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
//