SMC3_PLAF7
ID SMC3_PLAF7 Reviewed; 1193 AA.
AC Q8I1U7;
DT 03-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 127.
DE RecName: Full=Structural maintenance of chromosomes protein 3 homolog;
GN Name=PFD0685c {ECO:0000312|EMBL:CAD49177.1};
OS Plasmodium falciparum (isolate 3D7).
OC Eukaryota; Sar; Alveolata; Apicomplexa; Aconoidasida; Haemosporida;
OC Plasmodiidae; Plasmodium; Plasmodium (Laverania).
OX NCBI_TaxID=36329;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=3D7;
RX PubMed=12368864; DOI=10.1038/nature01097;
RA Gardner M.J., Hall N., Fung E., White O., Berriman M., Hyman R.W.,
RA Carlton J.M., Pain A., Nelson K.E., Bowman S., Paulsen I.T., James K.D.,
RA Eisen J.A., Rutherford K.M., Salzberg S.L., Craig A., Kyes S., Chan M.-S.,
RA Nene V., Shallom S.J., Suh B., Peterson J., Angiuoli S., Pertea M.,
RA Allen J., Selengut J., Haft D., Mather M.W., Vaidya A.B., Martin D.M.A.,
RA Fairlamb A.H., Fraunholz M.J., Roos D.S., Ralph S.A., McFadden G.I.,
RA Cummings L.M., Subramanian G.M., Mungall C., Venter J.C., Carucci D.J.,
RA Hoffman S.L., Newbold C., Davis R.W., Fraser C.M., Barrell B.G.;
RT "Genome sequence of the human malaria parasite Plasmodium falciparum.";
RL Nature 419:498-511(2002).
RN [2] {ECO:0000312|EMBL:CAD49177.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=3D7;
RX PubMed=12368867; DOI=10.1038/nature01095;
RA Hall N., Pain A., Berriman M., Churcher C.M., Harris B., Harris D.,
RA Mungall K.L., Bowman S., Atkin R., Baker S., Barron A., Brooks K.,
RA Buckee C.O., Burrows C., Cherevach I., Chillingworth C., Chillingworth T.,
RA Christodoulou Z., Clark L., Clark R., Corton C., Cronin A., Davies R.M.,
RA Davis P., Dear P., Dearden F., Doggett J., Feltwell T., Goble A.,
RA Goodhead I., Gwilliam R., Hamlin N., Hance Z., Harper D., Hauser H.,
RA Hornsby T., Holroyd S., Horrocks P., Humphray S., Jagels K., James K.D.,
RA Johnson D., Kerhornou A., Knights A., Konfortov B., Kyes S., Larke N.,
RA Lawson D., Lennard N., Line A., Maddison M., Mclean J., Mooney P.,
RA Moule S., Murphy L., Oliver K., Ormond D., Price C., Quail M.A.,
RA Rabbinowitsch E., Rajandream M.A., Rutter S., Rutherford K.M., Sanders M.,
RA Simmonds M., Seeger K., Sharp S., Smith R., Squares R., Squares S.,
RA Stevens K., Taylor K., Tivey A., Unwin L., Whitehead S., Woodward J.R.,
RA Sulston J.E., Craig A., Newbold C., Barrell B.G.;
RT "Sequence of Plasmodium falciparum chromosomes 1, 3-9 and 13.";
RL Nature 419:527-531(2002).
RN [3] {ECO:0000305}
RP SYNTHESIS OF 779-816, AND POSSIBLE CANDIDATE MALARIA EPITOPE.
RX PubMed=17653272; DOI=10.1371/journal.pone.0000645;
RA Villard V., Agak G.W., Frank G., Jafarshad A., Servis C., Nebie I.,
RA Sirima S.B., Felger I., Arevalo-Herrera M., Herrera S., Heitz F.,
RA Baecker V., Druilhe P., Kajava A.V., Corradin G.;
RT "Rapid identification of malaria vaccine candidates based on alpha-helical
RT coiled coil protein motif.";
RL PLoS ONE 2:E645-E645(2007).
CC -!- FUNCTION: Central component of cohesin, a complex required for
CC chromosome cohesion during the cell cycle. The cohesin complex may form
CC a large proteinaceous ring within which sister chromatids can be
CC trapped. At anaphase, the complex is cleaved and dissociates from
CC chromatin, allowing sister chromatids to segregate. Cohesion is coupled
CC to DNA replication and is involved in DNA repair. The cohesin complex
CC also plays an important role in spindle pole assembly during mitosis
CC and in chromosomes movement (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Component of the cohesin complex.
CC {ECO:0000250|UniProtKB:P32908}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P32908}.
CC -!- DOMAIN: The flexible SMC hinge domain, which separates the large
CC intramolecular coiled coil regions, allows the heterotypic interaction
CC with the corresponding domain of SMC1A or SMC1B, forming a V-shaped
CC heterodimer. The two heads of the heterodimer are then connected by
CC different ends of the cleavable RAD21 protein, forming a ring structure
CC (By similarity). {ECO:0000250|UniProtKB:P32908}.
CC -!- PTM: Acetylation at Lys-101 by ESCO1 is important for genome stability
CC and S phase sister chromatid cohesion. {ECO:0000250}.
CC -!- BIOTECHNOLOGY: Possible candidate for an effective malaria vaccine as
CC determined by epitope response in sera. {ECO:0000269|PubMed:17653272}.
CC -!- SIMILARITY: Belongs to the SMC family. SMC3 subfamily. {ECO:0000255}.
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DR EMBL; AL844503; CAD49177.1; -; Genomic_DNA.
DR RefSeq; XP_001351448.1; XM_001351412.1.
DR AlphaFoldDB; Q8I1U7; -.
DR SMR; Q8I1U7; -.
