ID A0A2V5HVP7_9EURO Unreviewed; 837 AA.
AC A0A2V5HVP7;
DT 12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT 12-SEP-2018, sequence version 1.
DT 24-JAN-2024, entry version 17.
DE RecName: Full=RecA family profile 1 domain-containing protein {ECO:0000259|PROSITE:PS50162};
GN ORFNames=BP00DRAFT_440206 {ECO:0000313|EMBL:PYI26164.1};
OS Aspergillus indologenus CBS 114.80.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX NCBI_TaxID=1450541 {ECO:0000313|EMBL:PYI26164.1, ECO:0000313|Proteomes:UP000248817};
RN [1] {ECO:0000313|EMBL:PYI26164.1, ECO:0000313|Proteomes:UP000248817}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 114.80 {ECO:0000313|EMBL:PYI26164.1,
RC ECO:0000313|Proteomes:UP000248817};
RG DOE Joint Genome Institute;
RA Vesth T.C., Nybo J., Theobald S., Brandl J., Frisvad J.C., Nielsen K.F.,
RA Lyhne E.K., Kogle M.E., Kuo A., Riley R., Clum A., Nolan M., Lipzen A.,
RA Salamov A., Henrissat B., Wiebenga A., De vries R.P., Grigoriev I.V.,
RA Mortensen U.H., Andersen M.R., Baker S.E.;
RT "The genomes of Aspergillus section Nigri reveals drivers in fungal
RT speciation.";
RL Submitted (FEB-2018) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; KZ825609; PYI26164.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2V5HVP7; -.
DR Proteomes; UP000248817; Unassembled WGS sequence.
DR GO; GO:0033063; C:Rad51B-Rad51C-Rad51D-XRCC2 complex; IEA:InterPro.
DR GO; GO:0005657; C:replication fork; IEA:InterPro.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0140664; F:ATP-dependent DNA damage sensor activity; IEA:InterPro.
DR GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR GO; GO:0046982; F:protein heterodimerization activity; IEA:InterPro.
DR GO; GO:0000724; P:double-strand break repair via homologous recombination; IEA:InterPro.
DR GO; GO:0061982; P:meiosis I cell cycle process; IEA:UniProt.
DR CDD; cd08049; TAF8; 1.
DR CDD; cd19490; XRCC2; 1.
DR Gene3D; 1.10.20.10; Histone, subunit A; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR InterPro; IPR006565; BTP.
DR InterPro; IPR009072; Histone-fold.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR020588; RecA_ATP-bd.
DR InterPro; IPR019473; TFIID_su8_C.
DR InterPro; IPR030547; XRCC2.
DR PANTHER; PTHR46644; DNA REPAIR PROTEIN XRCC2; 1.
DR PANTHER; PTHR46644:SF2; DNA REPAIR PROTEIN XRCC2; 1.
DR Pfam; PF07524; Bromo_TP; 1.
DR Pfam; PF10406; TAF8_C; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR PROSITE; PS50162; RECA_2; 1.
PE 4: Predicted;
FT DOMAIN 533..711
FT /note="RecA family profile 1"
FT /evidence="ECO:0000259|PROSITE:PS50162"
FT REGION 1..46
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 131..157
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 329..349
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 139..157
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 837 AA; 94499 MW; 8533DA3D1E0299D6 CRC64;
MVESEPTIKR SASSFSPEDG LNPPDAKRVK RHYHHHHRLQ SPVNPSLPEP AIVDDVCVDQ
LLNRSISQYL RTCGFELADP AALDAFRRVT EEYILSVASY VRQSMLSSRR TQPIPHDFDD
ALRRHSVPYT DLLPHVQPHP NLDPIPTPQP TPPPEEDSFK ALPSFGPQLS VENDRVRSSY
IPKHFPAFPS KHTYRHTAVF TEREQDARII RERATEDGRH GEEALRKLAR AAFKDNQFGS
SAREKKPWGR RAETMDSMFE KTVKGLAKRM QRTATVPGAA APMEIDSGAG LDTEVKPVRS
KLALSIELPP IINCEREFWR RAPSSGTRRV VEDKQPAVKK EAHDRASRVD SWNLPSKQAH
NRLTDDDTRL GDPALRRITR VLYHLQQLAF LQIDGAAFAT LLLEVLGRDV DVLREGFGVE
NGDEGGHCLL LTEVHEERLD ELLHDLRELC QERIGRNTLK PRFGVDELDN LLGIFTAPVP
SGQHRADTAQ EELQIAPEHD QFGIDANTHS AGIAVPAYTS HADPVLEISS TSSAAGKTNL
LYYLTALAIL PAKVNGFQIG GHDSAVVFID TDGRFDAERL RTVLRGIVKE TERTIVSCLE
HVHIFQPQSS SALLATLQQL DTYLLDLARH VSSSRALRLL FLDSANAFYW QDRLQDEVTR
IEQIGRPAAE IETDRRKKQS FYLFAMYTDL VRELKRLQRV FSCAIVFTTT ATPHTTPSRH
SHGYQPSGPY ELFNPLDAPA FRRPSFRSAL PAPWGTFPAL RVVVQRDPVR PFPAAMGLQE
AEDNAAKRQE VLMRGRFCGW VNMWGREDWP RRWLEGVEAL DGGMFFFRMG RDGVQFE
//