SMC_PYRFU
ID SMC_PYRFU Reviewed; 1177 AA.
AC Q8TZY2; Q877I1;
DT 31-MAY-2011, integrated into UniProtKB/Swiss-Prot.
DT 31-MAY-2011, sequence version 2.
DT 03-AUG-2022, entry version 124.
DE RecName: Full=Chromosome partition protein Smc {ECO:0000255|HAMAP-Rule:MF_01894};
GN Name=smc {ECO:0000255|HAMAP-Rule:MF_01894}; OrderedLocusNames=PF1843;
OS Pyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1).
OC Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC Pyrococcus.
OX NCBI_TaxID=186497;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=14660695; DOI=10.1093/molbev/msh023;
RA Cobbe N., Heck M.M.S.;
RT "The evolution of SMC proteins: phylogenetic analysis and structural
RT implications.";
RL Mol. Biol. Evol. 21:332-347(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43587 / DSM 3638 / JCM 8422 / Vc1;
RX PubMed=10430560; DOI=10.1093/genetics/152.4.1299;
RA Maeder D.L., Weiss R.B., Dunn D.M., Cherry J.L., Gonzalez J.M.,
RA DiRuggiero J., Robb F.T.;
RT "Divergence of the hyperthermophilic archaea Pyrococcus furiosus and P.
RT horikoshii inferred from complete genomic sequences.";
RL Genetics 152:1299-1305(1999).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) OF 1-182 AND 1006-1177 IN COMPLEX
RP WITH ATP, AND DOMAIN.
RX PubMed=15458651; DOI=10.1016/j.cub.2004.09.044;
RA Lammens A., Schele A., Hopfner K.P.;
RT "Structural biochemistry of ATP-driven dimerization and DNA-stimulated
RT activation of SMC ATPases.";
RL Curr. Biol. 14:1778-1782(2004).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (1.63 ANGSTROMS) OF 1-182 AND 1006-1177.
RX PubMed=20600125; DOI=10.1016/j.jmb.2010.06.029;
RA Lammens A., Hopfner K.P.;
RT "Structural basis for adenylate kinase activity in ABC ATPases.";
RL J. Mol. Biol. 401:265-273(2010).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF 488-667, DNA-BINDING, SUBUNIT, AND
RP DOMAIN.
RX PubMed=21117236; DOI=10.1002/prot.22903;
RA Griese J.J., Hopfner K.P.;
RT "Structure and DNA-binding activity of the Pyrococcus furiosus SMC protein
RT hinge domain.";
RL Proteins 79:558-568(2011).
CC -!- FUNCTION: Required for chromosome condensation and partitioning (By
CC similarity). Binds single-stranded but not double-stranded DNA.
CC {ECO:0000255|HAMAP-Rule:MF_01894}.
CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_01894,
CC ECO:0000269|PubMed:15458651, ECO:0000269|PubMed:21117236}.
CC -!- INTERACTION:
CC Q8TZY2; Q8TZY3: PF1842; NbExp=3; IntAct=EBI-2505615, EBI-16033344;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01894}.
CC -!- DOMAIN: Contains large globular domains required for ATP hydrolysis at
CC each terminus and a third globular domain forming a flexible SMC hinge
CC near the middle of the molecule. These domains are separated by coiled-
CC coil structures. The N- and C-terminus interact to make up an ATP-
CC binding cassette-type ATPase domain. The SMC hinge domain mediates
CC dimerization and binds DNA. {ECO:0000255|HAMAP-Rule:MF_01894,
CC ECO:0000269|PubMed:15458651, ECO:0000269|PubMed:21117236}.
CC -!- SIMILARITY: Belongs to the SMC family. {ECO:0000255|HAMAP-
CC Rule:MF_01894}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAL81967.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AJ543649; CAD66602.1; -; Genomic_DNA.
DR EMBL; AE009950; AAL81967.1; ALT_INIT; Genomic_DNA.
DR RefSeq; WP_014835559.1; NC_018092.1.
DR PDB; 1XEW; X-ray; 2.00 A; X=1-182, Y=1006-1177.
DR PDB; 1XEX; X-ray; 2.50 A; A=1-182.
