGRRPAALNP ACQWYENYSV CEGCQEQRRR STEGSQAGEA
EAPPCDQHSP LPMACIDSAG PPVPPSPAGH DPPVPSPLPQ ARSPAAEPQD KLPAADEAKP
PDPDSKAEEP EEPPALAPEV PAKEEAMEVE LEPLPPTATP APSPPAPPGE GQAHQGRGLC
TRLPQGMLGP TL
//
