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RTEL1_PONAB
ID   RTEL1_PONAB             Reviewed;        1302 AA.
AC   Q5RE34;
DT   05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT   21-DEC-2004, sequence version 1.
DT   03-AUG-2022, entry version 75.
DE   RecName: Full=Regulator of telomere elongation helicase 1 {ECO:0000255|HAMAP-Rule:MF_03065};
DE            EC=3.6.4.12 {ECO:0000255|HAMAP-Rule:MF_03065};
GN   Name=RTEL1 {ECO:0000255|HAMAP-Rule:MF_03065};
OS   Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Pongo.
OX   NCBI_TaxID=9601;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain cortex;
RG   The German cDNA consortium;
RL   Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: ATP-dependent DNA helicase implicated in telomere-length
CC       regulation, DNA repair and the maintenance of genomic stability. Acts
CC       as an anti-recombinase to counteract toxic recombination and limit
CC       crossover during meiosis. Regulates meiotic recombination and crossover
CC       homeostasis by physically dissociating strand invasion events and
CC       thereby promotes noncrossover repair by meiotic synthesis dependent
CC       strand annealing (SDSA) as well as disassembly of D loop recombination
CC       intermediates. Also disassembles T loops and prevents telomere
CC       fragility by counteracting telomeric G4-DNA structures, which together
CC       ensure the dynamics and stability of the telomere. {ECO:0000255|HAMAP-
CC       Rule:MF_03065}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.12;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_03065};
CC   -!- SUBUNIT: Interacts with TERF1. Interacts (via PIP-box) with PCNA; the
CC       interaction is direct and essential for suppressing telomere fragility.
CC       Interacts with MMS19; the interaction mediates the association of RTEL1
CC       with the cytosolic iron-sulfur protein assembly (CIA) complex.
CC       {ECO:0000255|HAMAP-Rule:MF_03065}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|HAMAP-Rule:MF_03065}.
CC       Note=Colocalizes with PCNA within the replication foci in S-phase
CC       cells. {ECO:0000255|HAMAP-Rule:MF_03065}.
CC   -!- DOMAIN: The PIP-box (PCNA interacting peptide) motif mediates the
CC       interaction with PCNA and localization to replication foci.
CC       {ECO:0000255|HAMAP-Rule:MF_03065}.
CC   -!- SIMILARITY: Belongs to the helicase family. RAD3/XPD subfamily.
CC       {ECO:0000255|HAMAP-Rule:MF_03065}.
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DR   EMBL; CR857704; CAH89973.1; -; mRNA.
DR   RefSeq; NP_001124929.1; NM_001131457.1.
DR   AlphaFoldDB; Q5RE34; -.
DR   SMR; Q5RE34; -.
DR   GeneID; 100171800; -.
DR   KEGG; pon:100171800; -.
DR   CTD; 51750; -.
DR   eggNOG; KOG1132; Eukaryota.
DR   InParanoid; Q5RE34; -.
DR   OrthoDB; 186062at2759; -.
DR   Proteomes; UP000001595; Unplaced.
DR   GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR   GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0005524; F:ATP binding; ISS:UniProtKB.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:RHEA.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0003678; F:DNA helicase activity; ISS:UniProtKB.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0006310; P:DNA recombination; IEA:InterPro.
DR   GO; GO:0006281; P:DNA repair; IEA:UniProtKB-UniRule.
DR   GO; GO:0006260; P:DNA replication; IEA:InterPro.
DR   GO; GO:0010569; P:regulation of double-strand break repair via homologous recombination; ISS:UniProtKB.
DR   GO; GO:0000723; P:telomere maintenance; ISS:UniProtKB.
DR   Gene3D; 3.40.50.300; -; 2.
DR   HAMAP; MF_03065; RTEL1; 1.
DR   InterPro; IPR006555; ATP-dep_Helicase_C.
DR   InterPro; IPR010614; DEAD_2.
DR   InterPro; IPR045028; DinG/Rad3-like.
DR   InterPro; IPR014013; Helic_SF1/SF2_ATP-bd_DinG/Rad3.
DR   InterPro; IPR006554; Helicase-like_DEXD_c2.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR013020; Rad3/Chl1-like.
DR   InterPro; IPR030845; RTEL1.
DR   PANTHER; PTHR11472; PTHR11472; 2.
DR   Pfam; PF06733; DEAD_2; 1.
DR   Pfam; PF13307; Helicase_C_2; 1.
DR   SMART; SM00488; DEXDc2; 1.
DR   SMART; SM00491; HELICc2; 1.
DR   SUPFAM; SSF52540; SSF52540; 2.
