ID A0A060WHV3_ONCMY Unreviewed; 1303 AA.
AC A0A060WHV3;
DT 03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT 03-SEP-2014, sequence version 1.
DT 27-MAR-2024, entry version 36.
DE RecName: Full=Zinc-hook domain-containing protein {ECO:0000259|PROSITE:PS51131};
GN ORFNames=GSONMT00076160001 {ECO:0000313|EMBL:CDQ66848.1};
OS Oncorhynchus mykiss (Rainbow trout) (Salmo gairdneri).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Protacanthopterygii; Salmoniformes;
OC Salmonidae; Salmoninae; Oncorhynchus.
OX NCBI_TaxID=8022 {ECO:0000313|EMBL:CDQ66848.1, ECO:0000313|Proteomes:UP000193380};
RN [1] {ECO:0000313|EMBL:CDQ66848.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=24755649; DOI=10.1038/ncomms4657;
RA Berthelot C., Brunet F., Chalopin D., Juanchich A., Bernard M., Noel B.,
RA Bento P., Da Silva C., Labadie K., Alberti A., Aury J.M., Louis A.,
RA Dehais P., Bardou P., Montfort J., Klopp C., Cabau C., Gaspin C.,
RA Thorgaard G.H., Boussaha M., Quillet E., Guyomard R., Galiana D., Bobe J.,
RA Volff J.N., Genet C., Wincker P., Jaillon O., Roest Crollius H.,
RA Guiguen Y.;
RT "The rainbow trout genome provides novel insights into evolution after
RT whole-genome duplication in vertebrates.";
RL Nat. Commun. 5:3657-3657(2014).
RN [2] {ECO:0000313|EMBL:CDQ66848.1}
RP NUCLEOTIDE SEQUENCE.
RA Genoscope - CEA;
RL Submitted (MAR-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|ARBA:ARBA00001947};
CC -!- SUBCELLULAR LOCATION: Chromosome, telomere
CC {ECO:0000256|ARBA:ARBA00004574}.
CC -!- SIMILARITY: Belongs to the SMC family. RAD50 subfamily.
CC {ECO:0000256|ARBA:ARBA00009439}.
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DR EMBL; FR904558; CDQ66848.1; -; Genomic_DNA.
DR STRING; 8022.A0A060WHV3; -.
DR PaxDb; 8022-A0A060WHV3; -.
DR Proteomes; UP000193380; Unassembled WGS sequence.
DR GO; GO:0000781; C:chromosome, telomeric region; IEA:UniProtKB-SubCell.
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; 2.
DR SUPFAM; SSF75712; Rad50 coiled-coil Zn hook; 1.
DR PROSITE; PS51131; ZN_HOOK; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Chromosome {ECO:0000256|ARBA:ARBA00022895};
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:UP000193380};
KW Telomere {ECO:0000256|ARBA:ARBA00022895};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|PROSITE-ProRule:PRU00471}.
FT DOMAIN 625..724
FT /note="Zinc-hook"
FT /evidence="ECO:0000259|PROSITE:PS51131"
FT REGION 965..993
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 265..349
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 397..527
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 570..645
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 702..929
FT /evidence="ECO:0000256|SAM:Coils"
FT BINDING 671
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00471"
FT BINDING 674
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00471"
SQ SEQUENCE 1303 AA; 151821 MW; B50E214C318D9315 CRC64;
MSRIEKMSIL GVRSFGVEDK DKQVISFFNP LTVLVGPNGA GKTTIIECLK YVTAGEFPPG
SKGNTFVHDP KDAHETDVRA QIRLQFTDLN GEKVAVQRSM QATQKGKKTE FRSLEGVITR
IKHGEKVSLS SKCAELDREM ISALGVSKAV LDHVIFCHQE ESNWPLGEGK PLKNKFDAIF
SATRYIKVLE TLRQLRLKQS NEVKECQVEL KFLKLNKEKA LEIRELLASK ETQLASSKDA
VQKIEGQIEP LENRLVDIDE NLGKVMKLDN DIKALDSRKK QMEEDNQELE EKMEQVFQGS
DEQLQEMYQN HQRTVKEKEK RFTECQREME RAGRECQRLN RLKSDLLVEQ GRLQLEADRH
AQNIKARDSQ VRTLAAYLEM EGYDRSPFND RQLQSFNRQV KERLDQETEA ANQIMRDIQE
KEAMKQQSID EIRDKKTGLE RTMELKKDLQ VKKQQELRNV KSDLQRLEGS SSRLQELETE
LTKAERELES AVQSSNVDGL KAEVLELQKD KAELDRTQRR LDREMETLNT HTTTRTQMDM
LKKDKIDNXX EDLVSLLGHF PKKRELEDWI HSKSKEINST REKLAKLNKE LASGEQNKSH
ITAEIRRKEQ QLASYEEKMF NVCGSQDFQQ DLGKLQDDLE KTSKQRAMLA GATAVYTQFI
SQLTEEGEPC CPVCQRIFPS EAELQDVIND MQSKLRLVPD KLKNTEQDLK RKERRKDDMM
ALKPVRQSIA ELQEKELPEL RNRLQNVNRD IERLKGDVEE QETLLSTLMS EEDTAKACLQ
DISLMDRYQL DLKDVERKIA QQAAKLQGVD LSRTIQQVNQ EKQETQHRLD TTSSKMELKR
KLIQDQQEQI QSLKSSMNET RAEKLQISSN MQKQQQLEEQ CVEFTTEIQA LHREIKEAKE
QVSPLATTLE KLQQERLDLM ERRKQRQEEG QEKINSIKDK VKSMAAFERE ITGYTEEGKD
DYKEQKEGEL RETNTQVHEA EKQREKINKD SGNIRQDIDT QKVQERWLQD NLTLRKRIEE
LKDVTKKREA VAKDMGNMQV LQLRNERRES EQRVDDLKKN RSVSLGRQKG FEEEIIRFRK
ELREDQYGKA DERFRDRMIV MRTTELANKD LDIYYKALDQ TIMKFHSMKM EEINKIIRDL
WRSTYRGQDI EYVEIRSDVD ENSSGAGVKR RTYNYRVVMV KGDTALDMRG RCSAGQKVLA
SLIIRLALAE TFCLNCGILA LDEPTTNLDR ENIESLAHAL VEIIKSRSRQ RNFQLLIITH
DEDFVELMGR SSYVEHFYRI RKNMDQCSEI TKCSVSSLTS YLH
//