PRD10_XENTR
ID PRD10_XENTR Reviewed; 1173 AA.
AC B4F6U4;
DT 10-FEB-2009, integrated into UniProtKB/Swiss-Prot.
DT 23-SEP-2008, sequence version 1.
DT 03-AUG-2022, entry version 65.
DE RecName: Full=PR domain zinc finger protein 10;
DE EC=2.1.1.-;
DE AltName: Full=PR domain-containing protein 10;
GN Name=prdm10;
OS Xenopus tropicalis (Western clawed frog) (Silurana tropicalis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Silurana.
OX NCBI_TaxID=8364;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Testis;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (JUL-2008) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: May be involved in transcriptional regulation. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC -!- DOMAIN: The SET domain is degenerated, suggesting that it has lost
CC methyltransferase activity.
CC -!- SIMILARITY: Belongs to the class V-like SAM-binding methyltransferase
CC superfamily. {ECO:0000255|PROSITE-ProRule:PRU00190}.
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DR EMBL; BC168013; AAI68013.1; -; mRNA.
DR RefSeq; NP_001135541.1; NM_001142069.1.
DR AlphaFoldDB; B4F6U4; -.
DR SMR; B4F6U4; -.
DR STRING; 8364.ENSXETP00000062917; -.
DR PaxDb; B4F6U4; -.
DR PRIDE; B4F6U4; -.
DR GeneID; 100216084; -.
DR KEGG; xtr:100216084; -.
DR CTD; 56980; -.
DR Xenbase; XB-GENE-985864; prdm10.
DR eggNOG; KOG1721; Eukaryota.
DR InParanoid; B4F6U4; -.
DR OrthoDB; 1318335at2759; -.
DR Proteomes; UP000008143; Chromosome 7.
DR Proteomes; UP000790000; Unplaced.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
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 GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0010468; P:regulation of gene expression; IBA:GO_Central.
DR CDD; cd19194; PR-SET_PRDM10; 1.
DR Gene3D; 2.170.270.10; -; 1.
DR InterPro; IPR044403; PRDM10_PR/SET.
DR InterPro; IPR001214; SET_dom.
DR InterPro; IPR046341; SET_dom_sf.
DR InterPro; IPR036236; Znf_C2H2_sf.
DR InterPro; IPR013087; Znf_C2H2_type.
DR Pfam; PF00096; zf-C2H2; 3.
DR SMART; SM00355; ZnF_C2H2; 10.
DR SUPFAM; SSF57667; SSF57667; 3.
DR PROSITE; PS50280; SET; 1.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 10.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 10.
PE 2: Evidence at transcript level;
KW DNA-binding; Metal-binding; Methyltransferase; Nucleus; Reference proteome;
KW Repeat; S-adenosyl-L-methionine; Transcription; Transcription regulation;
KW Transferase; Zinc; Zinc-finger.
FT CHAIN 1..1173
FT /note="PR domain zinc finger protein 10"
FT /id="PRO_0000363966"
FT DOMAIN 248..366
FT /note="SET"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00190"
FT ZN_FING 395..417
FT /note="C2H2-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 559..581
FT /note="C2H2-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 589..611
FT /note="C2H2-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 617..639
FT /note="C2H2-type 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 645..668
FT /note="C2H2-type 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 673..695
FT /note="C2H2-type 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 701..724
FT /note="C2H2-type 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 756..779
FT /note="C2H2-type 8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 801..824
FT /note="C2H2-type 9"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 863..886
FT /note="C2H2-type 10"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT REGION 146..211
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 430..451
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1014..1056
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1125..1173
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 153..167
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 172..200
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 430..444
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1130..1173
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1173 AA; 132140 MW; 03B08ECC73CD1BE3 CRC64;
MDTKEGSPHV WPTSVEHQSN TAQVHFVPDG GSVAQIVYSD DQDRAQQQVV YTADASSFTS
VDASEHTLVY IHPVDGSQTL FTDQPQVAYV QQDATTQQVT VLLPAAQSMN AANLAVLSGV
SESAQTMSLD PVSQINRASL TVHDHRLPPM EGADSSTTIN SLPSPNAHSD GKEDDDDDDD
DDDDEEEEDD DGEDSDLDDW EAEPPRPFDP NDLWCEECNN AHPSVCPKHG ALHPIPNRPV
LTRARASLPL VLYIDRFLGG VYSKRRIPKR TQFGPLEGPL VKKTELKDSY IHLKVALNSP
VDSEGAFQED LWFELSEESL CNWMMFVRPA QNHLEQNLVA YQYGQHIYFT TIKNIEPKQE
LKVWYAASYA EFVNEKIHDI TQEERKVLRE QEKNWPCYEC NRRFMSSEQL QQHLNSHDEK
LDFISRTKPR GRTRTRRKFG PGRRPGRPPK FLRFDISSEN REKIDLGTQD LLQFHNKGPH
FEDCGHSTLN GLEQSELTLG TSTQGTPNQQ QATQLLPPNE ISTPVATTSI LTAEDMRRAK
RIRNAALQHL FIRKSFRPFK CLQCGKAFRE KEKLDQHLRF HGRDGNYPLT CDICNKGFIS
TSSLENHMKF HLDQKTYSCI FCPESFDRLD LLKDHVVVHI IDGCFSCPTC KKRFTDFIQV
KKHVRSFHSE KIYQCTECDK AFCRPDKLRL HMLRHSDRKD FLCSTCGKQF KRKDKLREHM
QRMHNPEREA KKADRTGRAK AFKPRLASTD YESFMFKCRV CMMGFRRRGM LVNHLSKRHP
EMKIDEVPEL TLPIIKPNRD YYCQYCEKVY KSASKRKAHI LKNHPGAELP PSIRKLRPAG
PGEPDPMLST HTQLTGTIAT PPVCCPHCSK QYSSKTKMVQ HIRKKHPEFS LLPISVQAPV
LGTAPAVLTA DGTSGETVVT TDLLTQAMTE LSQTLTTEYR TPQGDFQRIQ YIPVSQTTGG
MQQPQHIQLQ VVQVAQAQSP NQSQHSTVDM GQLHESQGYM QHAIQVQHIQ VAEPTSGTQS
TPQVGGQALS PSSQEAEEVN PSQLQTPASQ AQANSAVQHA YLPSGWNSFR GYPSEIQMMA
LPQGQYVIAE AAVGTPVTPV SSGQVKAVTQ THYVISEGQG VLDMKKSSSL AEEATPNPDH
MEQPASNSSQ TTQYIITTTT NMNGSSEVHI SKP