DR PDB; 3KTA; X-ray; 1.63 A; A/C=1-182, B/D=1006-1177.
DR PDB; 3NWC; X-ray; 1.70 A; A/B=488-667.
DR PDB; 4I99; X-ray; 2.30 A; A/B=1-1172.
DR PDB; 4RSJ; X-ray; 3.50 A; A/B/C/D=445-720.
DR PDB; 5XNS; X-ray; 2.01 A; A=1-201, A=973-1169.
DR PDBsum; 1XEW; -.
DR PDBsum; 1XEX; -.
DR PDBsum; 3KTA; -.
DR PDBsum; 3NWC; -.
DR PDBsum; 4I99; -.
DR PDBsum; 4RSJ; -.
DR PDBsum; 5XNS; -.
DR AlphaFoldDB; Q8TZY2; -.
DR SMR; Q8TZY2; -.
DR DIP; DIP-54374N; -.
DR IntAct; Q8TZY2; 3.
DR STRING; 186497.PF1843; -.
DR PRIDE; Q8TZY2; -.
DR EnsemblBacteria; AAL81967; AAL81967; PF1843.
DR GeneID; 41713663; -.
DR KEGG; pfu:PF1843; -.
DR PATRIC; fig|186497.12.peg.1914; -.
DR eggNOG; arCOG00371; Archaea.
DR HOGENOM; CLU_001042_2_2_2; -.
DR OrthoDB; 1023at2157; -.
DR BRENDA; 2.7.4.3; 5243.
DR EvolutionaryTrace; Q8TZY2; -.
DR Proteomes; UP000001013; Chromosome.
DR GO; GO:0005694; C:chromosome; IEA:InterPro.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0030261; P:chromosome condensation; IEA:InterPro.
DR GO; GO:0006260; P:DNA replication; IEA:UniProtKB-UniRule.
DR GO; GO:0007062; P:sister chromatid cohesion; IEA:InterPro.
DR Gene3D; 3.40.50.300; -; 2.
DR HAMAP; MF_01894; Smc_prok; 1.
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 InterPro; IPR011890; SMC_prok.
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.
DR TIGRFAMs; TIGR02169; SMC_prok_A; 1.
DR TIGRFAMs; TIGR02168; SMC_prok_B; 1.
PE 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Coiled coil; Cytoplasm; DNA-binding;
KW Nucleotide-binding; Reference proteome.
FT CHAIN 1..1177
FT /note="Chromosome partition protein Smc"
FT /id="PRO_0000409287"
FT DOMAIN 521..627
FT /note="SMC hinge"
FT COILED 167..506
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01894"
FT COILED 659..1012
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01894"
FT BINDING 34..41
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01894,
FT ECO:0000269|PubMed:15458651"
FT STRAND 3..12
FT /evidence="ECO:0007829|PDB:3KTA"
FT HELIX 13..15
FT /evidence="ECO:0007829|PDB:3KTA"
FT STRAND 20..23
FT /evidence="ECO:0007829|PDB:3KTA"
FT STRAND 26..33
FT /evidence="ECO:0007829|PDB:3KTA"
FT HELIX 39..49
FT /evidence="ECO:0007829|PDB:3KTA"
FT HELIX 56..58
FT /evidence="ECO:0007829|PDB:3KTA"
FT HELIX 63..66
FT /evidence="ECO:0007829|PDB:3KTA"
FT STRAND 80..87
FT /evidence="ECO:0007829|PDB:3KTA"
FT STRAND 93..106
FT /evidence="ECO:0007829|PDB:3KTA"
FT STRAND 112..116
FT /evidence="ECO:0007829|PDB:3KTA"
