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Database: UniProt
Entry: E4X9L9_OIKDI
LinkDB: E4X9L9_OIKDI
Original site: E4X9L9_OIKDI 
ID   E4X9L9_OIKDI            Unreviewed;      1335 AA.
AC   E4X9L9;
DT   08-FEB-2011, integrated into UniProtKB/TrEMBL.
DT   08-FEB-2011, sequence version 1.
DT   27-MAR-2024, entry version 38.
DE   RecName: Full=Rad50/SbcC-type AAA domain-containing protein {ECO:0000259|Pfam:PF13476};
GN   ORFNames=GSOID_T00005013001 {ECO:0000313|EMBL:CBY08442.1};
OS   Oikopleura dioica (Tunicate).
OC   Eukaryota; Metazoa; Chordata; Tunicata; Appendicularia; Copelata;
OC   Oikopleuridae; Oikopleura.
OX   NCBI_TaxID=34765 {ECO:0000313|EMBL:CBY08442.1};
RN   [1] {ECO:0000313|EMBL:CBY08442.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=21097902; DOI=10.1126/science.1194167;
RA   Denoeud F., Henriet S., Mungpakdee S., Aury J.M., Da Silva C.,
RA   Brinkmann H., Mikhaleva J., Olsen L.C., Jubin C., Canestro C.,
RA   Bouquet J.M., Danks G., Poulain J., Campsteijn C., Adamski M., Cross I.,
RA   Yadetie F., Muffato M., Louis A., Butcher S., Tsagkogeorga G., Konrad A.,
RA   Singh S., Jensen M.F., Cong E.H., Eikeseth-Otteraa H., Noel B.,
RA   Anthouard V., Porcel B.M., Kachouri-Lafond R., Nishino A., Ugolini M.,
RA   Chourrout P., Nishida H., Aasland R., Huzurbazar S., Westhof E., Delsuc F.,
RA   Lehrach H., Reinhardt R., Weissenbach J., Roy S.W., Artiguenave F.,
RA   Postlethwait J.H., Manak J.R., Thompson E.M., Jaillon O., Du Pasquier L.,
RA   Boudinot P., Liberles D.A., Volff J.N., Philippe H., Lenhard B.,
RA   Roest Crollius H., Wincker P., Chourrout D.;
RT   "Plasticity of animal genome architecture unmasked by rapid evolution of a
RT   pelagic tunicate.";
RL   Science 330:1381-1385(2010).
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; FN653031; CBY08442.1; -; Genomic_DNA.
DR   InParanoid; E4X9L9; -.
DR   Proteomes; UP000001307; Unassembled WGS sequence.
DR   GO; GO:0005634; C:nucleus; IEA:UniProt.
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:0006996; P:organelle organization; IEA:UniProt.
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   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:UP000001307};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT   DOMAIN          7..262
FT                   /note="Rad50/SbcC-type AAA"
FT                   /evidence="ECO:0000259|Pfam:PF13476"
FT   REGION          516..550
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          197..300
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          330..357
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          451..478
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          743..792
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          834..921
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          980..1028
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   1335 AA;  154474 MW;  42C69C66E40145A5 CRC64;
     MVFLKTIKIS GIRSIGPGEE HEVEIKFQRP FTLISGQNGA GKTTIIECLK YATSGSFPPG
     TTKATVTGKK RKAVNTTKVP AQVFLELEIP SECGKPQLVQ INRKLEGTLK DGDFTTKSLE
     GTITVKDKRS GEIISSKVQK VEELNKHIRG LLGVNKPVLE YAVFCHQDET LWPFEEAKLL
     KAKFDEIFQS AEYVKSLEQI KKAYKEASSE IVIMKERQRS ETYRVEHFRK QKERENKLTI
     EVAEARKEIQ TLDEQLDKVE EEEDQCATVL RDQRNKMEAV KSLQARCREI NEDVKRFKEM
     EGVPKIVSSH NESITEIEES ILNSEKGDDR RILEDQINEK QDEKKSLEEK LKSCQTRLDN
     EVMTIQQFDS DEKKIADIFE REHNRFPNVE TSGPLNEKES QEDFIDGVSE VLDHQREQIE
     ITEKKRDEEV GIIDEKLKEN SVEKTTLETT ISLKKKQMTT EKRKIEEIEE QLRSSSQIAD
     RHSRFVRKRD ALDKDYSAVS WETEFEKIDE SLTQNSDEKD ILTQKREKLE EEEEKSQIME
     DLEREKKSKE ADVSRMENEV RKSRDVLEDI FSQIEGFTDV EAVSKDDLEA WSMKYSKDFS
     RNEDALKRQV QALFQKQSEE KQLKKDHVKI QTRLVTNREK IESEILGELQ DEKSKLNELT
     CEETELFEKV QAMEEGKKLF KQFLSSVQKK KGCPVCTSDL SGSKLDQTIE FCKSNMSFKN
     GPQMKADLED LRTDITKKKE HIVVLEEIEK DEAEEAKVTA QQKTLKSQIL RINDDKIKLE
     KSKKTLETIK NKLQLTAFDQ FEIFTSANQQ LEPSKARLTK IDREIFQMGE SKSVTEVRNE
     LKSVKDEIKA LQLTENELRH SQNQLSTKQR TLNEQLNKTR EEIAKLEKSM GSGSEEMIAQ
     KSQLEEEVFR MQAEIESTND HLKDLHKEHS LLNTESQRKR KNFDQEIVKA KRTCEKILSC
     VTALKNSHKH HRERYQEFSK ERAEKEKTDL QQQIKSNQDE LYGLIEVIEE LQSRRGEFEV
     RKSKLQMART LLLKKTELDE HSLKYKQAKQ DFIEFNDSMG EDGIRGHLQP KLDEIRARRE
     DIVDRRAKLE GEKTAKLEAI AETRSLEEDL GEDREREFFR STIRVRIEES FARDLDKFSK
     ALGTAIIEVH QKQMTKLNSI ITSLWKTSYQ GSDIDTISIS AKDTRVGAST RSNMDYCVNM
     HRPDGAVLSM RGRASAGQRM LASLVLRLAL METFSSSGIL TLDEPTTNLD KDAIRKFAET
     VVSLAKTARG YNMKTQFIII THDKEFTEIL QDLATVEAAY RLEKSSGGYT VAKAMSEQTD
     MDFDVYDTDD IYDRH
//
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