ID   A0A0G2J1R2_9EURO        Unreviewed;      1331 AA.
AC   A0A0G2J1R2;
DT   22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT   22-JUL-2015, sequence version 1.
DT   27-MAR-2024, entry version 38.
DE   SubName: Full=DNA repair protein RAD50 {ECO:0000313|EMBL:KKZ63449.1};
GN   ORFNames=EMCG_02260 {ECO:0000313|EMBL:KKZ63449.1};
OS   Emmonsia crescens UAMH 3008.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Onygenales; Ajellomycetaceae; Emmonsia.
OX   NCBI_TaxID=1247875 {ECO:0000313|EMBL:KKZ63449.1, ECO:0000313|Proteomes:UP000034164};
RN   [1] {ECO:0000313|Proteomes:UP000034164}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=UAMH 3008 {ECO:0000313|Proteomes:UP000034164};
RX   PubMed=26439490; DOI=10.1371/journal.pgen.1005493;
RA   Munoz J.F., Gauthier G.M., Desjardins C.A., Gallo J.E., Holder J.,
RA   Sullivan T.D., Marty A.J., Carmen J.C., Chen Z., Ding L., Gujja S.,
RA   Magrini V., Misas E., Mitreva M., Priest M., Saif S., Whiston E.A.,
RA   Young S., Zeng Q., Goldman W.E., Mardis E.R., Taylor J.W., McEwen J.G.,
RA   Clay O.K., Klein B.S., Cuomo C.A.;
RT   "The dynamic genome and transcriptome of the human fungal pathogen
RT   Blastomyces and close relative Emmonsia.";
RL   PLoS Genet. 11:E1005493-E1005493(2015).
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:KKZ63449.1}.
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DR   EMBL; LCZI01000983; KKZ63449.1; -; Genomic_DNA.
DR   VEuPathDB; FungiDB:EMCG_02260; -.
DR   Proteomes; UP000034164; 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   Pfam; PF13558; SbcC_Walker_B; 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   Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT   DOMAIN          27..254
FT                   /note="Rad50/SbcC-type AAA"
FT                   /evidence="ECO:0000259|Pfam:PF13476"
FT   REGION          1068..1097
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          225..273
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          375..466
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          491..575
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          601..653
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          719..789
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          814..1012
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        1068..1086
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1331 AA;  153253 MW;  212245F39C46B415 CRC64;
     MSYSGVSSST GDLSSYVANS CQAKIDKLSI LGVRSFDNTR SETIQFHTPL TLIVGYNGSG
     KTTIIECLKY ATTGDLPPNS KGGAFIHDPK LCGEKEVLAQ VKLSFKSMSG ARMVATRSLQ
     LTVKKTTRQQ KTLEGQLLMV KDGERTSISS RVAELDQIMP QYLGVSKAVL DSVIFCHQDE
     SLWPMSEPSV LKKKFDEIFE ALKYTKAIDN IKALRKKQNE ELSKFKIMEQ HCKENKDKAD
     RAEKRSIKLQ EEIEALRAES HELSQQMRRA AELADKAWKE SESYARILGI LEGKRIEAKS
     IQSSIDNLQQ HLVEIDESDE WLERTLEQFE SQQAHYREQE ESLKEKYMDL KQVIEDNRTR
     LGLKQAEYGK HENDKAQFER QLRRREKLIK EIARQNNIRG FDDDLDDMQV NDFMQRIRKL
     SKDLNQALER TRREAQMELR EGQNLLNQLS QRKSALQEVK NAARKQISSN DIEADSYQRR
     LNEIDIDEGT KAVLESRIEE TERSLHEAKE KAKAASWDNT IQSKTAEIRL LEDESSKLNA
     ELIEGTKRAG DLARLDHLKK ELKDRERSLE TMKGAHSDRI KKFLTQEWNP STLDQEYQTA
     LQETTNALTR VERDRDGVSR ELEHAEFKLK TTRKDLQQRR NELKQCVQKI RDVVDDEPAE
     YPDILKQRQV QLDMAKKDAD QYAGLGEYLS KCMDAARQKK VCRMCSRPFK TEGEFQVFLN
     KLDALVKRAT QDAEDESMQQ LEEDLEAAQS VSTFYDTWVR LSSTEIPALE KEESQLESQR
     ENLLSQIEDH DKIVSERAES KKNVESLSKT VATISKYHSE ITTLRSQIED LSANQQDVSG
     SRTLEDIQEQ ISAIGLKYRE LQKVISKLNN DKDQSRTEIT TLELKLRDVR SNLDNANYQL
     EKKASYAARV EEYRNLNAKE RERIEKADQD IESLVPEVSK AQARYDDISS RAEARERELQ
     QEASQLSDSL HQLDLANEEI TSYNERGGPA QLTKCESEVR SIEMEIVNLE KEQGSITKDI
     NAISTRLMDS ENTKRQYADN LRYRRETAAL DDVNATIEEL AAQNAEVDRG RFREESERRT
     REHNALSARQ ASKMGEMKSK DDQLMQLLAD WNTDYKDAAV KFKEAHIKVE TTKAAVDDLG
     RYGSALDKAI MKYHSLKMEE INRIIEELWQ KTYRGTDVDT ILIRSDNENA KGNRSYNYRV
     CMVKQDAEMD MRGRCSAGQK VLASIIIRLA LAECFGVNCG LIALDEPTTN LDRDNIRSLA
     ESLHDIIKSR QQQSNFQLIV ITHDEEFLRH MQCGDFCDYY YRVSRNERQK SIIERQSIAA
     VSIFSWDPLP L
//