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Database: UniProt
Entry: A0A2Y9D5R0_TRIMA
LinkDB: A0A2Y9D5R0_TRIMA
Original site: A0A2Y9D5R0_TRIMA 
ID   A0A2Y9D5R0_TRIMA        Unreviewed;       778 AA.
AC   A0A2Y9D5R0;
DT   12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT   12-SEP-2018, sequence version 1.
DT   24-JAN-2024, entry version 23.
DE   SubName: Full=Retrotransposon-derived protein PEG10 isoform 1 {ECO:0000313|RefSeq:NP_001278031.1};
GN   Name=PEG10 {ECO:0000313|RefSeq:NP_001278031.1};
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:NP_001278031.1};
RN   [1] {ECO:0000313|RefSeq:NP_001278031.1}
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=17942406; DOI=10.1074/jbc.M705676200;
RA   Clark M.B., Janicke M., Gottesbuhren U., Kleffmann T., Legge M.,
RA   Poole E.S., Tate W.P.;
RT   "Mammalian gene PEG10 expresses two reading frames by high efficiency -1
RT   frameshifting in embryonic-associated tissues.";
RL   J. Biol. Chem. 282:37359-37369(2007).
RN   [2] {ECO:0000313|RefSeq:NP_001278031.1}
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=20084274;
RA   Lux H., Flammann H., Hafner M., Lux A.;
RT   "Genetic and molecular analyses of PEG10 reveal new aspects of genomic
RT   organization, transcription and translation.";
RL   PLoS ONE 5:e8686-e8686(2010).
RN   [3] {ECO:0000313|RefSeq:NP_001278031.1}
RP   IDENTIFICATION.
RG   RefSeq;
RL   Submitted (SEP-2023) to UniProtKB.
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DR   RefSeq; NP_001278031.1; NM_001291102.1.
DR   AlphaFoldDB; A0A2Y9D5R0; -.
DR   STRING; 127582.A0A2Y9D5R0; -.
DR   GeneID; 101361553; -.
DR   KEGG; tmu:101361553; -.
DR   CTD; 23089; -.
DR   InParanoid; A0A2Y9D5R0; -.
DR   OrthoDB; 1469084at2759; -.
DR   Proteomes; UP000248480; Unplaced.
DR   GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   CDD; cd00303; retropepsin_like; 1.
DR   Gene3D; 3.30.70.270; -; 1.
DR   Gene3D; 2.40.70.10; Acid Proteases; 1.
DR   Gene3D; 3.10.10.10; HIV Type 1 Reverse Transcriptase, subunit A, domain 1; 1.
DR   InterPro; IPR043502; DNA/RNA_pol_sf.
DR   InterPro; IPR032549; DUF4939.
DR   InterPro; IPR032567; LDOC1-rel.
DR   InterPro; IPR021109; Peptidase_aspartic_dom_sf.
DR   InterPro; IPR043128; Rev_trsase/Diguanyl_cyclase.
DR   InterPro; IPR001878; Znf_CCHC.
DR   InterPro; IPR036875; Znf_CCHC_sf.
DR   PANTHER; PTHR15503; LDOC1 RELATED; 1.
DR   PANTHER; PTHR15503:SF31; RETROTRANSPOSON-DERIVED PROTEIN PEG10; 1.
DR   Pfam; PF16297; DUF4939; 1.
DR   SUPFAM; SSF50630; Acid proteases; 1.
DR   SUPFAM; SSF56672; DNA/RNA polymerases; 1.
DR   SUPFAM; SSF57756; Retrovirus zinc finger-like domains; 1.
DR   PROSITE; PS50158; ZF_CCHC; 1.
PE   4: Predicted;
KW   Metal-binding {ECO:0000256|PROSITE-ProRule:PRU00047};
KW   Reference proteome {ECO:0000313|Proteomes:UP000248480};
KW   Zinc {ECO:0000256|PROSITE-ProRule:PRU00047};
KW   Zinc-finger {ECO:0000256|PROSITE-ProRule:PRU00047}.
FT   DOMAIN          371..385
FT                   /note="CCHC-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50158"
FT   REGION          1..91
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          112..133
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          321..352
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          388..417
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        21..37
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        38..60
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        61..75
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        76..91
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   778 AA;  87289 MW;  64D5C69251B0C621 CRC64;
     MRNKRLLKTR RRKGGRSGQD PGPQSHHSEA TPGRSPPTPT LNLGPDCPPP PPPPPPNHPS
     SSSSKHSGQK GQYNANLSER KRDDLSEEIN SLREKVMKQS EENNNLQNQV QKLTEENTSL
     REQVEPAPQA EEDDLELCGA AAAAAPPPPC EEECPDDLPE KFDGNPDMLA PFMAQCQLFM
     EKSTRDFSVD RVRVCFVTSM MTGRAARWAS AKLEQSNYLM HNYPAFMIEM KHVFEDPQRR
     EAAKRKIRRL RQGMGSVIDY SNAFQMIAQD LDWNEPALID QYHEGLSDHI QEELSRLEVA
     KSLPALIGQC IHIERRLARA AAARKPRSPP RALMLPHSSG HHQVDPTEPV GGARMRLTQE
     EKERRRKLNL CLYCGTGGHY ADSCPAKASK ASPAGKLPGP AVEGPSATGP ERIRSPRDEI
     STPHLQVMLQ IHLPGRHTLF VRAMIDSGAS GNFIDHEYVA QNGIPLRVKD WPILVEAIDG
     RPIASGPVVH ETHDLIVDLG DHREVLSFDV TQSPFFPIVL GVRWLSIHDP NITWSTRSIV
     FDSEYCRYHC RMYSPLPPSP PPAPQPSIYY PVDGYRVYQP VRYYYVQNVY TPVDENVYPD
     NHVADCSVDM IPGAHSIPSG HIYSLSEPEM AALRDFVARN VKDGLITPTI APNGAQVLQV
     KRGWKLQVSY DCRAPNNFTI QNQYPRLSIP NLDDQAHLAS YVEYVPQVPA YQAYPTYATY
     PTYPVGFAWY PVGRDGHGRS LYVPVMITWN PHWYRQPPVP QYPPPPPPPP PPPSYSTM
//
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