ID X0CGK9_FUSOX Unreviewed; 1484 AA.
AC X0CGK9;
DT 14-MAY-2014, integrated into UniProtKB/TrEMBL.
DT 14-MAY-2014, sequence version 1.
DT 24-JAN-2024, entry version 40.
DE RecName: Full=Structural maintenance of chromosomes protein {ECO:0000256|PIRNR:PIRNR005719};
GN ORFNames=FOQG_05445 {ECO:0000313|EMBL:EXK93316.1};
OS Fusarium oxysporum f. sp. raphani 54005.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium;
OC Fusarium oxysporum species complex.
OX NCBI_TaxID=1089458 {ECO:0000313|EMBL:EXK93316.1, ECO:0000313|Proteomes:UP000030663};
RN [1] {ECO:0000313|EMBL:EXK93316.1, ECO:0000313|Proteomes:UP000030663}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=54005 {ECO:0000313|EMBL:EXK93316.1,
RC ECO:0000313|Proteomes:UP000030663};
RG The Broad Institute Genome Sequencing Platform;
RA Ma L.-J., Gale L.R., Schwartz D.C., Zhou S., Corby-Kistler H., Young S.K.,
RA Zeng Q., Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Alvarado L.,
RA Arachchi H.M., Berlin A., Brown A., Chapman S.B., Chen Z., Dunbar C.,
RA Freedman E., Gearin G., Goldberg J., Griggs A., Gujja S., Heiman D.,
RA Howarth C., Larson L., Lui A., MacDonald P.J.P., Montmayeur A., Murphy C.,
RA Neiman D., Pearson M., Priest M., Roberts A., Saif S., Shea T., Shenoy N.,
RA Sisk P., Stolte C., Sykes S., Wortman J., Nusbaum C., Birren B.;
RT "The Genome Sequence of Fusarium oxysporum PHW815.";
RL Submitted (NOV-2011) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123,
CC ECO:0000256|PIRNR:PIRNR005719}.
CC -!- SIMILARITY: Belongs to the SMC family. SMC4 subfamily.
CC {ECO:0000256|ARBA:ARBA00006005}.
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DR EMBL; JH658369; EXK93316.1; -; Genomic_DNA.
DR eggNOG; KOG0996; Eukaryota.
DR HOGENOM; CLU_001042_4_1_1; -.
DR Proteomes; UP000030663; 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 Gene3D; 1.10.287.1490; -; 2.
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; IPR010935; SMC_hinge.
DR InterPro; IPR036277; SMC_hinge_sf.
DR PANTHER; PTHR18937:SF172; STRUCTURAL MAINTENANCE OF CHROMOSOMES PROTEIN; 1.
DR PANTHER; PTHR18937; STRUCTURAL MAINTENANCE OF CHROMOSOMES SMC FAMILY MEMBER; 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|PIRNR:PIRNR005719};
KW Reference proteome {ECO:0000313|Proteomes:UP000030663}.
FT DOMAIN 730..843
FT /note="SMC hinge"
FT /evidence="ECO:0000259|SMART:SM00968"
FT REGION 1..147
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 690..709
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1076..1097
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1162..1238
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1464..1484
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 1270..1307
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 11..48
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 133..147
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1162..1177
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1186..1227
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1484 AA; 166020 MW; 89ABB1AEAC7954BB CRC64;
MSSPVRPRRA TRRTAIIDSD DEDDVSNRSR VQDEEEDFEP EKPAPRRQTR SRKSTTPAPT
PAAAPKARGR PRKAPTPAAS VEASELLDAD TTLKAEASSP AKVASPRKRK STARSSISSV
PDLAPPTPKP DSPTASQEAS ALADITDSSV NTSVVDNTQA TIKPIKPMDT IMEKPMDIVL
KSRTLAVPVV EDTTPKSRIV LTHLILNNFK SYAGRQEVGP FHASFSSVVG PNGSGKSNVI
DSLLFVFGFR ASKMRQGKIS ALIHNSAKFP NLDHCEVAVY FQEVMDQPGG GHEVIPNSEL
IISRKAFKNN SSKYYINGKE SNFTTVTTLL RDRGVDLDHK RFLILQGEVE SIAQMKAKAG
NEHEDGLLEY LEDIIGTSKY KAPIEESATE VETLNDVCME KSGRVQHVEK EKNSLEDKKD
KAIAYIRDEN ELAMKQSALY QLFIHKCNEN IAVTEEAISQ MQAQLDAELE KHHGGEQIIK
SLEKDYAKGA KEFEAQEKST QALVKEMAKF EQERVKFDEK RKFLDDKRKK LEKAIANAET
NSAEADETIE QCGEEIENRT QEIAELEEQI QTAEAELAQI RESLKGKTQA FSDQIAAKQK
SLEPWNEKIN QKQSAVAVAE SELNILQEKA NAGAVALQEL ETKIASIEEG KTAKRAELKS
CQAEKAELLK EAENMKSELK VLSEQEPKIR SKISNARQKA DEARSSLSNT QARGNVLAAL
MRMKESGRID GFHGRLGNLG TIDQKYDVAI STACGALDNF VTETVEAGQQ CIEYLRKNNV
GRGNFICLDK LRVRDMSPIQ TPENAPRLFD LVTAKEDKFR AAFYHAMQDT LVAADLAQAN
RIAYGAKRWR VVTLDGELID KSGTMSGGGS TVKRGLMSSK LVSDVSKEQV AKFESDRDGW
ETKFQEFQEY QRECETRLRE LGEQIPQLDT KMQKIGLEIE SAERNITDMQ RRMKEVSKEH
QPSATDNSRI AALQKEIAKL NKEVERLHGE TSSVEDEIKA LQDKIMEVGG EKLRAQRAKV
DSIKEEISSN NEEISNAEVR KVKAEKQKIK LAKDHAKSSK ELEAATRDLE KLENDINNQG
ERAEELQAQA EEAEEGLAAK KKELKALKSE LDEKTAELNE TRAVEIEMRN KLEENQKALL
ENQARLRHWD DKLSKIVLQN IDDLTGGSSG SRSKKPKSQP KPQMDDDDDV DMDDAPQDDV
DMTDAPQEDE EQEEDQEEEE DEEESVNGQP NELPRYTPDE LADMNERTLK GEIAALEEKT
QNVNVDLGVL AEYRRRVEEH AARASDLQTA IEQRDSAKKR CDDLRRLRLE GFMEGFSAIS
LRLKEMYQMI TMGGNAELEL VDSLDPFSEG ILFSVMPPKK SWKNISNLSG GEKTLSSLAL
VFALHHYKPT PLYVMDEIDA ALDFRNVSIV ANYIKERTKN AQFIVISLRN NMFELAARLV
GVYKVNHMTK SVTIENKDYI ARPPGHSSQQ RTQVGGNTTI LPFR
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