ID A0A6I9HE44_GEOFO Unreviewed; 1312 AA.
AC A0A6I9HE44;
DT 07-OCT-2020, integrated into UniProtKB/TrEMBL.
DT 07-OCT-2020, sequence version 1.
DT 18-JUN-2025, entry version 24.
DE SubName: Full=DNA repair protein RAD50 {ECO:0000313|RefSeq:XP_005418732.1};
GN Name=RAD50 {ECO:0000313|RefSeq:XP_005418732.1};
OS Geospiza fortis (Medium ground-finch).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Neoaves; Telluraves; Australaves;
OC Passeriformes; Thraupidae; Geospiza.
OX NCBI_TaxID=48883 {ECO:0000313|Proteomes:UP000504602, ECO:0000313|RefSeq:XP_005418732.1};
RN [1] {ECO:0000313|RefSeq:XP_005418732.1}
RP IDENTIFICATION.
RG RefSeq;
RL Submitted (MAR-2025) to UniProtKB.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O = ADP + phosphate + H(+); Xref=Rhea:RHEA:13065,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:456216;
CC Evidence={ECO:0000256|ARBA:ARBA00049360};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|ARBA:ARBA00001947};
CC -!- SUBCELLULAR LOCATION: Chromosome, telomere
CC {ECO:0000256|ARBA:ARBA00004574}. Nucleus
CC {ECO:0000256|ARBA:ARBA00004123}.
CC -!- SIMILARITY: Belongs to the SMC family. RAD50 subfamily.
CC {ECO:0000256|ARBA:ARBA00009439}.
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DR RefSeq; XP_005418732.1; XM_005418675.2.
DR Ensembl; ENSGFOT00000001894; ENSGFOP00000001862; ENSGFOG00000001305.
DR GeneID; 102037092; -.
DR KEGG; gfr:102037092; -.
DR CTD; 10111; -.
DR InParanoid; A0A6I9HE44; -.
DR OrthoDB; 18797at2759; -.
DR Proteomes; UP000504602; Unplaced.
DR GO; GO:0070533; C:BRCA1-C complex; IEA:Ensembl.
DR GO; GO:0000781; C:chromosome, telomeric region; IEA:UniProtKB-SubCell.
DR GO; GO:0000794; C:condensed nuclear chromosome; IEA:TreeGrafter.
DR GO; GO:0030870; C:Mre11 complex; IEA:Ensembl.
DR GO; GO:0035861; C:site of double-strand break; IEA:Ensembl.
DR GO; GO:0008408; F:3'-5' exonuclease activity; IEA:Ensembl.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:Ensembl.
DR GO; GO:0003678; F:DNA helicase activity; IEA:Ensembl.
DR GO; GO:0003691; F:double-stranded telomeric DNA binding; IEA:TreeGrafter.
DR GO; GO:0051880; F:G-quadruplex DNA binding; IEA:TreeGrafter.
DR GO; GO:0042802; F:identical protein binding; IEA:Ensembl.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0043539; F:protein serine/threonine kinase activator activity; IEA:Ensembl.
DR GO; GO:0030674; F:protein-macromolecule adaptor activity; IEA:Ensembl.
DR GO; GO:0000014; F:single-stranded DNA endodeoxyribonuclease activity; IEA:Ensembl.
DR GO; GO:0043047; F:single-stranded telomeric DNA binding; IEA:TreeGrafter.
DR GO; GO:0070192; P:chromosome organization involved in meiotic cell cycle; IEA:TreeGrafter.
DR GO; GO:0000729; P:DNA double-strand break processing; IEA:Ensembl.
DR GO; GO:0110025; P:DNA strand resection involved in replication fork processing; IEA:Ensembl.
DR GO; GO:0000724; P:double-strand break repair via homologous recombination; IEA:Ensembl.
DR GO; GO:1904354; P:negative regulation of telomere capping; IEA:Ensembl.
DR GO; GO:2000781; P:positive regulation of double-strand break repair; IEA:Ensembl.
DR GO; GO:0032206; P:positive regulation of telomere maintenance; IEA:Ensembl.
DR GO; GO:0062176; P:R-loop processing; IEA:Ensembl.
DR GO; GO:0000019; P:regulation of mitotic recombination; IEA:Ensembl.
DR GO; GO:0000722; P:telomere maintenance via recombination; IEA:TreeGrafter.
DR GO; GO:0007004; P:telomere maintenance via telomerase; IEA:Ensembl.
DR GO; GO:0031860; P:telomeric 3' overhang formation; IEA:Ensembl.
DR FunFam; 3.40.50.300:FF:001037; DNA repair protein RAD50; 1.
DR FunFam; 3.40.50.300:FF:001065; DNA repair protein RAD50 isoform X1; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR038729; Rad50/SbcC_AAA.
DR InterPro; IPR004584; Rad50_eukaryotes.