DR BioGRID; 1207895; 8.
DR IntAct; Q8I1U7; 7.
DR STRING; 5833.PFD0685c; -.
DR PRIDE; Q8I1U7; -.
DR EnsemblProtists; CAD49177; CAD49177; PF3D7_0414000.
DR GeneID; 812569; -.
DR KEGG; pfa:PF3D7_0414000; -.
DR VEuPathDB; PlasmoDB:PF3D7_0414000; -.
DR HOGENOM; CLU_001042_5_0_1; -.
DR InParanoid; Q8I1U7; -.
DR OMA; KTQDEDN; -.
DR PhylomeDB; Q8I1U7; -.
DR Proteomes; UP000001450; Chromosome 4.
DR GO; GO:0000785; C:chromatin; ISS:UniProtKB.
DR GO; GO:0000228; C:nuclear chromosome; ISS:GeneDB.
DR GO; GO:0034990; C:nuclear mitotic cohesin complex; ISS:UniProtKB.
DR GO; GO:0005524; F:ATP binding; ISS:GeneDB.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0140664; F:ATP-dependent DNA damage sensor activity; IEA:InterPro.
DR GO; GO:0061775; F:cohesin loading activity; IBA:GO_Central.
DR GO; GO:0003690; F:double-stranded DNA binding; IBA:GO_Central.
DR GO; GO:0003680; F:minor groove of adenine-thymine-rich DNA binding; ISS:UniProtKB.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0051276; P:chromosome organization; ISS:GeneDB.
DR GO; GO:0007064; P:mitotic sister chromatid cohesion; IBA:GO_Central.
DR GO; GO:0000070; P:mitotic sister chromatid segregation; ISS:UniProtKB.
DR GO; GO:0006275; P:regulation of DNA replication; ISS:UniProtKB.
DR CDD; cd03272; ABC_SMC3_euk; 1.
DR Gene3D; 3.40.50.300; -; 2.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR038729; Rad50/SbcC_AAA.
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 Pfam; PF13476; AAA_23; 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; SSF52540; 1.
DR SUPFAM; SSF75553; SSF75553; 1.
PE 1: Evidence at protein level;
KW Acetylation; ATP-binding; Cell cycle; Cell division; Coiled coil; Mitosis;
KW Nucleotide-binding; Nucleus; Reference proteome.
FT CHAIN 1..1193
FT /note="Structural maintenance of chromosomes protein 3
FT homolog"
FT /id="PRO_0000365117"
FT DOMAIN 505..631
FT /note="SMC hinge"
FT COILED 179..286
FT /evidence="ECO:0000255"
FT COILED 332..483
FT /evidence="ECO:0000255"
FT COILED 665..993
FT /evidence="ECO:0000255"
FT BINDING 31..38
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT MOD_RES 101
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250"
SQ SEQUENCE 1193 AA; 141225 MW; F4EB7581C3DAFDE8 CRC64;
MYIKQIRLKG FRTYKNETTI DFTRGINCIV GFNGSGKSNI LLAIEFILSD VCEYKQIYLH
EGIGNAVRNC YVEIIFDNSE KYFSMFKESE IKIKKVLENM KCEIFVNDKN ISKNQYVELL
ESCGLCINNL YNIIKQGQII KLSNMKDEEI LNYLKSILGA KIFEEKKKDA LSMLKECDSK
KVTIEKEFND MNSKLESLQE EFENFLEYKK LEKEKVHLDY FLNEINYKNI YEETQMLKSK
LQELKNKTQD EDNHLNLSNN NKSEYNEKLN KMKLEIASCQ NHLNKTISED IQNKRNIVHL
QMLIDEKIKE KNIKESQNKN RIKNINQINE FILRVNEKLQ SLKSDIVSKE KQIENKNNEI
NMLLSKNKNK NTDANYSHNV KKIEKMINDI NIELSFLEKE TIKNEKYLKE LEEESKVLNK
SIKENETLSQ KYGSEINELN NKSEKCVEQK RQCQQKISEG TTNLNEIKCQ IIEVNDKYDE
IIKSSNKEIL KIVDLIMAEK SIKRENILGF LIDNINVDKT YVKAVDTILE NHYFTLIVED
MQTAKKIVEF IEKKREERTS KEFNFKEFYF GKLTIVPLLN IKKFNEFNYP NDKNIVPLIK
CVNYNSKIYE FLKNILFKTI IVKSLESCEN YLEDNYNCVN IDGDYLSKHG FMYGGYNKKK
YGIYTVYNKL KELKEEEKKE KSHIEELNNN IEKIDDELRN IYDTKSSTVA KKNGCASTIN
SINNNIYSNE ENIRLTSEKI NYIQEKKQNL EQHKDQLKMQ ILQLRNNNVN PDESEKVGST
DINSLNDEVK KLKEELNKIR NEYDDFKNKL ELLYQKRNEN DSSIYMEEYE DVDIDEYNND
LADKKDHSDK IEKEKIHYEQ KIREINKEME NVKSSIDKIL INEKKHKKKI LDLCHQMNQI
NEELRILEGK EENIRKKKVL LPQGIQELEE YRTYDKQQLS AKLKSVTMEL KKYSNVNEKA
GDRLNILMND FNELKKRHEE INSSHKNIKD MIQHIGKKKD EALEATYVKI NKYFSEYFSL
LFKNRKASLV LKKMNEKEYK EKLQEMSEKR IKRRIIDEEV YIDKITGISI NITSNDDEKM
TYTIQELSGG ERSIVAICLF LCLNKIDNFS FFFFDEIDAA LDTIHRDNLS LLLKELAHRG
TQFIITTFRK ELLEYSDNMY IVKIVDRESY ISKGTKNEAY EIISIEEKHA LEN
