ID A0A0A2KZY6_PENIT Unreviewed; 1317 AA.
AC A0A0A2KZY6;
DT 04-FEB-2015, integrated into UniProtKB/TrEMBL.
DT 04-FEB-2015, sequence version 1.
DT 27-MAR-2024, entry version 34.
DE SubName: Full=Recombination/repair protein Rad50 {ECO:0000313|EMBL:KGO73344.1};
GN ORFNames=PITC_086320 {ECO:0000313|EMBL:KGO73344.1};
OS Penicillium italicum (Blue mold).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX NCBI_TaxID=40296 {ECO:0000313|EMBL:KGO73344.1, ECO:0000313|Proteomes:UP000030104};
RN [1] {ECO:0000313|EMBL:KGO73344.1, ECO:0000313|Proteomes:UP000030104}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PHI-1 {ECO:0000313|EMBL:KGO73344.1,
RC ECO:0000313|Proteomes:UP000030104};
RX PubMed=25338147; DOI=10.1094/MPMI-09-14-0261-FI;
RA Ballester A.R., Marcet-Houben M., Levin E., Sela N., Selma-Lazaro C.,
RA Carmona L., Wisniewski M., Droby S., Gonzalez-Candelas L., Gabaldon T.;
RT "Genome, transcriptome, and functional analyses of Penicillium expansum
RT provide new insights into secondary metabolism and pathogenicity.";
RL Mol. Plant Microbe Interact. 28:232-248(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:KGO73344.1}.
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DR EMBL; JQGA01000828; KGO73344.1; -; Genomic_DNA.
DR STRING; 40296.A0A0A2KZY6; -.
DR HOGENOM; CLU_006184_0_0_1; -.
DR OMA; FSDYYYR; -.
DR OrthoDB; 5477220at2759; -.
DR PhylomeDB; A0A0A2KZY6; -.
DR Proteomes; UP000030104; 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 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:UP000030104};
KW Signal {ECO:0000256|SAM:SignalP}; Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT SIGNAL 1..21
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 22..1317
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5002001965"
FT DOMAIN 23..253
FT /note="Rad50/SbcC-type AAA"
FT /evidence="ECO:0000259|Pfam:PF13476"
FT COILED 220..271
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 321..543
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 596..644
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 726..784
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 809..1065
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 1317 AA; 151413 MW; F93A613DB3095001 CRC64;
MAIRALSLSL CLAVLLKMSK IDKLSILGVR SFDNTRSETI QFHTPLTLIV GYNGSGKTII
ECLKYATTGD LPPNSKGGAF IHDPKLCGEK EVLAQVKLSF KATSGAKMVA TRSLQLTVKK
TTRQQKTLEG QLLMVKNGER TAISSRVAEL DQIMPQYLGV SKAVLDSVIF CHQDESLWPM
SEPSVLKKRF DEIFEAMKYT KAIDNIKALR KKQNEELGKY KIMEQHAKED KDKADRAEKR
SIKLQDEIEA LREETQRMSR EMRRVAELAD KAWTQSESYA QVLGALEGKR IEAKSIQTTI
DNLKRHLVEL DDSDDWLEST LEQFETKQIQ YQQQEESQKE NYMEIKERIE QTRHRLGLKQ
AENGKFENDK ANFERQSQRR QNMINEIARA NNIRGLGEKM DQTEIDTFMQ KIKRLLREQN
QSLDRVKREA QKELREVQET LNEIGQTKSA LQETKNAAKR QIAANDKEAT TYQKKLNEIE
VDEGFQAALE SKVEDITSNL EHAKERAKNA SWDQDIQDTN AEIRRLEDES SRLNTELIDS
TKKAGDLARL DHLKKESKDR ERSLQTMKGA HGDRLEKVVG SDWKPETLER GFQQALDSES
KQVADAERER DGVSRELEHV EFKLKTAKKN LKQRQKELDE CVKEIHEAVD AEPSEYPDIV
KERQAQYDLA RKDADQYAGM GEYLTKCLDA AKRTKLCRTC QRSFKNEAEL QTFTKKLEAL
VKKAGLDAED ETLKGLEEDL ETARAASASY DTWVRLSETV IPELEQEEQE CESQRDQLLE
KLETQDGKVS EKTESKRDVE GLAKTVSTIA RYDAEIKTIK LQIQELSAKQ QDASTARTLE
DIQEEIASMN EKSRELKKTL TKVTNEKEKT RSEINKLELE FRDVKSNLDN AKFQLEKKAD
LTVRMEEFKK LNNQQRDAIE KADRDIENLT PELLQAQARY DDISQRADER ERDLQHEISR
LSENIHQLDL ANDDINSYNQ RGGPDQLERS KQELQEIEAE ISRLEADQSE ITREINKIST
QLKDSENTKR QYSDNLTYRQ ATRSLNTVVE EVEQLEAQNA EVDRGRFKQE SERWTREHNA
LAAKQASKMG EMKSKDDQLM QLLADWNTDY KDASSKYKES HIKVETTKAA VEDLARYGGA
LDKAIMQYHG LKMAEINAIA GELWQKTYRG TDVDTILIRS DNENAKGNRS YNYRVCMVKS
GAEMDMRGRC SAGQKVLASI IIRLALAECF GVNCGLIALD EPTTNLDRDN ICSLAESLHD
IIRTRQQQAN FQLIVITHDE EFLRHMKCGD FSDYYYRVSR NERQKSIIER QSIAEVM
//
