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Database: UniProt
Entry: A0A1V6S5C6_9EURO
LinkDB: A0A1V6S5C6_9EURO
Original site: A0A1V6S5C6_9EURO 
ID   A0A1V6S5C6_9EURO        Unreviewed;      1297 AA.
AC   A0A1V6S5C6;
DT   07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT   07-JUN-2017, sequence version 1.
DT   27-MAR-2024, entry version 25.
DE   RecName: Full=Rad50/SbcC-type AAA domain-containing protein {ECO:0000259|Pfam:PF13476};
GN   ORFNames=PENVUL_c008G06293 {ECO:0000313|EMBL:OQE08944.1};
OS   Penicillium vulpinum.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX   NCBI_TaxID=29845 {ECO:0000313|EMBL:OQE08944.1, ECO:0000313|Proteomes:UP000191518};
RN   [1] {ECO:0000313|Proteomes:UP000191518}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IBT 29486 {ECO:0000313|Proteomes:UP000191518};
RX   PubMed=28368369; DOI=10.1038/nmicrobiol.2017.44;
RA   Nielsen J.C., Grijseels S., Prigent S., Ji B., Dainat J., Nielsen K.F.,
RA   Frisvad J.C., Workman M., Nielsen J.;
RT   "Global analysis of biosynthetic gene clusters reveals vast potential of
RT   secondary metabolite production in Penicillium species.";
RL   Nat. Microbiol. 2:17044-17044(2017).
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:OQE08944.1}.
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DR   EMBL; MDYP01000008; OQE08944.1; -; Genomic_DNA.
DR   STRING; 29845.A0A1V6S5C6; -.
DR   OrthoDB; 5477220at2759; -.
DR   Proteomes; UP000191518; 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; 1.
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:UP000191518};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT   DOMAIN          8..241
FT                   /note="Rad50/SbcC-type AAA"
FT                   /evidence="ECO:0000259|Pfam:PF13476"
FT   COILED          200..251
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          389..523
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          576..631
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          706..761
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          789..1045
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   1297 AA;  149382 MW;  4D7B5B067842D484 CRC64;
     MLTAFQVVRS FDNTRSETIQ FHTPLTLIVG YNGSGKTTII ECLKYATTGD LPPNSKGGAF
     IHDPKLCGEK EVLAQVKLSF KATSGAKMVA TRSLQLTVKK TTRQQKTLEG QLLMVKNGER
     TAISSRVAEL DQIMPQYLGV SKAVLDSVIF CHQDESLWPM SEPSVLKKRF DEIFEAMKYT
     KAIDNIKALR KKQNEELGKY KIMEQHAKED KDKADRAEKR SVKLQDEIEA LREEAQQMSQ
     EMRRVAELAD KAWTQSESYA QILGALEGKR IEAKSIQTTI DNLKRHLVEL DDSDEWLEST
     LEQFETKQIQ YQQQEESQKE HYMETKEQIE QTRHRLGLKQ AEHGKFENDK ANFERQSQRR
     QKMINEIARA NNIRGLDEKM DQSEIDTFMQ KIKRLLRDQN QSLDRVRREA QKELREVQDI
     LNEIGQKKSA LQETKNAAKR QIAANDKEAT TYQKKLNEIE VDEGFQAALE SKVEDITSKL
     EHAKERAKTA SWDQDIQDTN AEIRRLEDES SRLNTELIDS TKKAGDLARL DHLKKESKDR
     ERSLQTMKGA HGDRLEKVVG PDWKPETLER GFQQALDSES KQVADAERER DGVSRELEHV
     EFKLKTAKKN LKQRQKELDE CMKEIHEAVD TEPSEYPEIV KERQAQYDLA RKDADQYAGM
     GEYLTKCLDA AKRTKLCRTC QRSFKNEAEL QTFTKKLDAL VKKAGLDAED ETLKSLEEDL
     ETARAASASY DTWVRLSETV IPELEQEEQE FETRRDQLLE KLETQDGKVS EKRESKREVE
     GLAKTVSTIA RYDIEIKAIK SQIQELSANH QDASTARTLE DIQEEIASIN EKSRELKKTL
     TKMTNEKEKT RSEINKLELE FRDVKSNLDN AKFQLEKKAD LTVRMEESKK LNNQQRDAIE
     KADRDIESLT PELLQAQARY DDISQRADER ERDLQHEISR LSENIHQLDL ANDDINSYNQ
     RGGPGQLERS KQELQEIEAE IGKLEAEQSA ITREINKISA QLKDSENTKR QYSDNLTYRQ
     ATRSLNTVVE EVEQLEAQNA EVDRGRFKQE SERWTREHNA LAAKQASKMG EMKSKDDQLM
     QLLADWNTDY KDASSKYKES HIKVETTKAA VEDLARYGGA LDKAIMQYHG LKMAEINAIA
     GELWQKTYRG TDVDTILIRS DNENAKGNRS YNYRVCMVKS GAEMDMRGRC SAGQKVLASI
     IIRLALAECF GVNCGLIALD EPTTNLDRDN IRSLAESLHD IIRTRQQQAN FQLIVITHDE
     EFLRHMKCGD FSDYYYRVSR NERQKSIIER QSIAEVM
//
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