GenomeNet

Database: UniProt
Entry: Q5RAX9
LinkDB: Q5RAX9
Original site: Q5RAX9 
ID   PRD10_PONAB             Reviewed;        1117 AA.
AC   Q5RAX9;
DT   10-FEB-2009, integrated into UniProtKB/Swiss-Prot.
DT   21-DEC-2004, sequence version 1.
DT   16-JAN-2019, entry version 80.
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   Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Hominidae; Pongo.
OX   NCBI_TaxID=9601;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Kidney;
RG   The German cDNA consortium;
RL   Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: May be involved in transcriptional regulation.
CC       {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
CC       methyltransferase superfamily. {ECO:0000255|PROSITE-
CC       ProRule:PRU00190}.
DR   EMBL; CR858882; CAH91081.1; -; mRNA.
DR   RefSeq; NP_001125628.1; NM_001132156.1.
DR   UniGene; Pab.13712; -.
DR   ProteinModelPortal; Q5RAX9; -.
DR   STRING; 9601.ENSPPYP00000004643; -.
DR   GeneID; 100172546; -.
DR   KEGG; pon:100172546; -.
DR   CTD; 56980; -.
DR   eggNOG; KOG1721; Eukaryota.
DR   eggNOG; COG5048; LUCA.
DR   HOGENOM; HOG000168283; -.
DR   HOVERGEN; HBG053664; -.
DR   InParanoid; Q5RAX9; -.
DR   OrthoDB; 1318335at2759; -.
DR   Proteomes; UP000001595; Unplaced.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
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   InterPro; IPR001214; SET_dom.
DR   InterPro; IPR022755; Znf_C2H2_jaz.
DR   InterPro; IPR036236; Znf_C2H2_sf.
DR   InterPro; IPR013087; Znf_C2H2_type.
DR   Pfam; PF00096; zf-C2H2; 3.
DR   Pfam; PF12171; zf-C2H2_jaz; 1.
DR   SMART; SM00355; ZnF_C2H2; 10.
DR   SUPFAM; SSF57667; SSF57667; 4.
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   Complete proteome; DNA-binding; Isopeptide bond; Metal-binding;
KW   Methyltransferase; Nucleus; Phosphoprotein; Reference proteome;
KW   Repeat; S-adenosyl-L-methionine; Transcription;
KW   Transcription regulation; Transferase; Ubl conjugation; Zinc;
KW   Zinc-finger.
FT   CHAIN         1   1117       PR domain zinc finger protein 10.
FT                                /FTId=PRO_0000363964.
FT   DOMAIN      182    300       SET. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00190}.
FT   ZN_FING     329    351       C2H2-type 1. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00042}.
FT   ZN_FING     500    522       C2H2-type 2. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00042}.
FT   ZN_FING     530    552       C2H2-type 3. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00042}.
FT   ZN_FING     558    580       C2H2-type 4. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00042}.
FT   ZN_FING     586    609       C2H2-type 5. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00042}.
FT   ZN_FING     614    636       C2H2-type 6. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00042}.
FT   ZN_FING     642    665       C2H2-type 7. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00042}.
FT   ZN_FING     697    720       C2H2-type 8. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00042}.
FT   ZN_FING     742    765       C2H2-type 9. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00042}.
FT   ZN_FING     804    827       C2H2-type 10. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00042}.
FT   COMPBIAS    836    886       Thr-rich.
FT   COMPBIAS    888   1001       Gln-rich.
FT   COMPBIAS   1101   1104       Poly-Thr.
FT   MOD_RES     398    398       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:Q9NQV6}.
FT   MOD_RES     402    402       Phosphothreonine.
FT                                {ECO:0000250|UniProtKB:Q9NQV6}.
FT   CROSSLNK    354    354       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in SUMO2).
FT                                {ECO:0000250|UniProtKB:Q9NQV6}.
SQ   SEQUENCE   1117 AA;  126746 MW;  C84E0E1B4E1835F0 CRC64;
     MDSKDESSHV WPTSAEHEQN AAQVHFVPDT GTVAQIVYTD DQVRPPQQVV YTADGASYTS
     VDGPEHTLVY IHPVEAAQTL FTDPGQVAYV QQDATAQQTP LGGLEAKEEE DEDEDEDTEE
     DEEEDGEDAD LDDWEPDPPR PFDPHDLWCE ECNNAHSSVC PKHGPLHPIP NRPVLTRARA
     SLPLVLYIDR FLGGVFSKRR IPKRTQLGPV EGPLVRGSEL KDCYIHLKVS LDKGDRKDRD
     LHEDLWFELS DETLCNWMMF VRPAQNHLEQ NLVAYQYGHH VYYTTIKNVE PKQELKVWYA
     ASYAEFVNQK IHDISEEERK VLREQEKNWP CYECNRRFIS SEQLQQHLNS HDEKLDVFSR
     TRGRGRGRGK RRFGPGRRPG RPPKFIRLEI TSENGEKSDD GTQDLLHFPT KEQFDEAEPA
     TLNGLDQPEQ TTIPIPQLPQ ETQSSLEHEP ETHTLHLQPQ HEESVVPTQS TLTADDMRRA
     KRIRNAALQH LFIRKSFRPF KCLQCGKAFR EKDKLDQHLR FHGREGNCPL TCDLCNKGFI
     SSASLESHMK LHSDQKTYSC IFCPESFDRL DLLKDHVAIH INDGYFTCPT CKKRFPDFIQ
     VKKHVRSFHS EKIYQCTECD KAFCRPDKLR LHMLRHSDRK DFLCSTCGKQ FKRKDKLREH
     MQRMHNPERE AKKADRISRS KTFKPRITST DYDSFTFKCR LCMMGFRRRG MLVNHLSKRH
     PDMKIEEVPE LTLPIIKPNR DYFCQYCDKV YKSASKRKAH ILKNHPGAEL PPSIRKLRPA
     GPGEPDPMLS THTQLTGTIA TPPVCCPHCS KQYSSKTKMV QHIRKKHPEF AQLSSTIHTP
     LTTAVISATP AVLTTDSATG ETVVTTDLLT QAMTELSQTL TTDYRTPQGD YQRIQYIPVS
     QSASGLQQPQ HIQLQVVQVA PATSPHQSQQ STVDVGQLHD PQPYPQHAIQ VQHIQVSGQP
     LSPSAQQAQQ GLSPSHIQGS SSTQGQALQQ QQQQQQNSSV QHTYLPSAWN SFRGYSSEIQ
     MMTLPPGQFV ITDSGVATPV TTGQVKAVTS GHYVLSESQS DLEEKQTSAL SGGVQVQPPA
     HSDSLDPQTT SQQQTTQYII TTTTNGNGSS EVHITKP
//
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