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Database: UniProt
Entry: A0A1S2ZJV1_ERIEU
LinkDB: A0A1S2ZJV1_ERIEU
Original site: A0A1S2ZJV1_ERIEU 
ID   A0A1S2ZJV1_ERIEU        Unreviewed;      1408 AA.
AC   A0A1S2ZJV1;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   27-MAR-2024, entry version 28.
DE   RecName: Full=Telomerase-binding protein EST1A {ECO:0000256|RuleBase:RU369098};
DE            EC=3.1.-.- {ECO:0000256|RuleBase:RU369098};
GN   Name=SMG6 {ECO:0000313|RefSeq:XP_007520455.1};
OS   Erinaceus europaeus (Western European hedgehog).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Eulipotyphla; Erinaceidae; Erinaceinae;
OC   Erinaceus.
OX   NCBI_TaxID=9365 {ECO:0000313|Proteomes:UP000079721, ECO:0000313|RefSeq:XP_007520455.1};
RN   [1] {ECO:0000313|RefSeq:XP_007520455.1}
RP   IDENTIFICATION.
RG   RefSeq;
RL   Submitted (NOV-2023) to UniProtKB.
CC   -!- FUNCTION: Component of the telomerase ribonucleoprotein (RNP) complex
CC       that is essential for the replication of chromosome termini.
CC       {ECO:0000256|RuleBase:RU369098}.
CC   -!- FUNCTION: Plays a role in nonsense-mediated mRNA decay.
CC       {ECO:0000256|RuleBase:RU369098}.
CC   -!- COFACTOR:
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC         Evidence={ECO:0000256|RuleBase:RU369098};
CC   -!- SUBCELLULAR LOCATION: Nucleus, nucleolus
CC       {ECO:0000256|RuleBase:RU369098}. Chromosome, telomere
CC       {ECO:0000256|RuleBase:RU369098}. Cytoplasm, cytosol
CC       {ECO:0000256|RuleBase:RU369098}.
CC   -!- DOMAIN: The PINc domain confers endonuclease activity and is expected
CC       to bind the catalytic metal ion. {ECO:0000256|RuleBase:RU369098}.
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DR   RefSeq; XP_007520455.1; XM_007520393.2.
DR   STRING; 9365.ENSEEUP00000003215; -.
DR   GeneID; 103111141; -.
DR   CTD; 23293; -.
DR   eggNOG; KOG2162; Eukaryota.
DR   InParanoid; A0A1S2ZJV1; -.
DR   OrthoDB; 3094546at2759; -.
DR   Proteomes; UP000079721; Unplaced.
DR   GO; GO:0000781; C:chromosome, telomeric region; IEA:UniProtKB-SubCell.
DR   GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR   GO; GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell.
DR   GO; GO:0004519; F:endonuclease activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0030145; F:manganese ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0000184; P:nuclear-transcribed mRNA catabolic process, nonsense-mediated decay; IEA:UniProtKB-KW.
DR   CDD; cd09885; PIN_Smg6-like; 1.
DR   Gene3D; 3.40.50.1010; 5'-nuclease; 1.
DR   Gene3D; 1.25.40.10; Tetratricopeptide repeat domain; 1.
DR   InterPro; IPR018834; DNA/RNA-bd_Est1-type.
DR   InterPro; IPR019458; Est1-like_N.
DR   InterPro; IPR045153; Est1/Ebs1-like.
DR   InterPro; IPR029060; PIN-like_dom_sf.
DR   InterPro; IPR002716; PIN_dom.
DR   InterPro; IPR011990; TPR-like_helical_dom_sf.
DR   PANTHER; PTHR15696; SMG-7 SUPPRESSOR WITH MORPHOLOGICAL EFFECT ON GENITALIA PROTEIN 7; 1.
DR   PANTHER; PTHR15696:SF40; TELOMERASE-BINDING PROTEIN EST1A; 1.
DR   Pfam; PF10374; EST1; 1.
DR   Pfam; PF10373; EST1_DNA_bind; 1.
DR   Pfam; PF13638; PIN_4; 1.
DR   SMART; SM00670; PINc; 1.
DR   SUPFAM; SSF88723; PIN domain-like; 1.
DR   SUPFAM; SSF48452; TPR-like; 1.