DR   TIGRFAMs; TIGR00604; rad3; 1.
DR   PROSITE; PS51193; HELICASE_ATP_BIND_2; 1.
PE   2: Evidence at transcript level;
KW   4Fe-4S; ATP-binding; DNA damage; DNA repair; DNA-binding; Helicase;
KW   Hydrolase; Iron; Iron-sulfur; Metal-binding; Nucleotide-binding; Nucleus;
KW   Reference proteome.
FT   CHAIN           1..1302
FT                   /note="Regulator of telomere elongation helicase 1"
FT                   /id="PRO_0000370612"
FT   DOMAIN          7..297
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03065"
FT   REGION          758..819
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          981..1006
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1019..1058
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1134..1153
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1160..1234
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           152..168
FT                   /note="Nuclear localization signal"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03065"
FT   MOTIF           251..254
FT                   /note="DEAH box"
FT   MOTIF           873..879
FT                   /note="Nuclear localization signal"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03065"
FT   MOTIF           1180..1187
FT                   /note="PIP-box"
FT   COMPBIAS        1173..1188
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         42..49
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03065"
FT   BINDING         146
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03065"
FT   BINDING         164
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03065"
FT   BINDING         173
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03065"
FT   BINDING         208
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03065"
SQ   SEQUENCE   1302 AA;  142673 MW;  05591DABC80FAE4A CRC64;
     MPKIVLNGVT VDFPFQPYKC QQEYMTKVLE CLQQKVNGIL ESHTGTGKTL CLLCTTLAWR
     EHLRDGISAR KIAERVQGEL FPDRALSSWG NAAAAAAGDP IACYTDIPKI IYASRTHSQL
     TQVINELRNT SYRPKVCVLG SREQLCIHPE VKKQESNHIQ IHLCRKKVAS RSCHFYNNVE
     EKSLEQELAS PILDIEDLVK SGSKHRVCPY YLSRNLKQQA DIIFMPYNYL LDAKSRRAHN
     IDLKGTVVIF DEAHNVEKMC EESASFDLTP HDLASGLDII DQVLEEQTKT AQQGEPHPEF
     SADSTSPGLN MELEDIAKLK MILLRLEGAI DAVELPGDDS GVTKPGSYIF ELFAEAQITF
     QTKVCILDSL DQIIQHLAGR AGVFTNTAGL QKLADIIQIV FSVDPSEGGP GSLAGLGALQ
     SYKVHIHPDA GHRQTAQRSD AWSTTAARKR GKVLSYWCFS PGLSMRELVR QGVRSLILTS
     GTLAPVSSFA LEMQIPFPVC LENPHIIDKH QIWVGVVPRG PDGAQLSSAF DRRFSEECLS
     SLGKALGNTA RVVPCGLLIF FPSYPVMEKS LEFWRARDLA RKMEALKPLF VEPRSKGSFS
     ETISAYYARV AAPGSTGATF LAVCRGKASE GLDFSDTNGR GVIVTGLPYP PRMDPRVVLK
     MQFLDEMKGQ GGAGGQFLSG QEWYRQQASR AVNQAIGRVI RHRQDYGAVF LCDHRFAFAD
     ARAQLPSWVR PHVRVYDNFG HVIRDVAQFF RVAERTMPAP APRATAPSVR EGEDAVREVK
     SPGPLFSTRK AKSLDLHVPS LKQRSSGSAA AGDPESSLCV EYEQEPIPAR QRPRGLLAAL
     EHSEQQAGSP GEEQAHSCST LFLLSAKRPA EEPRGGRKKI RLVSHPEEPV AGAQTDRAKL
     YMVAVKQELS QANFATFTQA LQDYKGSDDF AALAACLGPL FAEDPKKHSL LQGFYQFVRP
     HHKQQFEEVC IQLTGRGCGY RPEHSIPRRQ PAQPVLDPTG RTAPDPKLTL SKAAAQQLDP
     REHLNQGRPH LSPRPPPTGD PGSHPQWRSG VPRAGKQGQR AVSAYLADAR RALGSAGCSQ
     LLAALRAYKQ DDDLDKVLAV LAALTTAKPE DFPLLHRFSM FVRPHHKQRF SQTCTDLTGR
     PYPGMERPGP QEESLVVPPV LTHGAPQPGP SRSEKPGKTQ SKISSLLRQR PAGTVGAGSE
     DAGPSQSPGP PHGPAASEWG EPHGRDIAGQ QAAGAPGGPL SAGCVCQGCG AEDVVPFQCP
     ACDFQRCQAC WQRHLQASRM CPACHTASRK QSVTQVFWPE PQ
 
 
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