ID N1Q9E2_PSEFD Unreviewed; 1265 AA.
AC N1Q9E2;
DT 26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT 26-JUN-2013, sequence version 1.
DT 27-MAR-2024, entry version 54.
DE RecName: Full=Structural maintenance of chromosomes protein {ECO:0000256|PIRNR:PIRNR005719};
GN ORFNames=MYCFIDRAFT_85709 {ECO:0000313|EMBL:EME87512.1};
OS Pseudocercospora fijiensis (strain CIRAD86) (Black leaf streak disease
OS fungus) (Mycosphaerella fijiensis).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Dothideomycetidae; Mycosphaerellales; Mycosphaerellaceae; Pseudocercospora.
OX NCBI_TaxID=383855 {ECO:0000313|EMBL:EME87512.1, ECO:0000313|Proteomes:UP000016932};
RN [1] {ECO:0000313|EMBL:EME87512.1, ECO:0000313|Proteomes:UP000016932}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CIRAD86 {ECO:0000313|EMBL:EME87512.1,
RC ECO:0000313|Proteomes:UP000016932};
RX PubMed=23236275; DOI=10.1371/journal.ppat.1003037;
RA Ohm R.A., Feau N., Henrissat B., Schoch C.L., Horwitz B.A., Barry K.W.,
RA Condon B.J., Copeland A.C., Dhillon B., Glaser F., Hesse C.N., Kosti I.,
RA LaButti K., Lindquist E.A., Lucas S., Salamov A.A., Bradshaw R.E.,
RA Ciuffetti L., Hamelin R.C., Kema G.H.J., Lawrence C., Scott J.A.,
RA Spatafora J.W., Turgeon B.G., de Wit P.J.G.M., Zhong S., Goodwin S.B.,
RA Grigoriev I.V.;
RT "Diverse lifestyles and strategies of plant pathogenesis encoded in the
RT genomes of eighteen Dothideomycetes fungi.";
RL PLoS Pathog. 8:E1003037-E1003037(2012).
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123,
CC ECO:0000256|PIRNR:PIRNR005719}.
CC -!- SIMILARITY: Belongs to the SMC family. SMC1 subfamily.
CC {ECO:0000256|ARBA:ARBA00005597}.
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DR EMBL; KB446555; EME87512.1; -; Genomic_DNA.
DR RefSeq; XP_007920613.1; XM_007922422.1.
DR AlphaFoldDB; N1Q9E2; -.
DR STRING; 383855.N1Q9E2; -.
DR GeneID; 19342379; -.
DR KEGG; pfj:MYCFIDRAFT_85709; -.
DR eggNOG; KOG0018; Eukaryota.
DR HOGENOM; CLU_001042_0_1_1; -.
DR OrthoDB; 231904at2759; -.
DR Proteomes; UP000016932; Unassembled WGS sequence.
DR GO; GO:0008278; C:cohesin complex; 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:0007062; P:sister chromatid cohesion; IEA:InterPro.
DR CDD; cd03275; ABC_SMC1_euk; 1.
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; IPR028468; Smc1_ABC.
DR InterPro; IPR010935; SMC_hinge.
DR InterPro; IPR036277; SMC_hinge_sf.
DR PANTHER; PTHR18937:SF12; 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|ARBA:ARBA00023242, ECO:0000256|PIRNR:PIRNR005719};
KW Reference proteome {ECO:0000313|Proteomes:UP000016932}.
FT DOMAIN 552..668
FT /note="SMC hinge"
FT /evidence="ECO:0000259|SMART:SM00968"
FT REGION 82..115
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 203..395
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 433..516
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 736..812
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 837..962
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 1265 AA; 144070 MW; 04662B7B6D3D9FF4 CRC64;
MGKLLALELY NFKSYRGHHV LQFGDSYFTS IIGPNGSGKS NSMDAISFVL GIKSSHLRST
HLKDLVYRGR VMKSAKINAD GTVAEEIPNG HANDDADGGA SDEEEIDMPQ SQRNDPQTAW
VMAVYEDDAG EEQRWKRSIN AAGQSEYRIN NKPVTAKAYN ESLEAENILI KARNFLVFQG
DVEAIAAQSP KDLTRLIEQI SGSLEHKADY ERLKAEAERA DEDMRYKMKN RQGINHEIRE
YQKQKEELDK YEQTRDEKDE AVITHILWKL FHFQRTIDES TAEIAKHQAE LKEYRRSVQK
YQDRLDAVKT EQAKAGREVS KCEREIKRKE KEVEEKENQL IPIDEKLSIH ANNMKAYKTK
LASITEERDG MRQELEKREK ELQTVQKAQK RWEEKWHAEQ QNAGRELTAQ DLSEYDRLRR
EVYKRTAGDQ NKVDNITRQL KTDEETVASL KSKVDSTEAT VNSLQDEIGG LEHRRGDLQK
AIKSTGKEID SKKVAINAII SDRDRTDQKR RELEEKLFQA LTKLGDAQGY QRETQKEAAQ
SEMIRQLRQI YPGVKGQLGR QCRPKQKKYE TAVSTVLGRH YDSVIVDSEK TARECIKYLK
DAKLGLITFI PLDTIIHKQA NANLRGMHPG MRLAIDTIDY DTNLERAMSF ACGNAIVCDN
IGIAKTLVYQ RGVDAKAVAL DGTVIHKGGN ITGGDGPGDK KRKFDDAEVD NLKQLVEKFR
GDIEALPKGH KRQADEEQLR SEIDGLEAKL KYDRDELQTI ERNLASKNKE LKYHRSQLAQ
IKPQYEEQAR GVETLRETLE ESSAEVAEAE DEVFGAFCQR LGYANIREYE KQQGALQDEA
LLKQSEFKKQ LSRLENQLAF DRQRLQSVET RLRDTESKSK RDEDAIKTLQ AQKNAIAGEL
ESLNEELEAL QTLLADYQKE NDERAEKVQE ARRELQKRSK GLEATEKEIS NLQVEIQKAS
AERYGVLRKC KVENLSLPLE QGSRKLESLP QEDEILQEEE DAMDIDEDSA APVKVNDYGI
HVSFEKLDED LKEDPSEECE AGLCEKINEL QSQLDKMAPN MRSAERLEAT EARMAATDKE
FKDAKDLRTK AEKAFANVKE QRSSLFKAAY RHISEQIGPV YRELTKTQSF PLGGSASLDV
EDEEEPYLSG VKYHAMPPLK RFRDMEHLSG GEKTMAALAL LFAVHTFAPS PFFVLDEVDA
ALDHANTTQL AQYVREHAGP GMQFVVISLK PGLFENSETL VGIMRDQAVN SSRPLTLDLR
KYQHA
//
