ID   W2ZMI7_PHYPR            Unreviewed;      1341 AA.
AC   W2ZMI7;
DT   19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT   19-MAR-2014, sequence version 1.
DT   27-MAR-2024, entry version 35.
DE   RecName: Full=Rad50/SbcC-type AAA domain-containing protein {ECO:0000259|Pfam:PF13476};
GN   ORFNames=F442_05769 {ECO:0000313|EMBL:ETP48513.1};
OS   Phytophthora parasitica P10297.
OC   Eukaryota; Sar; Stramenopiles; Oomycota; Peronosporales; Peronosporaceae;
OC   Phytophthora.
OX   NCBI_TaxID=1317064 {ECO:0000313|EMBL:ETP48513.1, ECO:0000313|Proteomes:UP000018948};
RN   [1] {ECO:0000313|EMBL:ETP48513.1, ECO:0000313|Proteomes:UP000018948}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=P10297 {ECO:0000313|EMBL:ETP48513.1,
RC   ECO:0000313|Proteomes:UP000018948};
RG   The Broad Institute Genomics Platform;
RA   Russ C., Tyler B., Panabieres F., Shan W., Tripathy S., Grunwald N.,
RA   Machado M., Johnson C.S., Walker B., Young S.K., Zeng Q., Gargeya S.,
RA   Fitzgerald M., Haas B., Abouelleil A., Allen A.W., Alvarado L.,
RA   Arachchi H.M., Berlin A.M., Chapman S.B., Gainer-Dewar J., Goldberg J.,
RA   Griggs A., Gujja S., Hansen M., Howarth C., Imamovic A., Ireland A.,
RA   Larimer J., McCowan C., Murphy C., Pearson M., Poon T.W., Priest M.,
RA   Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J., Nusbaum C.,
RA   Birren B.;
RT   "The Genome Sequence of Phytophthora parasitica P10297.";
RL   Submitted (NOV-2013) 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:ETP48513.1}.
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DR   EMBL; ANIY01001225; ETP48513.1; -; Genomic_DNA.
DR   EnsemblProtists; ETP48513; ETP48513; F442_05769.
DR   Proteomes; UP000018948; Unassembled WGS sequence.
DR   GO; GO:0030870; C:Mre11 complex; IEA:InterPro.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0006302; P:double-strand break repair; IEA:InterPro.
DR   GO; GO:0000723; P:telomere maintenance; IEA:InterPro.
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; IPR004584; Rad50_eukaryotes.
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   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
PE   3: Inferred from homology;
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Meiosis {ECO:0000256|ARBA:ARBA00023254};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000018948};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT   DOMAIN          6..240
FT                   /note="Rad50/SbcC-type AAA"
FT                   /evidence="ECO:0000259|Pfam:PF13476"
FT   REGION          600..619
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          940..959
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          213..278
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          308..370
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          421..497
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          621..686
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   1341 AA;  155095 MW;  5D7722DF60E8B59A CRC64;
     MSSIEKLSIR GIRSFSPNRE EIIEFYHPLT ILLGDNGCGK TTVIECLKLA CTGGLPPGAR
     SGQSLIHDPK IAGTNEVKAS IRLRFRNRAG KAMLVHRTYQ VRQTKKTMNF KALDGVIRVV
     NELGEKVSLS HKCGELDQHI PDMLGVSKAI LESVIFCHQE ESNWPLREGA ELKKRFDNIF
     ESARYTKALE AIRKLKKARL ENAKDYKRDL DVLTTHMKMA EEIRDKIERL QEKLEEITEQ
     GEGAKEKIDK AKETLRELQQ LQEEVKNFHL QLERRQEDVV MKEQSVRTAY SKIENIMSDT
     DDELRGFLND YDAIIEDHRR AFTRLQEQDE KLQKEQHKAK EDYVTLRDNK ARVETNIDTY
     QKKVADLIDS ASKLSTKYRF HLQPLSSQQE DISTFLAEFR NVVKDKQEAV NKLDVKQRQD
     DDALTTELSE LTSQVKRLRD DLRTKTQSLE ALNRDKKVIA DRLRELGGAG LHSQRDAEEM
     SSQVSEAERA LEDYRAKHNV MALRDEIQGF NRQMSDINHV IEDLGQQISQ LRIYARRNAE
     IEFQRSEYRK KQEIFQASLH EKVADIEEIF EGGEKPTDRS SLVSALRNID DLIAERKHSL
     DTKRREQASA EQRLMENTTS SKLAEKELNS LRSKKNQLDR QHMTGLKELL DKVIPGHDLK
     NAELGVKEAE RAYADAKDKV VRRKNMVMFL NIYKKKGLKD HCCPLCERDM SPEEEQAFES
     ILSDKTDDGK VADKIKKAED LEKSSLQTLT QIKEKMPSWR KWLELETAIP EKVTELEEIY
     AAQKALEVDV QDKKAVFDLA QEQFDAAKTA KSDMEILRKS ADELHYSDVA ITKEEERMRG
     SQGSNGCSLS DVEAEKDAKQ AEVQELNHQL QRKQKELDHI NEMLQQLQNE IHSRKEEKLR
     IETQRKEYDE AIKEQNRLRE QEKSLKEACA KLKKSEPELE REVRAKTTQR ETRRAEAREQ
     LRAQRSELQE RQGDFRVFSD KCKQVQHGEL DRLEREVQTI SDNIAQTKQR EDRVVQALAD
     LAPQMKSAEK NLSENEIVKR RIQDNLDYRE LQKELAKMRA EVEDLKNHIG NLPSLDDVND
     RVEAADAALT SAQRSAAMMV GKRQQLMEEI REQKIKLRVP TLKDVEEKYR HKLIQFETTQ
     MAVTDLDRYF KALDESLLQY HSKKVDEINT IIRSLWQITY KGQDIDTIEL VSGQQEGQVS
     KAARSYDYRV VMKKAGAAID MRGRCSAGQK VLAALVIRLA LAETFCLNCG ILALDEPTTN
     LDTENKFGLA QAITDILNAR SQQQNFQLVC ITHDEEFVQM LSRTQAMEGT RPEFYWRILR
     EDIGGNRFVS KIERREWEDG I
//