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Database: UniProt
Entry: A8PTI8_MALGO
LinkDB: A8PTI8_MALGO
Original site: A8PTI8_MALGO 
ID   A8PTI8_MALGO            Unreviewed;      1164 AA.
AC   A8PTI8;
DT   15-JAN-2008, integrated into UniProtKB/TrEMBL.
DT   15-JAN-2008, sequence version 1.
DT   24-JAN-2024, entry version 70.
DE   RecName: Full=Rad50/SbcC-type AAA domain-containing protein {ECO:0000259|Pfam:PF13476};
GN   ORFNames=MGL_0431 {ECO:0000313|EMBL:EDP45442.1};
OS   Malassezia globosa (strain ATCC MYA-4612 / CBS 7966) (Dandruff-associated
OS   fungus).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Ustilaginomycotina;
OC   Malasseziomycetes; Malasseziales; Malasseziaceae; Malassezia.
OX   NCBI_TaxID=425265 {ECO:0000313|EMBL:EDP45442.1, ECO:0000313|Proteomes:UP000008837};
RN   [1] {ECO:0000313|EMBL:EDP45442.1, ECO:0000313|Proteomes:UP000008837}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC MYA-4612 / CBS 7966 {ECO:0000313|Proteomes:UP000008837};
RX   PubMed=18000048; DOI=10.1073/pnas.0706756104;
RA   Xu J., Saunders C.W., Hu P., Grant R.A., Boekhout T., Kuramae E.E.,
RA   Kronstad J.W., Deangelis Y.M., Reeder N.L., Johnstone K.R., Leland M.,
RA   Fieno A.M., Begley W.M., Sun Y., Lacey M.P., Chaudhary T., Keough T.,
RA   Chu L., Sears R., Yuan B., Dawson T.L.Jr.;
RT   "Dandruff-associated Malassezia genomes reveal convergent and divergent
RT   virulence traits shared with plant and human fungal pathogens.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:18730-18735(2007).
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:EDP45442.1}.
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DR   EMBL; AAYY01000001; EDP45442.1; -; Genomic_DNA.
DR   RefSeq; XP_001732656.1; XM_001732604.1.
DR   AlphaFoldDB; A8PTI8; -.
DR   STRING; 425265.A8PTI8; -.
DR   GeneID; 5856962; -.
DR   KEGG; mgl:MGL_0431; -.
DR   VEuPathDB; FungiDB:MGL_0431; -.
DR   InParanoid; A8PTI8; -.
DR   OMA; NIIFCHQ; -.
DR   OrthoDB; 5477220at2759; -.
DR   Proteomes; UP000008837; Unassembled WGS sequence.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR   GO; GO:0006302; P:double-strand break repair; 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   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   4: Predicted;
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008837};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT   DOMAIN          5..165
FT                   /note="Rad50/SbcC-type AAA"
FT                   /evidence="ECO:0000259|Pfam:PF13476"
FT   REGION          830..856
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          137..188
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          328..373
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          488..515
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          626..681
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          937..1015
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        832..856
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1164 AA;  132388 MW;  8FD1326CD52C30FC CRC64;
     MAGTDTVKAQ VRLRFRNTSG TRMSCVRNLQ VTKKKGGGLT MKTLEGVLGI DDDAADPQAR
     ASISTRCAEL DQEMASLLGV SHAILENVLF CHQEESNWPL SEPAILKKRF DEIFEVSRYT
     KALDSIRALR KQRAQDARVD EAELRALQNE KERAENIRAT IRTLEASLSA KKNERDDLDA
     AIQRKTTENQ QLYDDATRFR EVVNQAEMLE EKIALCEEHK ASLLSRMTLL AMPDSELQDE
     LTALPTQLET QHARLSHVRS NMQVYVDKRS SAAEEHERLV RRHAELETAE RTRQRVLQAT
     AKELRTFGSD ISSAPTKAQF DACSTMCEAS LREKLQEHEI KAEQHQRAAD ELESQALTEY
     EHLETRLRDL KSQREHTGAS LQRLHERIMS CENQLARQAS TTSVCELDKA RERLAELGSV
     SLPDVQEAME HLATLEAERD AIATSFVDSQ QDTKHVARQE ELASKLPVLR ERENLWRQMC
     VERLGHVPKN LEEELEQAEH VLDQSQAQLL KASEQVVQWA TTVDVYQDVL SRSEKLCSSL
     RVAKQTLLGD FASVDAGLVT VQEEIQVLQE SLFLLEHASA FFERIQHHAH ARHMCLACNR
     DISSSQLQSV DAHIEETRQR KQPEKVAVLE QDLDAWNRQL SNLYAARAIE KQLREQQEPE
     LSRLVAQLED AKKCHQDAEG ERDRSSGATA SAVARVKTLR SLQVPMYRLV DLRLDVQLLK
     RQLDSIASTS ASATTSNASP ESLKALSQEI HAQQAHCHEL REQCDQHRNR VREAERHVHA
     LEMQLMTEQQ HAAATQTAHQ RLEEYMADAK DLEKQRETLT FTINELTQPL SEAQKHLEDT
     RRERREQEER YKEKRSDLEQ QLAKLAGMVQ RVSSAWDEAE ADGGTLVSCS IELDRAAQAL
     QHTQKEAERA TQDTYALETA IHDVRAREAN LQDNMRYRQV LRELEHVTAE LNKLDLEAAH
     MRHKRASSAY DAARREENEL SGRAAHIRGE IQGIEAELQR REAELRHDYK DISNRYMRQL
     VHIKVAGMAN HDLDIYCGAL QQAILQYHAI KMEEVNQTLD YLWKKTYQGT DIDSISIRSD
     TEGRVSANGL RSYQYRVCMV KDAVELDMRG RCSAGQKVLA CILIRLALAD SFGGSCGFMA
     LDEPTANLDR ENVEGLAASL IEYV
//
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