ID A0A371HWJ6_MUCPR Unreviewed; 1363 AA.
AC A0A371HWJ6;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE SubName: Full=DNA repair protein RAD50 {ECO:0000313|EMBL:RDY07171.1};
GN Name=RAD50 {ECO:0000313|EMBL:RDY07171.1};
GN ORFNames=CR513_08755 {ECO:0000313|EMBL:RDY07171.1};
OS Mucuna pruriens (Velvet bean) (Dolichos pruriens).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC NPAAA clade; indigoferoid/millettioid clade; Phaseoleae; Mucuna.
OX NCBI_TaxID=157652 {ECO:0000313|EMBL:RDY07171.1, ECO:0000313|Proteomes:UP000257109};
RN [1] {ECO:0000313|EMBL:RDY07171.1, ECO:0000313|Proteomes:UP000257109}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Jos {ECO:0000313|Proteomes:UP000257109};
RC TISSUE=Seed {ECO:0000313|EMBL:RDY07171.1};
RA Nnadi N.E., Vos R., Hasami M.H., Devisetty U.K., Aguiy J.C.;
RT "Draft genome of Mucuna pruriens seed.";
RL Submitted (MAY-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|ARBA:ARBA00001947};
CC -!- SIMILARITY: Belongs to the SMC family. RAD50 subfamily.
CC {ECO:0000256|ARBA:ARBA00009439}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:RDY07171.1}.
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DR EMBL; QJKJ01001532; RDY07171.1; -; Genomic_DNA.
DR STRING; 157652.A0A371HWJ6; -.
DR Proteomes; UP000257109; Unassembled WGS sequence.
DR GO; GO:0005634; C:nucleus; IEA:UniProt.
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:0006996; P:organelle organization; IEA:UniProt.
DR Gene3D; 1.10.287.1490; -; 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; IPR013134; Zn_hook_RAD50.
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 SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR PROSITE; PS51131; ZN_HOOK; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
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 Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|PROSITE-ProRule:PRU00471}.
FT DOMAIN 695..794
FT /note="Zinc-hook"
FT /evidence="ECO:0000259|PROSITE:PS51131"
FT COILED 267..389
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 585..694
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 800..1018
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 1085..1132
FT /evidence="ECO:0000256|SAM:Coils"
FT BINDING 742
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00471"
FT BINDING 745
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00471"
SQ SEQUENCE 1363 AA; 157344 MW; 47D4AF655EF2FE34 CRC64;
MSTVDKMLIK GIRSFDPENK NVITFFKPLT LIVGPNGAGK TTIIECLKLS CTGELPPNAR
SGHSFIHDPK VAGETETKGQ IKLRFKTAAG KDVVCVRSFQ LTQKASKMEY KAIESVLQTI
NPHTGEVATS LFSSSLSSSS INSLLLCHYL QKVCLSYRCA DMDREIPALM GVSKAILENV
IFVHQDEANW PLQDPSTLKK KFDDIFSATR YTKALEVIKK LHKEQAQEIK TYKLKLENLQ
TLKDAAYKLR ESIAQDEEKT ESVKCQVQQL DGNIKELDDK IHHTEKILKD LRKLQEQIST
KTAQRSTLFK EQQKQYAALA EENEDTDEEL MEWKTKFEER IAILETKISK LEREINDTDT
KSSFLKRTID DSIREIAKLQ AEAEAHMSLK NERDTSIHNL FATYNLGSLP KTPFSAEVAL
NLTNRVKSRL ADLEKDLGDK KVPVVGDKLR SGRIFKDLLV FFVKANDNEL KMALDCYMNA
NDCWKDTEAK KTAMTGIKSG ILKRIEEKKN ELDSFELQIS NVNFSHIDER ERNLGNEVER
KASQLAERQF DPNIRQVQNE IYSVDQTIKA VNREKDIMAS DSEDRVKLSL KKAELENQKK
KHKKIIDDQK DKIRKVLKGR VPLDKDVKKE ITQALRAVGA EFDDLNAKYR EAEKEVNMLQ
MKIQEVNSNI SKHHKDLESR KRFVESKLQS LDQQCSGIDS YLKVLESAKE KRDVHRSKYN
IADGMRQMFD PFERVARAHH FCPCCERPFS PEEEDNFVKK QRVKAASSAE HMKVLAVESS
NTESHYQQLD KLRMVYEDYV KLGKETIPNA EKELQQLKEE MDDKSQALDD VLGVLAQVKT
EKDLVESLVQ PVENADRLFQ EIQALQKQIE DLEYKLDFRG QGVRTLEEIQ LELNTFQSTK
DNLQSELERL SDERRHMEND LSNIQIRWHT LREEKVKATN ILQGVKKLEE ELERLTEEKT
QVDLEEKHLA EALGPLSKEK DKLLADHNEL KVRLNHEYED LAEQKRSYQQ EAEALFKMNS
KIKEYSDLKK GDRLKELQEK KSLSESQIRS CDSRKQEILT ELNKSKDLMR DQDQLKRNIE
DNLNYRKTKA EVDELALEIE TLEENILKAG GISTVETELQ KLAQERERLL SELNRCHGTM
SVYQSNISKN KVDLKLAQYK DIDKRYFNQL IQLKTTEMAN KDLDRYYNAL DKALMRFHTM
KMEEINKIIR ELWQQTYRGQ DIDYISIHSD SEGAGTRSYS YKVLMQTGDA ELEMRGRCSA
GQKVLASLII RLALAETFCL NCGILALDEP TTNLDGPNAE SLAAALVRIM EDRKGQENFQ
LIVITHDERF AQLIGQRQHA ERYYRVTKDD HQHSIIESQE IFD
//