FT STRAND 119..121
FT /evidence="ECO:0007829|PDB:3KTA"
FT HELIX 123..132
FT /evidence="ECO:0007829|PDB:3KTA"
FT HELIX 137..139
FT /evidence="ECO:0007829|PDB:1XEX"
FT HELIX 150..153
FT /evidence="ECO:0007829|PDB:3KTA"
FT HELIX 156..167
FT /evidence="ECO:0007829|PDB:3KTA"
FT HELIX 170..200
FT /evidence="ECO:0007829|PDB:5XNS"
FT HELIX 210..226
FT /evidence="ECO:0007829|PDB:5XNS"
FT HELIX 232..253
FT /evidence="ECO:0007829|PDB:5XNS"
FT HELIX 257..275
FT /evidence="ECO:0007829|PDB:5XNS"
FT STRAND 276..283
FT /evidence="ECO:0007829|PDB:5XNS"
FT STRAND 285..287
FT /evidence="ECO:0007829|PDB:5XNS"
FT STRAND 292..295
FT /evidence="ECO:0007829|PDB:5XNS"
FT HELIX 307..309
FT /evidence="ECO:0007829|PDB:5XNS"
FT HELIX 315..324
FT /evidence="ECO:0007829|PDB:5XNS"
FT HELIX 326..331
FT /evidence="ECO:0007829|PDB:5XNS"
FT STRAND 335..341
FT /evidence="ECO:0007829|PDB:5XNS"
FT TURN 342..345
FT /evidence="ECO:0007829|PDB:5XNS"
FT HELIX 353..362
FT /evidence="ECO:0007829|PDB:5XNS"
FT TURN 365..367
FT /evidence="ECO:0007829|PDB:5XNS"
FT STRAND 368..373
FT /evidence="ECO:0007829|PDB:5XNS"
FT STRAND 381..389
FT /evidence="ECO:0007829|PDB:5XNS"
FT STRAND 395..401
FT /evidence="ECO:0007829|PDB:5XNS"
FT HELIX 402..412
FT /evidence="ECO:0007829|PDB:5XNS"
FT HELIX 490..505
FT /evidence="ECO:0007829|PDB:3NWC"
FT HELIX 510..514
FT /evidence="ECO:0007829|PDB:3NWC"
FT STRAND 521..525
FT /evidence="ECO:0007829|PDB:3NWC"
FT HELIX 526..529
FT /evidence="ECO:0007829|PDB:3NWC"
FT STRAND 531..533
FT /evidence="ECO:0007829|PDB:3NWC"
FT HELIX 535..537
FT /evidence="ECO:0007829|PDB:3NWC"
FT HELIX 538..545
FT /evidence="ECO:0007829|PDB:3NWC"
FT HELIX 546..550
FT /evidence="ECO:0007829|PDB:3NWC"
FT STRAND 552..556
FT /evidence="ECO:0007829|PDB:3NWC"
FT HELIX 557..569
FT /evidence="ECO:0007829|PDB:3NWC"
FT STRAND 577..579
FT /evidence="ECO:0007829|PDB:3NWC"
FT TURN 580..582
FT /evidence="ECO:0007829|PDB:3NWC"
FT STRAND 592..595
FT /evidence="ECO:0007829|PDB:3NWC"
FT HELIX 596..599
FT /evidence="ECO:0007829|PDB:3NWC"
FT HELIX 604..606
FT /evidence="ECO:0007829|PDB:3NWC"
FT HELIX 607..614
FT /evidence="ECO:0007829|PDB:3NWC"
FT STRAND 617..621
FT /evidence="ECO:0007829|PDB:3NWC"
FT HELIX 624..629
FT /evidence="ECO:0007829|PDB:3NWC"
FT TURN 630..632
FT /evidence="ECO:0007829|PDB:3NWC"
FT STRAND 633..637
FT /evidence="ECO:0007829|PDB:3NWC"
FT TURN 638..640
FT /evidence="ECO:0007829|PDB:4RSJ"
FT STRAND 649..651
FT /evidence="ECO:0007829|PDB:4RSJ"
FT STRAND 659..661
