ID G8BVP0_TETPH Unreviewed; 698 AA.
AC G8BVP0;
DT 25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT 25-JAN-2012, sequence version 1.
DT 24-JAN-2024, entry version 60.
DE RecName: Full=Double-strand break repair protein {ECO:0000256|PIRNR:PIRNR000882};
GN Name=TPHA0G01310 {ECO:0000313|EMBL:CCE63968.1};
GN OrderedLocusNames=TPHA_0G01310 {ECO:0000313|EMBL:CCE63968.1};
OS Tetrapisispora phaffii (strain ATCC 24235 / CBS 4417 / NBRC 1672 / NRRL
OS Y-8282 / UCD 70-5) (Yeast) (Fabospora phaffii).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Tetrapisispora.
OX NCBI_TaxID=1071381 {ECO:0000313|EMBL:CCE63968.1, ECO:0000313|Proteomes:UP000005666};
RN [1] {ECO:0000313|EMBL:CCE63968.1, ECO:0000313|Proteomes:UP000005666}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 24235 / CBS 4417 / NBRC 1672 / NRRL Y-8282 / UCD 70-5
RC {ECO:0000313|Proteomes:UP000005666};
RX PubMed=22123960; DOI=10.1073/pnas.1112808108;
RA Gordon J.L., Armisen D., Proux-Wera E., OhEigeartaigh S.S., Byrne K.P.,
RA Wolfe K.H.;
RT "Evolutionary erosion of yeast sex chromosomes by mating-type switching
RT accidents.";
RL Proc. Natl. Acad. Sci. U.S.A. 108:20024-20029(2011).
CC -!- FUNCTION: Involved in DNA double-strand break repair (DSBR). Possesses
CC single-strand endonuclease activity and double-strand-specific 3'-5'
CC exonuclease activity. Also involved in meiotic DSB processing.
CC {ECO:0000256|PIRNR:PIRNR000882}.
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000256|PIRNR:PIRNR000882};
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123,
CC ECO:0000256|PIRNR:PIRNR000882}.
CC -!- SIMILARITY: Belongs to the MRE11/RAD32 family.
CC {ECO:0000256|ARBA:ARBA00009028, ECO:0000256|PIRNR:PIRNR000882,
CC ECO:0000256|RuleBase:RU003447}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; HE612862; CCE63968.1; -; Genomic_DNA.
DR RefSeq; XP_003686402.1; XM_003686354.1.
DR AlphaFoldDB; G8BVP0; -.
DR STRING; 1071381.G8BVP0; -.
DR GeneID; 11535838; -.
DR KEGG; tpf:TPHA_0G01310; -.
DR eggNOG; KOG2310; Eukaryota.
DR HOGENOM; CLU_009535_3_0_1; -.
DR OMA; NHTGHTN; -.
DR OrthoDB; 169704at2759; -.
DR Proteomes; UP000005666; Chromosome 7.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0030870; C:Mre11 complex; IEA:UniProtKB-UniRule.
DR GO; GO:0008296; F:3'-5'-DNA exonuclease activity; IEA:InterPro.
DR GO; GO:0004520; F:DNA endonuclease activity; IEA:InterPro.
DR GO; GO:0030145; F:manganese ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0006302; P:double-strand break repair; IEA:UniProtKB-UniRule.
DR GO; GO:0051321; P:meiotic cell cycle; IEA:UniProtKB-KW.
DR CDD; cd00840; MPP_Mre11_N; 1.
DR Gene3D; 3.60.21.10; -; 1.
DR Gene3D; 3.30.110.110; Mre11, capping domain; 1.
DR InterPro; IPR004843; Calcineurin-like_PHP_ApaH.
DR InterPro; IPR029052; Metallo-depent_PP-like.
DR InterPro; IPR003701; Mre11.
DR InterPro; IPR038487; Mre11_capping_dom.
DR InterPro; IPR007281; Mre11_DNA-bd.
