ID A0A093R5B6_PYGAD Unreviewed; 1312 AA.
AC A0A093R5B6;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE SubName: Full=DNA repair protein RAD50 {ECO:0000313|EMBL:KFW66199.1};
GN ORFNames=AS28_08216 {ECO:0000313|EMBL:KFW66199.1};
OS Pygoscelis adeliae (Adelie penguin).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Sphenisciformes; Spheniscidae; Pygoscelis.
OX NCBI_TaxID=9238 {ECO:0000313|EMBL:KFW66199.1, ECO:0000313|Proteomes:UP000054081};
RN [1] {ECO:0000313|EMBL:KFW66199.1, ECO:0000313|Proteomes:UP000054081}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGI_AS28 {ECO:0000313|EMBL:KFW66199.1};
RA Zhang G., Li C.;
RT "Genome evolution of avian class.";
RL Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
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}.
CC -!- SIMILARITY: Belongs to the SMC family. RAD50 subfamily.
CC {ECO:0000256|ARBA:ARBA00009439}.
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DR EMBL; KL224978; KFW66199.1; -; Genomic_DNA.
DR RefSeq; XP_009321006.1; XM_009322731.1.
DR STRING; 9238.A0A093R5B6; -.
DR GeneID; 103915802; -.
DR KEGG; padl:103915802; -.
DR CTD; 10111; -.
DR OrthoDB; 5477220at2759; -.
DR Proteomes; UP000054081; Unassembled WGS sequence.
DR GO; GO:0000781; C:chromosome, telomeric region; IEA:UniProtKB-SubCell.
DR GO; GO:0030870; C:Mre11 complex; IEA:InterPro.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0006302; P:double-strand break repair; IEA:InterPro.
DR GO; GO:0051321; P:meiotic cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0000723; P:telomere maintenance; IEA:InterPro.
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 PROSITE; PS51131; ZN_HOOK; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Chromosome {ECO:0000256|ARBA:ARBA00022895};
KW Coiled coil {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 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 Reference proteome {ECO:0000313|Proteomes:UP000054081};
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..349
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 467..607
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 712..815
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 846..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; 153067 MW; D0E2BEB3D38E6651 CRC64;
MSKIEKMSIL GVRSFGVEDK DKQIITFFNP LTILVGPNGA GKTTIIECLK YISTGDFPPG
TKGNSFVHDP KVANETDVRA QIRLQFRDVN GELVAVQRSM VCTQKGKKME FKTLEGVITR
TKHGEKVSLS SKCAEIDREM ISALGVSKSV INNVIFCHQE ESNWPLSEGK ALKQKFDEIF
SATRYIKALE TLRQVRLKQS VKVKECQTEL KYLKQNKEKA QEIQDHLTKR EAQLAASKEN
VKSIESQLDP LKTSLAAVEQ NLIKVMRLDN DVKALESRTR QMEKDNQDLQ QKMEKVFQGT
DEQLKDIYQN HQRTVKEKEK RLSDCKRELD RAAKECQRFT SEKSELLVER GRLQLQADRH
QEHITMRDSL IQSLAAQLEL DGFERAPFNE RHITSFHRLL KERQERDTEA ANHLMREFAR
KEAMKQKQID EIRDKKTGLE RTIDLKSDIQ SKKQVELKNV RYELQQLEGF SDRILELDQE
IVKTEHELEK AEKNSNVETL ELEVQTLQKE KINLDTALRK LDQEMEQLNL HTMTITQMEM
LKKDKADKEE QIRKVKSRHS DELTSLLGYF PNKNQLEDWL HLKNRKINQT RDNLADLNKR
LASVEYHKTY VSNELRKKEA QLSLHEAKLF DVCGSQDFDS DLSKLQDEIE KSSKQRAVLA
GATAVYSQFI TQLTEENQSC CPVCQRVFQT EAELQDVISD LQSKLRLAPD KLKSTESELK
RKEKKRDEMM SLKPLRRTVV ELQDRDIPDL RSKIQNANRD LTGLKSEIEE QESVLRTALS
KEESAKARLQ DITLMERYQT DIRDGERKIA QQEAKLLGVD LSRTVLQVSQ EKQEKKHLWD
TVTGKIELNQ KLKQDQQNQI QQLKSAVNEL KAEKLQISSS MQRRRQLEEQ TVELTTEVQS
LCRDIEEAKE QVFPLDATLE KLQQEKEDLM NKRTASNKET QEKINGIKEK VKDINKYVKE
IENYIQEGRE DYKKQKESEL EDVNSQLAAC EKQKEMISKE MEMIRQDIDT QKVQERWLED
NLTLRKRNEE LKEVENNIKN LVKEMGEMKV PQMKNEQKHL EEKIESLKRN HHVALGRQRG
FEEEIVRFKK ELRESQFKDA EEKYREMMIV MRTTELVNKD LDLYYKALDK AIMTFHSMKM
EEINKIIRDL WRSTYRGQDI EYIEIRSDAD ENVSASDKRR SYNYRVVMIK GDIALDMRGR
CSAGQKVLAS LIIRLALAET FCLNCGILAL DEPTTNLDRE NIESLAHALV EIIKSRSQQR
NFQLLVITHD EDFVELLGRS EYVETFYRIK KNIDQCSEIM KCSVSSLGSY VH
//
