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Database: UniProt
Entry: A9NIR5_TRIVA
LinkDB: A9NIR5_TRIVA
Original site: A9NIR5_TRIVA 
ID   A9NIR5_TRIVA            Unreviewed;       562 AA.
AC   A9NIR5;
DT   05-FEB-2008, integrated into UniProtKB/TrEMBL.
DT   05-FEB-2008, sequence version 1.
DT   27-MAR-2024, entry version 49.
DE   SubName: Full=MRE11-like protein {ECO:0000313|EMBL:ABC61985.1};
OS   Trichomonas vaginalis.
OC   Eukaryota; Metamonada; Parabasalia; Trichomonadida; Trichomonadidae;
OC   Trichomonas.
OX   NCBI_TaxID=5722 {ECO:0000313|EMBL:ABC61985.1};
RN   [1] {ECO:0000313|EMBL:ABC61985.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=NIH-C1 {ECO:0000313|EMBL:ABC61985.1};
RA   Malik S.-B., Stefaniak L.M., Logsdon J.M.Jr.;
RL   Submitted (DEC-2005) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:ABC61985.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=NIH-C1 {ECO:0000313|EMBL:ABC61985.1};
RX   PubMed=18663385; DOI=10.1371/journal.pone.0002879;
RA   Malik S.B., Pightling A.W., Stefaniak L.M., Schurko A.M., Logsdon J.M.Jr.;
RT   "An expanded inventory of conserved meiotic genes provides evidence for sex
RT   in Trichomonas vaginalis.";
RL   PLoS ONE 3:E2879-E2879(2008).
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DR   EMBL; DQ321776; ABC61985.1; -; Genomic_DNA.
DR   VEuPathDB; TrichDB:TVAG_098295; -.
DR   VEuPathDB; TrichDB:TVAGG3_0390540; -.
DR   GO; GO:0005634; C:nucleus; IEA:InterPro.
DR   GO; GO:0004519; F:endonuclease activity; IEA:UniProtKB-KW.
DR   GO; GO:0004527; F:exonuclease activity; IEA:UniProtKB-KW.
DR   GO; GO:0030145; F:manganese ion binding; IEA:InterPro.
DR   GO; GO:0006302; P:double-strand break repair; IEA:InterPro.
DR   CDD; cd00840; MPP_Mre11_N; 1.
DR   Gene3D; 3.60.21.10; -; 1.
DR   InterPro; IPR004843; Calcineurin-like_PHP_ApaH.
DR   InterPro; IPR029052; Metallo-depent_PP-like.
DR   InterPro; IPR007281; Mre11_DNA-bd.
DR   InterPro; IPR041796; Mre11_N.
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   SMART; SM01347; Mre11_DNA_bind; 1.
DR   SUPFAM; SSF56300; Metallo-dependent phosphatases; 1.
PE   4: Predicted;
FT   DOMAIN          293..448
FT                   /note="Mre11 DNA-binding"
FT                   /evidence="ECO:0000259|SMART:SM01347"
FT   REGION          509..562
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        531..551
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   562 AA;  64783 MW;  1F8B19025E9D2807 CRC64;
     MGESQQDTFK IAIFTDTHIG YDEQDAITEK DSFRAFKECV QNAHIQNADI ILHAGDFFNE
     RNPSRYAVIK TMKILDEFVI GQGNPPEILY SEGLSSDPNW LNPNINIKIP FFCMHGNHDA
     PNGLGSTSPI QLLSVSKYLN FFKPVDIKET IELQPIVLKR GTIRVVVYGL GYIFEEKFKE
     VVMGKKLKLI APEEGEFERT YTILMIHQNM SSYDHDIGVM ATRLSDAIWS ETNPHNVDLV
     IWGHEHENLI QRKKYGNIYV TQPGSTVYTQ FKKKNAMQRS MAILTISQNP DFDKFEDIKL
     ESPRTFIYDK IEIDNKGLGF ENDKLNYIKE QIDDKLLEFM DKDGKTIPKX QRPIMRIDVE
     STLSPSSLNL RGLVDEYKEL VANPTKMFRY VVKKANSGTK QSEKAEKQTS YISEQEHIKI
     EDILSQKISP SDLNFISFDS LKDSLMEYIN SDNMSKSKAF ENNINAVFNE RINYIIEQSK
     NKQKEVYDAN KAKEFILNQK ENLPTVKKEN IAEIKGKKKT SAQPSPQKPS VHQESEEEKE
     VIEEEPKRTV ERPKRPRRKA TQ
//
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