FT /evidence="ECO:0007829|PDB:3NWC"
FT HELIX 663..713
FT /evidence="ECO:0007829|PDB:4RSJ"
FT TURN 714..716
FT /evidence="ECO:0007829|PDB:4RSJ"
FT HELIX 1008..1031
FT /evidence="ECO:0007829|PDB:3KTA"
FT STRAND 1036..1042
FT /evidence="ECO:0007829|PDB:3KTA"
FT STRAND 1044..1046
FT /evidence="ECO:0007829|PDB:3KTA"
FT HELIX 1047..1049
FT /evidence="ECO:0007829|PDB:3KTA"
FT STRAND 1052..1057
FT /evidence="ECO:0007829|PDB:3KTA"
FT STRAND 1060..1062
FT /evidence="ECO:0007829|PDB:3KTA"
FT HELIX 1066..1068
FT /evidence="ECO:0007829|PDB:3KTA"
FT HELIX 1071..1088
FT /evidence="ECO:0007829|PDB:3KTA"
FT STRAND 1092..1098
FT /evidence="ECO:0007829|PDB:3KTA"
FT TURN 1099..1102
FT /evidence="ECO:0007829|PDB:3KTA"
FT HELIX 1105..1118
FT /evidence="ECO:0007829|PDB:3KTA"
FT TURN 1119..1121
FT /evidence="ECO:0007829|PDB:3KTA"
FT STRAND 1122..1127
FT /evidence="ECO:0007829|PDB:3KTA"
FT HELIX 1131..1134
FT /evidence="ECO:0007829|PDB:3KTA"
FT STRAND 1138..1146
FT /evidence="ECO:0007829|PDB:3KTA"
FT STRAND 1149..1154
FT /evidence="ECO:0007829|PDB:3KTA"
FT HELIX 1157..1168
FT /evidence="ECO:0007829|PDB:3KTA"
SQ SEQUENCE 1177 AA; 135014 MW; EC12C4C060E5A1CB CRC64;
MPYIEKLELK GFKSYGNKKV VIPFSKGFTA IVGANGSGKS NIGDAILFVL GGLSAKAMRA
SRISDLIFAG SKNEPPAKYA EVAIYFNNED RGFPIDEDEV VIRRRVYPDG RSSYWLNGRR
ATRSEILDIL TAAMISPDGY NIVLQGDITK FIKMSPLERR LLIDDISGIA EYDSKKEKAL
EELKQAEENL ARVDLLIKEV KKQLDKLEKE RNDALRYLDL KDKLEKAKVS LLLGEIKILE
TQIKEGEKRR AEIEEEIQKI EKEIEKIGKE IVEKVKVLRE IEERIEKESG EEAIQITKKI
GEVTSKIELT KRNIEVAKEE LEDAQRRLAK TKEELRKVLS EIEKSKGAIT RWKKRRDALI
NEIKKKEEER NVLVVKLGEI DKTFGAAREE FDSVVKELEE TTRKMYEIEG NIRRLQEEKE
KLHSRILFLR AKLPGIKEKI NEFKAVVEDK RAEISEIEGK LSTIQAKRIK VEKEIEAKSN
ELEKVSKELE SSERELIAAE AQREVRGNRA AEELKRSGIG GIYGTLAELI KVKDEAYALA
IEVALGNRAD NVVVEDELVA EKAIKYLKEH KLGRLTFLPL NKIKPKHVDS SVGLPAVDVI
EYDQKIENAV KFALGDTVIV NSMEEARPHI GKVRMVTIEG ELYERSGAIT GGHFRARGLA
VDTTKLREKV ESLRRRKEAL EGELNSLKIE LRSLENASFE LRIKLSDEKK ELELASKDLN
RLLEEENAVK EEIEESERKI QEIEQKIENE KSELAKLRGR IQRLERKKEK LKKALENPEA
RELMEKIRII DGEISSLKEE LSRIESRIES LESRLNEELL PRKASLEEEI EGLVNKINAL
KNNISENEKA LELLNKELEK LKSIEENIKG EIRTLREKRK KLEEDISKLR EKKEVLQRKL
QELEIEANTL KVRDAQLNAQ LEEKKYQLTH YDKNLIKSIK EIPLDLEKVK KEIEKMEEEI
RSLEPVNMKA IEDFEIVERR YLELKSKREK LEAEKESIIE FINEIEKEKK NVFMRTFEAI
SRNFSEIFAK LSPGGSARLI LENPEDPFSG GLEIEAKPAG KDVKRIEAMS GGEKALTALA
FVFAIQKFKP APFYLFDEID AHLDDANVKR VADLIKESSK ESQFIVITLR DVMMANADKI
IGVSMRDGVS KVVSLSLEKA MKILEEIRKK QGWEHGN
