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Database: UniProt
Entry: A0A1E3Q9I7_LIPST
LinkDB: A0A1E3Q9I7_LIPST
Original site: A0A1E3Q9I7_LIPST 
ID   A0A1E3Q9I7_LIPST        Unreviewed;      1321 AA.
AC   A0A1E3Q9I7;
DT   18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT   18-JAN-2017, sequence version 1.
DT   27-MAR-2024, entry version 32.
DE   RecName: Full=Rad50/SbcC-type AAA domain-containing protein {ECO:0000259|Pfam:PF13476};
GN   ORFNames=LIPSTDRAFT_69941 {ECO:0000313|EMBL:ODQ74341.1};
OS   Lipomyces starkeyi NRRL Y-11557.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Lipomycetaceae; Lipomyces.
OX   NCBI_TaxID=675824 {ECO:0000313|EMBL:ODQ74341.1, ECO:0000313|Proteomes:UP000094385};
RN   [1] {ECO:0000313|EMBL:ODQ74341.1, ECO:0000313|Proteomes:UP000094385}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NRRL Y-11557 {ECO:0000313|EMBL:ODQ74341.1,
RC   ECO:0000313|Proteomes:UP000094385};
RX   PubMed=27535936; DOI=10.1073/pnas.1603941113;
RA   Riley R., Haridas S., Wolfe K.H., Lopes M.R., Hittinger C.T., Goeker M.,
RA   Salamov A.A., Wisecaver J.H., Long T.M., Calvey C.H., Aerts A.L.,
RA   Barry K.W., Choi C., Clum A., Coughlan A.Y., Deshpande S., Douglass A.P.,
RA   Hanson S.J., Klenk H.-P., LaButti K.M., Lapidus A., Lindquist E.A.,
RA   Lipzen A.M., Meier-Kolthoff J.P., Ohm R.A., Otillar R.P., Pangilinan J.L.,
RA   Peng Y., Rokas A., Rosa C.A., Scheuner C., Sibirny A.A., Slot J.C.,
RA   Stielow J.B., Sun H., Kurtzman C.P., Blackwell M., Grigoriev I.V.,
RA   Jeffries T.W.;
RT   "Comparative genomics of biotechnologically important yeasts.";
RL   Proc. Natl. Acad. Sci. U.S.A. 113:9882-9887(2016).
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; KV454292; ODQ74341.1; -; Genomic_DNA.
DR   STRING; 675824.A0A1E3Q9I7; -.
DR   OrthoDB; 5477220at2759; -.
DR   Proteomes; UP000094385; 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; 2.
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:UP000094385};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT   DOMAIN          6..230
FT                   /note="Rad50/SbcC-type AAA"
FT                   /evidence="ECO:0000259|Pfam:PF13476"
FT   COILED          194..339
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          405..432
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          501..528
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          570..608
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          758..806
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          843..915
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   1321 AA;  152265 MW;  535972E885C698CA CRC64;
     MSSIQKLSIQ GVRSFDNAER ETIHFYAPLT LIVGHNGSGK TTIIECLRYA TTGDLPPQNK
     GGAFIHDPRI AGEKEVMAQV KLGFTSTNGM QMICTRSMQL TMKKTTRTFK TLDGQLLVMH
     NGQRETISTR CAELDAQLPQ YLGVSKAILD YVVFCHQDES LWPLSEPAVL KKRFDEIFEA
     LKYTKALDTI KSLRKEFATE IRLLQNDVDH LKNDKDRADK IRARADQLKS GIEKTKEEAS
     ILGREMQHVE GQLNTLFKSG QEFQKVLSEL DQKRAHLAAL NEQALELEST IEVLRDSDED
     LEKKKAEFSD HIHTRQEELR ELRNTVEKAK QELIHVRSKH SDALVQEGKL NAEAEAQKGR
     LKKRQDLVKE ISDRHNIAGF GIMDLDRRQI DAFREKLMGA IRSSTNQVQR NKAEAEDQIG
     SIQSKIQQIR EEKSSYEMRY KLSKNSNDKR QDDVRKLQAS IDAVTVEEAD IVYHASQLKS
     AEQQLGDQRA AFEQANFTAQ QTEKAENLKD VERKLDAVSD ELTRSNKQTE MRANLGILHK
     NSNSRDEQLN AVINTNRAKF KAFTGAELQR NTVEKQFRTA QERLQDTLNE ATRSYESCAK
     ELSKIETQYS IVKGDLQKKS LERERSTKVF QDIVSPENGD DDYARAFQDC LRDAEKTVER
     DRRNLNQCDF ILAYYRKARD SAMQKHECNL CRRPLKDRRD EIEDSDDLGH TTELEIFCEL
     MDAQIEYFGN KSQLVDRLEE SEKILEETRG AAPHVTKMEE LDAVIPDLKA QLVQLESRLD
     TAGREVEKST SEIADVRQRI SELESLRKVV NDIVRFTSEI SDMNLEIESY TSQLSDTGIG
     RSVDEIEAER QHLNALASQY RKELTRITDE RDRQRTQINV LENQSRDKKA VLNDKKTKLQ
     AKNDLISRAE ELRKETADTV SKMEQVKTHI NTMDPLLQSH AHDLEQTRSH FNKIESEKMK
     EVADLNASLQ KFMAVHADIG KYEENGGDSR LEHAQQRTQK YANRMKTLVE ETDQLMERAN
     LQDKELTSID MQERQISDNI LLRSLHDRIE ETRSRICELE QKNAIQERDA FEKKAQQLRI
     HHARLNADYG SKVGEIKQMD DQFKRYEDEL RTEFLNVHET YRETLIKLKT TTASSEDLAK
     YGKALDSGIM KYHSLKMEEI NRIIDELWKK TYSGTDVDTI LIRSDDESAK GNRSYNYRVC
     MVKQDVELDM RGRCSAGQKV LASIIIRLAL AECFGVNCGI IALDEPTTNL DQENVQSLAR
     SLGSIIDARR AQRNFQLIVI THDEDFLRYM NGSDYCEYYF RVSRNERQKS QIERQKISEV
     F
//
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