ID A8PXI0_MALGO Unreviewed; 1065 AA.
AC A8PXI0;
DT 15-JAN-2008, integrated into UniProtKB/TrEMBL.
DT 15-JAN-2008, sequence version 1.
DT 27-MAR-2024, entry version 81.
DE RecName: Full=Structural maintenance of chromosomes protein 5 {ECO:0000256|ARBA:ARBA00018687};
GN ORFNames=MGL_1451 {ECO:0000313|EMBL:EDP44054.1};
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:EDP44054.1, ECO:0000313|Proteomes:UP000008837};
RN [1] {ECO:0000313|EMBL:EDP44054.1, 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 -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC -!- SIMILARITY: Belongs to the SMC family. SMC5 subfamily.
CC {ECO:0000256|ARBA:ARBA00010171}.
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:EDP44054.1}.
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DR EMBL; AAYY01000004; EDP44054.1; -; Genomic_DNA.
DR RefSeq; XP_001731268.1; XM_001731216.1.
DR AlphaFoldDB; A8PXI0; -.
DR STRING; 425265.A8PXI0; -.
DR GeneID; 5855575; -.
DR KEGG; mgl:MGL_1451; -.
DR VEuPathDB; FungiDB:MGL_1451; -.
DR InParanoid; A8PXI0; -.
DR OMA; RFWTSQP; -.
DR OrthoDB; 232016at2759; -.
DR Proteomes; UP000008837; Unassembled WGS sequence.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0030915; C:Smc5-Smc6 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:0000724; P:double-strand break repair via homologous recombination; IEA:InterPro.
DR GO; GO:0000160; P:phosphorelay signal transduction system; IEA:InterPro.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR003395; RecF/RecN/SMC_N.
DR InterPro; IPR008207; Sig_transdc_His_kin_Hpt_dom.
DR InterPro; IPR027131; SMC5.
DR PANTHER; PTHR45916; STRUCTURAL MAINTENANCE OF CHROMOSOMES PROTEIN 5; 1.
DR PANTHER; PTHR45916:SF1; STRUCTURAL MAINTENANCE OF CHROMOSOMES PROTEIN 5; 1.
DR Pfam; PF02463; SMC_N; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR PROSITE; PS50894; HPT; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW DNA recombination {ECO:0000256|ARBA:ARBA00023172};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Phosphoprotein {ECO:0000256|PROSITE-ProRule:PRU00110};
KW Reference proteome {ECO:0000313|Proteomes:UP000008837}.
FT DOMAIN 264..366
FT /note="HPt"
FT /evidence="ECO:0000259|PROSITE:PS50894"
FT COILED 191..232
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 265..362
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 684..711
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 767..794
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 864..894
FT /evidence="ECO:0000256|SAM:Coils"
FT MOD_RES 303
FT /note="Phosphohistidine"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00110"
SQ SEQUENCE 1065 AA; 121614 MW; 56943EF015F83B3C CRC64;
MSSQCTSHAL GARAPRNEHG FRPGSIVRVA CEHFVTYDAV EFRPGPYLNM IIGPNGTGKS
TVVCAIALGL GWKPSVLGRA KDVASYVKLG HTQGWVEIEL QGYPPPQRNV TIKRILFRES
NTSDWILDGV AASAREVHQA VSQFNIEVGN LCAFLPQDRV ADFAAMTPQR LLQDTEHAAG
HAQLSDWHMQ LIECGRQKSE LQSRLEQEQR EHDYLEERNT VLERDVRRYE ERIALEKRVC
ALEVRIAFAE FHDSKSRYHA AHAKREEAKR ALERIFQSIE PLEQELERAQ EKLDKMELVS
SSHRREADDA SSALRRYSTA RERLDAEMAA LSEQEKRLEA QAAERRELMQ QMRSRIADLE
RAIEARATPE PLAPYEQRLR AVKAEHRMAS EDLRDMDSQS ADLYTQQQRL ASQMAEARVS
LERLHTERHQ RLQLLARADR DTFEAVQWLQ HHQDMFERTV YEPVLIAVHI NRPEAARAIE
TCLSWPIQRT FVCQTRADYD LFTHELIDKR KWRLNVVELE AARSLASYTP PIPKADLLSL
GFDAYALDCI DAPEEVLKYL CSAASLHAIP LDLRGRVRPQ DMESRQAVRR YIVADTIFTT
TTSSYGRRLP QTMSRVLKPL RSFAHTSDQQ ERQNAAAVLR HLEEQHTACQ ASIQHAKSMR
EQHAARVDSL SQQRSEAASA YQLVADAHKE SQRLELKLQS QRDRLAHEEA QPSLAVQRRE
IHATRQKYAV ELSKLAERSF RCFEAIVRSN AASDETLLAS LHACTDVQTC RASLREQQTR
IEESEQAVRA AVAEFTTIKT RTLELKRCAE QKLQEAGPDV QSLVQTSLED GRHESVEHLH
TLLDRARAQL DVPWGVGPGV METFRARKDK MAELKRTIEQ ARSEQNRLVA LIEQVEGMWL
PELEALIRAV NERFSAAFAR LGCAGEVHLA RDDNYEKWGI DILVKFRDTE RLQLLTNQRQ
SGGERSLSTI LYLLSLTELS RTPFSLVDEI NQGMDPRAER AVHDQMVAMT CQPQAGQYFL
ITPKLLPGLL YHELMKVLII NNGEWLPERL SCTLSEILLT HIHSL
//
