ID G0V5A1_NAUCC Unreviewed; 1304 AA.
AC G0V5A1;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 19-OCT-2011, sequence version 1.
DT 27-MAR-2024, entry version 60.
DE RecName: Full=Zinc-hook domain-containing protein {ECO:0000259|PROSITE:PS51131};
GN Name=NCAS0A00770 {ECO:0000313|EMBL:CCC66637.1};
GN OrderedLocusNames=NCAS_0A00770 {ECO:0000313|EMBL:CCC66637.1};
OS Naumovozyma castellii (strain ATCC 76901 / BCRC 22586 / CBS 4309 / NBRC
OS 1992 / NRRL Y-12630) (Yeast) (Saccharomyces castellii).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Naumovozyma.
OX NCBI_TaxID=1064592 {ECO:0000313|EMBL:CCC66637.1, ECO:0000313|Proteomes:UP000001640};
RN [1] {ECO:0000313|EMBL:CCC66637.1, ECO:0000313|Proteomes:UP000001640}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 76901 / BCRC 22586 / CBS 4309 / NBRC 1992 / NRRL Y-12630
RC {ECO:0000313|Proteomes:UP000001640};
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]
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Type strain:CBS 4309;
RA Gordon J.L., Armisen D., Proux-Wera E., OhEigeartaigh S.S., Byrne K.P.,
RA Wolfe K.H.;
RT "Genome sequence of Naumovozyma castellii.";
RL Submitted (AUG-2011) 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; HE576752; CCC66637.1; -; Genomic_DNA.
DR RefSeq; XP_003673028.1; XM_003672980.1.
DR STRING; 1064592.G0V5A1; -.
DR GeneID; 11529152; -.
DR KEGG; ncs:NCAS_0A00770; -.
DR eggNOG; KOG0962; Eukaryota.
DR HOGENOM; CLU_006184_0_0_1; -.
DR InParanoid; G0V5A1; -.
DR OMA; FSDYYYR; -.
DR OrthoDB; 5477220at2759; -.
DR Proteomes; UP000001640; Chromosome 1.
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:UP000001640};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|PROSITE-ProRule:PRU00471}.
FT DOMAIN 632..733
FT /note="Zinc-hook"
FT /evidence="ECO:0000259|PROSITE:PS51131"
FT COILED 226..253
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 299..340
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 459..523
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 597..624
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 784..866
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 891..943
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 1000..1097
FT /evidence="ECO:0000256|SAM:Coils"
FT BINDING 679
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00471"
FT BINDING 682
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00471"
SQ SEQUENCE 1304 AA; 150793 MW; B6D7F11254ED7417 CRC64;
MSAIYKLSIQ GIRSFDSNDR ETIEFGKPLT LIVGSNGSGK TTIIECLKYA TTGDLPPNSK
GGVFVHDPKI TGEKDIRAQV KLAFTSANGI TMIVTRNIQL LAKKTTNTFK TLEGQLAAIN
QNGDRTTLST RSIELDTQVP LYLGVPKAIL EYVIFCHQED SLWPLSEPSN LKKKFDEIFQ
AMKFTKAIDN LKAIKKDMTV DIKLLKQSVE HLRVDRDRSR GTKMNIVQLQ AQIDEYQMKV
KDVEIELQKI TEQSDKLFKS NQEFQQVLSK IQNLRMLDKH LKEEIENVSN SVELISLPKQ
ELEELLANFS KSFDENEQEV KKIEVEIDIL KRDANQSQSK YTGLVRKMGE LQAREEAYKK
NVITLESLSM AFSDRYNLGY VGNKPQEFFE KSKKFNDDLN TSFSNFEKES RNRLKSLENE
LSEITNSETI QNQRLEYSKA DQQKISAEIE KLTSELTINE FTHSDLEAAK AKLNQYNEKL
TSWENDDIIT KLNSTLKEKN DQMIIAESDL QQIQERIMKT NQQADLFAKL ALIKGSLKEK
LHSLEKVTEK VTNDERARNW KLTVPDDLDM DFKRFYINLQ KEIAVNNKNI HEKDKSYTEA
NIKLTNAQKE IENSKETEQR LITALQSALP EDCSIDEYDE VVLETELSYK TALENLKMHQ
TTLEFNRKAL EIAERDSCCY LCSRKFETAD FKSKLLQELK AKTDANFETT LKDTVKEEKE
YLDSLRALER DVIKLHSTQT NSKNLGNGLT SLVEHVSSLK KELAKVEEIG NGLKEDRDHC
EKVLRPLVDQ VAQLRKETRD LEKESQDLSE ELQIYGDSDG GVQTVDELNQ QQQDKNNFMR
QLRKDIQDLQ NERESKMREH STLLNVIKDR NLKINEIERV LQRKQNIDDD LHSKNAELKE
ILLRIQTLKT ELIELRNKKQ ELSKVLNNEM ERFSGEMEAK RKNLGSITSY LDRISNLKQE
VSEFDNSGAK DLGMCIQESE DIQKEIAYIT KDIEVKQNHL NSKKDKLKDS SNEKRNLEQN
IHLANLRAKL KETENDISRL DIQNAEAERD KYQQESLRLR NLFEKLSAEN AGKLGEIKQL
QSQVDSLSQQ LRSDYKDVDE KYHKEWVSLQ TRTFVTDDID TYSKALDSAI MRYHGLKMQD
INRIIDELWK RTYSGTDIDT IKIRSDEVSS TVRGKSYNYR VVMYKQDAEL DMRGRCSAGQ
KVLASIIIRL ALSETFGINC GVIALDEPTT NLDEENIESL AKSLSNIIEM RRHQKNFQLI
VITHDEKFLN HMNASQFTDH FFQVKRDDRQ KSQIEWVDIT KVAE
//
