ID M4A799_XIPMA Unreviewed; 1618 AA.
AC M4A799;
DT 01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 2.
DT 27-MAR-2024, entry version 53.
DE RecName: Full=Telomerase-binding protein EST1A {ECO:0000256|RuleBase:RU369098};
DE EC=3.1.-.- {ECO:0000256|RuleBase:RU369098};
OS Xiphophorus maculatus (Southern platyfish) (Platypoecilus maculatus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Atherinomorphae; Cyprinodontiformes; Poeciliidae; Poeciliinae;
OC Xiphophorus.
OX NCBI_TaxID=8083 {ECO:0000313|Ensembl:ENSXMAP00000010343.2, ECO:0000313|Proteomes:UP000002852};
RN [1] {ECO:0000313|Proteomes:UP000002852}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JP 163 A {ECO:0000313|Proteomes:UP000002852};
RA Walter R., Schartl M., Warren W.;
RL Submitted (JAN-2012) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000002852}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JP 163 A {ECO:0000313|Proteomes:UP000002852};
RX PubMed=23542700; DOI=10.1038/ng.2604;
RA Schartl M., Walter R.B., Shen Y., Garcia T., Catchen J., Amores A.,
RA Braasch I., Chalopin D., Volff J.N., Lesch K.P., Bisazza A., Minx P.,
RA Hillier L., Wilson R.K., Fuerstenberg S., Boore J., Searle S.,
RA Postlethwait J.H., Warren W.C.;
RT "The genome of the platyfish, Xiphophorus maculatus, provides insights into
RT evolutionary adaptation and several complex traits.";
RL Nat. Genet. 45:567-572(2013).
RN [3] {ECO:0000313|Ensembl:ENSXMAP00000010343.2}
RP IDENTIFICATION.
RC STRAIN=JP 163 A {ECO:0000313|Ensembl:ENSXMAP00000010343.2};
RG Ensembl;
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_014329305.1; XM_014473819.1.
DR STRING; 8083.ENSXMAP00000010343; -.
DR Ensembl; ENSXMAT00000010357.2; ENSXMAP00000010343.2; ENSXMAG00000010321.2.
DR GeneID; 102238347; -.
DR KEGG; xma:102238347; -.
DR CTD; 23293; -.
DR eggNOG; KOG2162; Eukaryota.
DR GeneTree; ENSGT00940000155300; -.
DR HOGENOM; CLU_004735_0_0_1; -.
DR InParanoid; M4A799; -.
DR OMA; SKSNIRH; -.
DR OrthoDB; 3094546at2759; -.
DR Proteomes; UP000002852; Unassembled WGS sequence.
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:0043009; P:chordate embryonic development; IEA:Ensembl.
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:UP000002852};
KW Telomere {ECO:0000256|RuleBase:RU369098}.
FT DOMAIN 1428..1596
FT /note="PIN"
FT /evidence="ECO:0000259|SMART:SM00670"
FT REGION 18..559
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 573..621
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 989..1050
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1334..1385
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 63..83
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 96..124
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 125..141
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 142..172
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 199..214
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 278..414
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 415..451
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 476..528
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1023..1039
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1343..1362
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1368..1383
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1618 AA; 181394 MW; C160975408467AB6 CRC64;
MANELERVRI SAAELRAETT NSLQMTDRLN EEQQERKKHK QHKRREAKRP DLQRYQPAAG
HGRCHQDSEE GETGQRDFLD AKAQHSDQSS MSGKRVSEDV LDKKGCTDLS GTKNKDEDRM
RGDGSNSLNY KQGTQSLGKI DANSENDKEQ QDASGAPKPA KKVRKPDREF YQPGSRRNVQ
GKDCSVGREL DKLSPNKQGL TLEPESQLSA GEGNSKKSIP KHRGKDKVKF SDSIEETTEQ
GRQTVDQTVE KIMSKVERLN IKEKGEVGSP SNNVGDVACT RREKESSAQG GEIKCQEEKT
DRKEKGNRRR RGGEKEKKEE IETHLESQRE EEANQSRKHN QRKLEKEKDK RAPNTDRRKS
EKPGEPHHSK RNDNPRENHK IKDNNSNFKD TEKAAKTGSH RDRVVAERDR HRSNLNATTP
NSKRYSKSNI RHSRNRTYSS SSASSVTSQD GPRRHMGMEG VKWPRLPGQN NKELGDTCEG
PRRHSSTESL DRSEVCDREE ADRRRRRRKS VGKEEISAVK RGEEWKTSNK SGGRGILRVS
LDNQSPVTKD SPVPRGRGRG ILVLPARTDI SNSPEVGQRL FSTGTRGGAA GRTRGGRGGG
VRRLWDPNNP DQKPALTNTQ TSKHAALKQP LYLQSGTGFG QLHFLDTDDE LSGSPPVAQG
DHFQSQQAAA MAYYKFQNSD NPYCYPIATN SPNSTAGQRY PHPYNMGPYQ MAHPNGMYPS
PGTSPFSGSY RGAGYSQPRV AGGLTFEEDL GRMLKAADAH ELQLSNLISR DRVSADGLDR
MSQLRADLLG LYERIILTDI EFSDSQNVDQ ALWKNVFYQV IERFRQLLKD PSCDNTHDIR
NMLLTLLDEG ALFFDALLQK LQAVYQFTLE DYMDGMAIRT RPLRKTVKYA LISAQRCMIC
QGDIARYREQ ATNSANYGKA RSWYLKAQQI APKNGRPYNQ LALLAVYTKR KLDAVCYYMR
SLAASNPILT AKESLMSLFE EAKRKAEQFE RRRRQEQEGG SQGPAVKGRR KWDDGARVEI
WIRPSGQTTT PSSQRGGSES SRDSEQDGEL GSLTATELNK RFILSFLHAH GKLFTKVGME
SFPGVASRVL QEFKTLLQHG PSLLGFTNLL QIITINMFAI YNAHSRGEEG DVRSVLLEQS
TALGLDMFAL LVQRCTELLK ETPAETVPMT DGEEEGKTEE RQGMVRVSAF PLDLRELLPS
IKVWSDWMLG HPEEWNPPPC SLECSPDVWQ CLADLCNALA RVDHEEMLLY KVDTDEGEGD
EELTVLQLKE DKLLAGFVPL LAAPQEPCYT DKHTDMAIAA DCKRVTVLKY FLEALCGQEE
PLLAFKGGKY VSVATSSSPN HSEDTRSRQD SLTEKESDDV ILEAESSLSG SEEEEDFEEA
GESENDIKEL KARRHALANK LAQQQKRRDK IQAVLQTGGQ LELEVRPLFL VPDTNCFIDH
LDRLKNLLQC GTYIIVVPLI VITELDGLAK GQEPFGGAVG TGGRSSGSRG NYNVSVAHMR
AVQEQARSAV AFLEKGFEAR EPCLRALTSR GNQLESIAFR SEDTSGQQGN NDDVILSCCL
HYCKDKAKDF MPPQRNGTVR LQREVVLLTD DRNLRVKALT RNVPVRDIPS FLSWAKVG
//