DR InterPro; IPR013134; Zn_hook_RAD50.
DR NCBIfam; TIGR00606; rad50; 1.
DR PANTHER; PTHR18867:SF12; DNA REPAIR PROTEIN RAD50; 1.
DR PANTHER; PTHR18867; RAD50; 1.
DR Pfam; PF13476; AAA_23; 1.
DR Pfam; PF04423; Rad50_zn_hook; 1.
DR Pfam; PF13558; SbcC_Walker_B; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF75712; Rad50 coiled-coil Zn hook; 1.
DR SUPFAM; SSF46966; Spectrin repeat; 1.
DR PROSITE; PS51131; ZN_HOOK; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Chromosome {ECO:0000256|ARBA:ARBA00022454};
KW Coiled coil {ECO:0000256|ARBA:ARBA00023054, ECO:0000256|SAM:Coils};
KW DNA damage {ECO:0000256|ARBA:ARBA00022763};
KW DNA repair {ECO:0000256|ARBA:ARBA00023204};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Meiosis {ECO:0000256|ARBA:ARBA00023254};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|PROSITE-
KW ProRule:PRU00471}; Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000504602};
KW Telomere {ECO:0000256|ARBA:ARBA00022895};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|PROSITE-ProRule:PRU00471}.
FT DOMAIN 635..734
FT /note="Zinc-hook"
FT /evidence="ECO:0000259|PROSITE:PS51131"
FT COILED 203..233
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 265..349
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 450..607
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 635..662
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 712..822
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 853..1070
FT /evidence="ECO:0000256|SAM:Coils"
FT BINDING 681
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00471"
FT BINDING 684
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00471"
SQ SEQUENCE 1312 AA; 153426 MW; 35CFB95B6E9DBA6A CRC64;
MSRIEKMSIL GVRSFGIEDK DKQIITFFNP LTILVGPNGA GKTTIIECLK YISTGDFPPG
TKGKTFVHDP KIANETDVRA QIRLQFRDVN GEVMAVQRSM VCTQKSKEPE FKTLESVITR
TKHGEKVSLS SKCAEIDREM INALGVSKAV LNNVIFCHQE ESNWPLSEGK ALKQKFDEIF
SATRYIKALE ALRQVRLKQS LKVKECQTEL KYLKQNKEKA QEIQDHLSNR EAQLAASKEN
VISIENQLEP LKNSLAVVEQ NLTKVMRLDN DVKALESRKR QMEKDNQDLQ QKMEKVFQGT
DEQLRDRYQN HQRIVKEKEK RLLDCKRDLD RATKECQRFN SEKSELLIER GRLQLQADRH
QEHIVTRDSL VQSLAAQLEL DGFERAPFTD RHIASFHRLV KDRQDRDTEA ANRMMREFAQ
KETMKQKQID EIRDKKTGLE RTIDLKSDIQ NKKQAELKNV KRELQQLEGF SDRISELDEE
IGKMEHDLET AERNSNIETL EQEVQTLQNE KINLDKALRR LDQEMEQLNL HTTTITQLEM
LKKDKAEKED QIRKVKSRHS EELTSLLGYF PNKKQLEDWL HGKNKKINQT RDTLANLNKR
LSSVEYDKTY ASNELKKKEA QLSSHEAKLF DVCGSQDFDS DLNKLQDEIE KSSKQRAVLA
GATAVYSQFI TQLTEENQSC CPVCQRVFQT EAELQDVISD LQSKLRLAPD KLKSTESELK
RKEKKRDEMM SLKPLRQTVV ELQDKEIPDL RNKIQNANRD LTGLKGEIEE QESLLQTALS
EEEGAKARLQ DITLMERYQT DIRDVERKIA QQEAKLLCVN LNRTVLQVSR EKQEKKQLWD
TVTSKIELNQ KHKQDQQSQI QQLKSAVNEL KAEKLQIVSS MQRRRQLEEQ TVELTTEVQS
LCREIKEAEE QILPLEAKLD KLQHEKEELV NKRTASNKET QEKMNNINEK VKDINKYVKE
IENYIQQGKE DYKKQKESEL EEVNSRLAAC EKQKEKISKE MEMTRQDIDT QKIQERWLED
NLTLRKRNEE LKEVEDNIKK LMKEMGEMKV PQMKNEQKHL EEKIESLKRN HHVALGRQRG
FEEEIVRFRK ELREPQFRDA EEKYRDMMIV MRTTELVNKD LDLYYKALDK AIMTFHSMKM
EEINKIIRDL WRSIYRGQDI EYIEIRSDAD ENVSATDKRR NYNYRVVMVK GDTALDMRGR
CSAGQKVLAS LIIRLALAET FCINCGILAL DEPTTNLDRE NIESLAHALV EIIKSRLHQR
NFQLLVITHD EDFVELLGRS EYVETFYRIK KNIDQCSEIM KCSVSSLGSY VH
//