ID K1XKR9_MARBU Unreviewed; 1210 AA.
AC K1XKR9;
DT 28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT 28-NOV-2012, sequence version 1.
DT 24-JAN-2024, entry version 59.
DE RecName: Full=Structural maintenance of chromosomes protein {ECO:0000256|PIRNR:PIRNR005719};
GN ORFNames=MBM_00281 {ECO:0000313|EMBL:EKD21168.1};
OS Marssonina brunnea f. sp. multigermtubi (strain MB_m1) (Marssonina leaf
OS spot fungus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Helotiales; Drepanopezizaceae; Drepanopeziza.
OX NCBI_TaxID=1072389 {ECO:0000313|EMBL:EKD21168.1, ECO:0000313|Proteomes:UP000006753};
RN [1] {ECO:0000313|EMBL:EKD21168.1, ECO:0000313|Proteomes:UP000006753}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MB_m1 {ECO:0000313|EMBL:EKD21168.1,
RC ECO:0000313|Proteomes:UP000006753};
RX PubMed=22876864; DOI=10.1186/1471-2164-13-382;
RA Zhu S., Cao Y.-Z., Jiang C., Tan B.-Y., Wang Z., Feng S., Zhang L.,
RA Su X.-H., Brejova B., Vinar T., Xu M., Wang M.-X., Zhang S.-G.,
RA Huang M.-R., Wu R., Zhou Y.;
RT "Sequencing the genome of Marssonina brunnea reveals fungus-poplar co-
RT evolution.";
RL BMC Genomics 13:382-382(2012).
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|PIRNR:PIRNR005719}.
CC -!- SIMILARITY: Belongs to the SMC family. SMC3 subfamily.
CC {ECO:0000256|ARBA:ARBA00005917}.
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DR EMBL; JH921428; EKD21168.1; -; Genomic_DNA.
DR RefSeq; XP_007288170.1; XM_007288108.1.
DR AlphaFoldDB; K1XKR9; -.
DR STRING; 1072389.K1XKR9; -.
DR GeneID; 18756216; -.
DR KEGG; mbe:MBM_00281; -.
DR eggNOG; KOG0964; Eukaryota.
DR HOGENOM; CLU_001042_5_0_1; -.
DR InParanoid; K1XKR9; -.
DR OMA; DQHQSMR; -.
DR OrthoDB; 231904at2759; -.
DR Proteomes; UP000006753; Unassembled WGS sequence.
DR GO; GO:0005694; C:chromosome; IEA:InterPro.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0051276; P:chromosome organization; IEA:InterPro.
DR CDD; cd03272; ABC_SMC3_euk; 1.
DR Gene3D; 1.20.1060.20; -; 1.
DR Gene3D; 3.30.70.1620; -; 1.
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; IPR024704; SMC.
DR InterPro; IPR041741; SMC3_ABC_euk.
DR InterPro; IPR010935; SMC_hinge.
DR InterPro; IPR036277; SMC_hinge_sf.
DR PANTHER; PTHR43977; STRUCTURAL MAINTENANCE OF CHROMOSOMES PROTEIN 3; 1.
DR PANTHER; PTHR43977:SF1; STRUCTURAL MAINTENANCE OF CHROMOSOMES PROTEIN 3; 1.
DR Pfam; PF06470; SMC_hinge; 1.
DR Pfam; PF02463; SMC_N; 1.
DR PIRSF; PIRSF005719; SMC; 1.
DR SMART; SM00968; SMC_hinge; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF75553; Smc hinge domain; 1.
PE 3: Inferred from homology;
KW Cell cycle {ECO:0000256|ARBA:ARBA00022776};
KW Cell division {ECO:0000256|ARBA:ARBA00022618};
KW Coiled coil {ECO:0000256|ARBA:ARBA00023054, ECO:0000256|SAM:Coils};
KW Mitosis {ECO:0000256|ARBA:ARBA00022776};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242, ECO:0000256|PIRNR:PIRNR005719};
KW Reference proteome {ECO:0000313|Proteomes:UP000006753}.
FT DOMAIN 522..634
FT /note="SMC hinge"
FT /evidence="ECO:0000259|SMART:SM00968"
FT REGION 482..501
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1048..1070
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 186..343
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 673..707
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 780..814
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 849..918
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 482..498
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1048..1069
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1210 AA; 137567 MW; C33AA78A6EC02B43 CRC64;
MYIKQIIIQG FKSYKEQTVI EPFSPKTNVI VGRNGSGKSN FFAAIRFVLS DAYSQMGREE
RQALLHEGSG SAVMSAYVEI IFDNSDDRFP TGKEELILRR TIGLKKDEYS LDRKNATKTD
VMNLLESAGF SRSNPYYIVP QGRVTALTNM KDPERLNLLK EVAGTQVYEA RRTESLKIMT
ETSNKRGKID ESLDYIKERL AELEEEKEEL RGYQEKDRDR RCLEYAFYQR EQNALTAALD
EIEELRQHGL DGSDGNREEF IEGEKAVLQL ENEIKKLTRQ MELLKLERRQ LEEDRRETSK
SQAKAEMTVK TLTDGLSATE QARTKQQQEL KSVKQEIKSK EDELAKLLPD YTKRKAKETE
VKNNLDVAEA SRTRLYNKQG RAARFKNKAE RDSWLNAEIE TLSTALGEQK ANRINAAEEV
KAVQSEIQNV EGGIAGLRKR FEGWGESRQA LYEEVTTAKD SLEKLQDERK ILRREDDKLT
SLVQDARQER DRAEKDLSNT MDGATSRGLA AVRRLKREHN VYGAYGTVAE LLNVPENYRT
ATEQAAGASL FHYVVDNEET ATFFVDSLYQ QRAGRVTFIP MNRLRLKSNK LPNASDAIAL
IDKLDFEPEY RRAMDHVFGK VVVCPNLTIA AQYARSHQCN AITPDGDTAN RKGAMTGGYI
DPRKSRLQAV RAVNKWRDEY EALLARLEEL RKESESKDNQ INRALGVLHK LQQQLSRMDD
SFDPLQKELR TSNLQLDKLR YSLEANIRQK EVVDQMIRDH GDTLSALEAD LASPFKKALT
SDEERQLESL NTTVQDLQRE WNELSKSRRE LESRKQLLEV DLRENLRLQL DQLNTQEIDA
TAGGGSGSLK EAQRELKRVQ KAAAAVEVKL QETEAQIEEA ENNISSLRKE KAQAEEQLEE
TAKAIEKFQK KMEKSVARKA LLTSSAAECA KNIRDLGVLP DEAFEKYSDK ESKYITAKLK
KVNDALKKYK GVNKKAFEQY NSFTNQREGL IKRRKELDDG LKSIQDLVEV LDQRKDEAIE
RTFKQVSKEF AQIFERLVPA GRGRLVIQRK TDQRAPANED SEDEPRGEGV ENYTGVGISV
SFNSKHDEQQ RIQQLSGGQK SLCALALVFA IQQCDPAPFY LFDEIDANLD AQYRTAVAQM
LEDVSEQQSS QNADNGSGGM SGQFICTTFR PEMLLVANKC YGVTFHNKTS GIGAVSREEA
LKFVDGEAPK
//