PE   4: Predicted;
KW   Chromosome {ECO:0000256|RuleBase:RU369098};
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|RuleBase:RU369098};
KW   Endonuclease {ECO:0000256|RuleBase:RU369098};
KW   Hydrolase {ECO:0000256|RuleBase:RU369098};
KW   Manganese {ECO:0000256|RuleBase:RU369098};
KW   Metal-binding {ECO:0000256|RuleBase:RU369098};
KW   Nonsense-mediated mRNA decay {ECO:0000256|ARBA:ARBA00023161,
KW   ECO:0000256|RuleBase:RU369098}; Nuclease {ECO:0000256|RuleBase:RU369098};
KW   Nucleus {ECO:0000256|ARBA:ARBA00023242, ECO:0000256|RuleBase:RU369098};
KW   Reference proteome {ECO:0000313|Proteomes:UP000079721};
KW   Telomere {ECO:0000256|RuleBase:RU369098}.
FT   DOMAIN          1235..1386
FT                   /note="PIN"
FT                   /evidence="ECO:0000259|SMART:SM00670"
FT   REGION          21..47
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          173..387
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          408..459
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          806..832
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          850..872
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        31..47
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        173..223
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        248..265
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        267..334
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        353..370
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        371..387
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1408 AA;  159507 MW;  B5673A626DC444B9 CRC64;
     MAEGLERVRI SASELRGILA TLAPQAGSRE NMKEPRQRKD NRRPDLEIYK PGLSRLRNKV
     KIKEPSGIDE YKDEIVNDRD SSVGNGVQLI KDVCKELDNQ NCPADPENVR VQESFPRTAG
     QEDKSLRIIK RAKKPDMQIY QPGRRLHTLS KELTNQADEE EIINQVEQLR VEDECRGNGK
     EEAVNKPDRE VADKSPCGDR VRVPKGERGK RVEKGEGMKK MNDDAAQGKP GSAKRYSRSD
     KRRNRYRTCS TSSAGSNNSA EGTGLTDNGC RRRRQDRTKD RPRLKKQVSM SSTDSLDEDR
     IDEVDGPRSS ERKKHLERNC SGRGEGEQKS NGKENRGNLR VTFDAETMSK DSPAVRSTRE
     DMDRLKSDKS SSSGGKGSEK QGSKNLKQEL QGRGRGILIL PAHTTLSVNS ASSPESTPLG
     PRLLFGSGSK GSRSWGRGGT TRRLWDPNNP DQKPALKSQT PQLHFLDTDD EVSPTSWGDS
     RQAQASYYKF QNSDNPYYYP RTPGPASQYP YPGYSPLQYP VGPTNGVYPG PYYPGYPTPS
     GQYVCSPLPA STMSPEELEQ HMRNMQQQEL HRLLRVADNQ ELQLSNLLSR DRISPEGLEK
     MAQLRAELLQ LYERCILLDI EFSDNQNVDQ ILWKNAFYQV IEKFRQLLKD PNVENPEQIR
     NRLLELLDEG SDFFDSLLQK LQVTYKFKLE DYMDGLAIRS KPLRKTVKYA LISAQRCMIC
     QGDIARYREQ ANDTANYGKA RSWYLKAQHI APKNGRPYNQ LALLAVYTRR KLDAVYYYMR
     SLAASNPILT AKESLMSLFE ETKRKAEQME KKQQEESELS SDQWRKGKKS TFQHVGEDTT
     RLEIWIHPSH SRSCQGTESG KDSEQENGLG SLSPNDLNKR FILSFLHAHG KLFTRIGMET
     FPAVAEKVLK EFQVLLQHSP SPIGSTRMLQ LMTINMFAVH NSQLKDCFSE ECRSVIQEQA
     AALGLAMFSL LVRRCTYLLK ESAKAQLSSP EDEDDQDDIK VSSFVPDLKE LLPSVKVWSD
     WMLGYPDTWN PPPTSLDLPS QVAVDVWSML ADFCNILTAV NQSEVPLYKD PDDDLTLLIL
     EEDRLLSGFV PLLAAPQDPC YVEKTSDKVI AADCKRVTVL KYFLEALCGQ EEPLLAFKGG
     KYVSVAPVPD TMGKEMGSQE GKQLEDEEED VVIEDFEEDS EAEGSVAEDD IRELRAKKLA
     LARKIAEQQR RQEKIQAVLE DQSQMRQMEL EIRPLFLVPD TNGFIDHLAS LARLLESRKY
     ILVVPLIVIN ELDGLAKGQE TDHRAGGYAR VVQEKARKSI EFLERRFESR DSCLRALTSR
     GNELESIAFR SEDITGQLGN NDDLILSCCL HYCKDKAKDF MPTNKEEPIR LLREVVLLTD
     DRNLRVKALT RNVPVRDIPA FLTWAQVG
//
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