ID A0A428UDF3_9HYPO Unreviewed; 1454 AA.
AC A0A428UDF3;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 24-JAN-2024, entry version 23.
DE RecName: Full=Structural maintenance of chromosomes protein {ECO:0000256|PIRNR:PIRNR005719};
GN ORFNames=CEP52_002485 {ECO:0000313|EMBL:RSM12336.1};
OS Fusarium oligoseptatum.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium;
OC Fusarium solani species complex.
OX NCBI_TaxID=2604345 {ECO:0000313|EMBL:RSM12336.1, ECO:0000313|Proteomes:UP000287144};
RN [1] {ECO:0000313|EMBL:RSM12336.1, ECO:0000313|Proteomes:UP000287144}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL62579 {ECO:0000313|EMBL:RSM12336.1,
RC ECO:0000313|Proteomes:UP000287144};
RA Stajich J.E., Carrillo J., Kijimoto T., Eskalen A., O'Donnell K.,
RA Kasson M.;
RT "Comparative genomic analysis of Ambrosia Fusariam Clade fungi.";
RL Submitted (JUN-2017) 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}.
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:RSM12336.1}.
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DR EMBL; NKCK01000014; RSM12336.1; -; Genomic_DNA.
DR STRING; 1325735.A0A428UDF3; -.
DR Proteomes; UP000287144; 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; -; 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; 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; 2.
DR PIRSF; PIRSF005719; SMC; 1.
DR SMART; SM00968; SMC_hinge; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR SUPFAM; SSF75553; Smc hinge domain; 1.
DR SUPFAM; SSF57997; Tropomyosin; 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:UP000287144}.
FT DOMAIN 705..818
FT /note="SMC hinge"
FT /evidence="ECO:0000259|SMART:SM00968"
FT REGION 1..163
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1139..1207
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1434..1454
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 373..400
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 468..688
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 879..1099
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 1241..1278
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 14..52
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 91..107
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 134..162
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1159..1196
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1454 AA; 163134 MW; 19D4CE4BB185E499 CRC64;
MSGASPTRPT RRATRRTAII DSDDEDDLVS NRSRIQEEEE DYEPEPQKSP RRQTRGGRKS
STPAAAPKPK GRTRKSAAST ASIEPSEVFD ADSTIKPEPE SAKKPAPRKR KSAATRSSIG
SIPDLPPPTP QGSSPDTSRI EASQADTSTS SVNTTTVDDT QATIKPIKPM DTIMEKPMDI
VLKSRTVTIP VVEDTTPKAR ISYAGRQEVG PFHASFSSVV GPNGSGKSNV IDSLLFVFGF
RASKMRQGKI SALIHNSAQH PNLDHCEVAV HFQEVMDQPG AFKNNSSKYY INGKESNFTT
VTTLLKDRGV DLDHKRFLIL QGEVESIAQM KPKAANEHDD GLLEYLEDII GTSKYKTPIE
ESAAEVETLN DVCMEKSGRV QHVEKEKNSL EDKKDKAIAY IRDENELAMK QSALYQLFLH
KCSENVAVTQ EAISQMQAQL DAELEKHHGS EQIIKSLKND HEMGAKEFEI KEKQAQALVK
EMSKFEQERV KFDEKRKFLE DKRKKLEKTI ANAETTSAEA DETIEQCGED IEIRTQAIGE
LEEQIQTAEA ELAKIRDSLK GKTQAFSDQI AALQKSLEPW MEKINQKQSA IAVAESELSI
LQEKANAGAV ALEELEAKIV SIEENKAAKK KELKSCQAEK GELLKEAAKM ESELQVLSEQ
EPKIRSKISN ARQKADEARS SLSNTQARGN VLAALMRMKE SGRIDGFHGR LGNLGTIDQK
YDVAISTACG ALDNFVTETV EAGQQCIEYL RKNNVGRGNF ICLDKLRVRD LKPIQTPENA
PRLFDLVQAK EDKFRPAFYH AMQDTLVATD LAQANRIAYG AKRWRVVTLD GELIDKSGTM
SGGGTTVKRG LMSSKLVSDV SKDQVAKLES DRDGWEAKFQ EFQEYQRECE TRLRELNEQI
PQLDTKMQKL NLEIESAERN VADLQRRIKE VSKEHQPSAT DNSRIATLQK EIAKLNKEVE
RLHEETSSVE EEIKALQDKI MEVGGEKLRA QRAKVDAIKE EISTNNEEIS NAEVRKVKAE
KQRIKLEKDQ AKSTKELEAA ARDLEKLEND INNQGEIAEQ LQAQVEEAEQ GLAAKKKELK
SLKKELDEKT DELNETRAVE IEMRNKLEEN QKVLVENQRR LRHWDDKLSK LVLQNIDDLI
GGPSQSRSRA KVKPEPSDDG DVDMDDAPQD DVDMTDAPQE DEEGEEEEEN EGDEDEHNGQ
PSELPRYTPD ELADMREETL KGEIAALEEK TQNVNVDLSV LSEYRRRVEE HAARSSDLQS
AIAQRDVAKK RCDDLRRLRL EGFMEGFSAI SLRLKEMYQM ITMGGNAELE LVDSLDPFSE
GILFSVMPPK KSWKNISNLS GGEKTLSSLA LVFALHHYKP TPLYVMDEID AALDFRNVSI
VANYIKERTK NAQFIVISLR NNMFELAARL VGVYKVNHMT KSVTIENKDF IVRPQGHQQQ
RAQGGNPTTT LPFR
//