DR InterPro; IPR041796; Mre11_N.
DR NCBIfam; TIGR00583; mre11; 1.
DR PANTHER; PTHR10139; DOUBLE-STRAND BREAK REPAIR PROTEIN MRE11; 1.
DR PANTHER; PTHR10139:SF1; DOUBLE-STRAND BREAK REPAIR PROTEIN MRE11; 1.
DR Pfam; PF00149; Metallophos; 1.
DR Pfam; PF04152; Mre11_DNA_bind; 1.
DR PIRSF; PIRSF000882; DSB_repair_MRE11; 1.
DR SMART; SM01347; Mre11_DNA_bind; 1.
DR SUPFAM; SSF56300; Metallo-dependent phosphatases; 1.
PE 3: Inferred from homology;
KW DNA damage {ECO:0000256|ARBA:ARBA00022763, ECO:0000256|PIRNR:PIRNR000882};
KW DNA repair {ECO:0000256|ARBA:ARBA00023204, ECO:0000256|PIRNR:PIRNR000882};
KW Endonuclease {ECO:0000256|ARBA:ARBA00022759,
KW ECO:0000256|PIRNR:PIRNR000882};
KW Exonuclease {ECO:0000256|ARBA:ARBA00022839, ECO:0000256|PIRNR:PIRNR000882};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|PIRNR:PIRNR000882};
KW Manganese {ECO:0000256|ARBA:ARBA00023211, ECO:0000256|PIRNR:PIRNR000882};
KW Meiosis {ECO:0000256|ARBA:ARBA00023254, ECO:0000256|PIRNR:PIRNR000882};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Nuclease {ECO:0000256|ARBA:ARBA00022722, ECO:0000256|PIRNR:PIRNR000882};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242, ECO:0000256|PIRNR:PIRNR000882};
KW Reference proteome {ECO:0000313|Proteomes:UP000005666};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 633..655
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 291..472
FT /note="Mre11 DNA-binding"
FT /evidence="ECO:0000259|SMART:SM01347"
FT REGION 551..607
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 557..574
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 575..601
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 125
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000882-1"
SQ SEQUENCE 698 AA; 80186 MW; E55340B978E122BE CRC64;
MDYPDENTIR VLITTDNHVG YNENDPIAGD DSWKTFHEIM MLAKDNNVDM VLQAGDLFHV
NKPSKKSMYQ VMRSLRMACM GDKPCELELL NDTSEIFHYN EFTDLNYQDP NFNISIPVFG
IAGNHDDASG DALLCPMDIL QVSGLVNHFG KVIEADKIKV PPLLFKKGET KLALYGLASV
RDERLFRTFK EGNVTFEVPD MEGDEWFNIM CVHQNHTGHT NTAFLPEQFL PGFLDMVIWG
HEHECIPHLV HNPLKNFDVL QPGSSVATSL CDAEAQDKHV FILEVRKGEP RKLIPIPLKT
TRPFIMRNIT LTDVAYLRPH DKEGIIKYLV NEVEDMISEA KVETTRKLGL ELKEEEEAAK
LLQLNLPLIR LRVDYSGPED RNSIIDYQLE NPRRFSNRFV GSVANSNNII QYHKKRKFPK
KNTSNTKGFE YNENLKDNDA ELDVQTLVND MLNKMSLALL PEIGMNEAVK KFIEKDEKSA
LKDFIDEEIK NEVKMLASSE ELLSLTDPEE IRKLIRHVKK AKASQDYSLD DDKDLDPNLA
SALAKAKKRL NEIEGNPESN RALTNFGITS NELDDIPKNQ EDKPVKKSRT ENKKRISSTK
RASPETKNPL YQIRSLFQMK NNQMPVVRIT SRIVLLPTHI LIIKLMMILL PSILVMKKII
QKIVPIKKEF HKWQALEKDH HHPPNLLQEL QRLRRQMS
//
