ID J7S727_KAZNA Unreviewed; 1306 AA.
AC J7S727;
DT 31-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 31-OCT-2012, sequence version 1.
DT 27-MAR-2024, entry version 54.
DE RecName: Full=Zinc-hook domain-containing protein {ECO:0000259|PROSITE:PS51131};
GN Name=KNAG0F00650 {ECO:0000313|EMBL:CCK70734.1};
GN OrderedLocusNames=KNAG_0F00650 {ECO:0000313|EMBL:CCK70734.1};
OS Kazachstania naganishii (strain ATCC MYA-139 / BCRC 22969 / CBS 8797 / KCTC
OS 17520 / NBRC 10181 / NCYC 3082 / Yp74L-3) (Yeast) (Saccharomyces
OS naganishii).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Kazachstania.
OX NCBI_TaxID=1071383 {ECO:0000313|EMBL:CCK70734.1, ECO:0000313|Proteomes:UP000006310};
RN [1] {ECO:0000313|EMBL:CCK70734.1, ECO:0000313|Proteomes:UP000006310}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-139 / BCRC 22969 / CBS 8797 / CCRC 22969 / KCTC 17520
RC / NBRC 10181 / NCYC 3082 {ECO:0000313|Proteomes:UP000006310};
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).
RN [2] {ECO:0000313|Proteomes:UP000006310}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-139 / BCRC 22969 / CBS 8797 / CCRC 22969 / KCTC 17520
RC / NBRC 10181 / NCYC 3082 {ECO:0000313|Proteomes:UP000006310};
RA Gordon J.L., Armisen D., Proux-Wera E., OhEigeartaigh S.S., Byrne K.P.,
RA Wolfe K.H.;
RT "Genome sequence of Kazachstania naganishii.";
RL Submitted (AUG-2012) to the EMBL/GenBank/DDBJ databases.
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}.
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DR EMBL; HE978319; CCK70734.1; -; Genomic_DNA.
DR STRING; 1071383.J7S727; -.
DR eggNOG; KOG0962; Eukaryota.
DR HOGENOM; CLU_006184_0_0_1; -.
DR OMA; FSDYYYR; -.
DR OrthoDB; 5477220at2759; -.
DR Proteomes; UP000006310; Chromosome 6.
DR GO; GO:0030870; C:Mre11 complex; IEA:InterPro.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0006302; P:double-strand break repair; IEA:InterPro.
DR GO; GO:0051321; P:meiotic cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0000723; P:telomere maintenance; IEA:InterPro.
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 InterPro; IPR013134; Zn_hook_RAD50.
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; PF04423; Rad50_zn_hook; 1.
DR Pfam; PF13558; SbcC_Walker_B; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR PROSITE; PS51131; ZN_HOOK; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW DNA damage {ECO:0000256|ARBA:ARBA00022763};
KW DNA repair {ECO:0000256|ARBA:ARBA00023204};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Meiosis {ECO:0000256|ARBA:ARBA00023254};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|PROSITE-
KW ProRule:PRU00471}; Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000006310};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|PROSITE-ProRule:PRU00471}.
FT DOMAIN 633..734
FT /note="Zinc-hook"
FT /evidence="ECO:0000259|PROSITE:PS51131"
FT COILED 219..253
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 306..347
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 466..523
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 729..867
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 899..926
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 973..1091
FT /evidence="ECO:0000256|SAM:Coils"
FT BINDING 680
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00471"
FT BINDING 683
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00471"
SQ SEQUENCE 1306 AA; 151286 MW; BB68879ABD034D75 CRC64;
MSAIHKLSIQ GIRSFDSNDR ETIEFGAPLT LIVGMNGSGK TTVIECLKYA TTGTLPPNSK
GGVFVHDPKI TGEKDVRAQV KLAFSSANGL NMIVTRNIQL LAKKTTNTFK TLEGQLVAIN
QSGERTTLST KSMELDTQVP LYMGVPSAIL DYVIFCHQED SLWPLSEPSN LKKKFDEIFQ
AMKFTKAIDN LKVIKKDMAV EIKLLQQSVE HLKIDRDRSK TTKIKIQQLE AKIEQFRQQV
KNIESQILDI TGQSDRLFKS NQTFQEVLSK VENLKTLKLA TSNEIERLSA TIELLDLPKD
ELSSLLDNFS LTLQQQESKL DQTQYEINQL KNQLQNAYIE KDDLIRKEAE LTSKRHDYEQ
LKHDRLTLIE EFKQKFPLDL SSDYPTECLR LLRDYKKTLE SDAQMVKAEG ESKLAKIENH
VAEQVYEETV QNQKLEYCIR DKTDLKKRID WLETELKSSD VSEETLEDEK KALTELNGQL
ANFEKGNASE EVIKLLKLKN MDILSAEEEL EKIQEQILKT NQQTDLFAKL GLIKKSIEEK
KGTVTDLEET LQKNDISQIL PTPLNNEDLD LEFKKFYISL QKDIALSNIV LHDKENKLSE
ITFRLDSSNA DIERNKAEIQ ALTLRLDAEL PEDCPIDEYD EVVADAELSY KTALENLKMH
QTTLEFNRKA LDIAQNKDCC YLCSRKFENV EVKSRLLAEL KKKTDANFEH TLVTAVNEEK
EFLHNLRTME KDIISLRNIK EQVKKLEELK PCLVEEHTST KASLEEIENS NRKLKEKREV
CEKTLRRTIE QIVDNSKELN LLEAEFKGLS KQLEMYNNSS GTLQTVDELR AEQKQKNDLL
RKLRKDINDL QEERERKTKE HNSLINMVKE KTLSIREMES SVASEKNIQR EYSAKKTELN
DIEHHIQSIK SEIEKTKGEK EKKQSQYNRQ KLGLKLLTEK SQTDIINITK ACDKLGGILD
KVRQYEQQDF NALEKCQDTI KQADSTLKNI EKQLNEKTEY LYMGRQKLQD SNNEKRNLRD
NIELLNLKDK LQSIIDNIKR LDVRNAETER EKYQQESEKL RNLYEGLSAE NAGKLGEMKQ
LQNQIDSLSL QLGSDYKDVD QKYQKEWVEL QARTFVTDDI DTYSKALDNA IMKYHGLKME
DINRIIDELW KRTYSGTDID TIKIRSEEVN NTVRGKSYNY RVVMFKQDAE LDMRGRCSAG
QKVLASIIIR LALSETFGLN CGVIALDEPT TNLDEENIES LAQSLHNIIQ MRKYQKNFQL
IVITHDEKFL MHMNAGQFTD HFFKIKRDDR QKSQIEWVDI NRVTEY
//
