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 24-JAN-2024, entry version 131. 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}; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AJ543649; CAD66602.1; -; Genomic_DNA. DR EMBL; AE009950; AAL81967.1; ALT_INIT; Genomic_DNA. DR RefSeq; WP_014835559.1; NZ_CP023154.1. 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 PaxDb; 186497-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; 9143at2157; -. 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:0007059; P:chromosome segregation; IEA:UniProtKB-UniRule. DR GO; GO:0006260; P:DNA replication; IEA:UniProtKB-UniRule. DR GO; GO:0007062; P:sister chromatid cohesion; 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 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 NCBIfam; TIGR02169; SMC_prok_A; 1. DR NCBIfam; TIGR02168; SMC_prok_B; 1. DR PANTHER; PTHR43977; STRUCTURAL MAINTENANCE OF CHROMOSOMES PROTEIN 3; 1. DR PANTHER; PTHR43977:SF1; STRUCTURAL MAINTENANCE OF CHROMOSOMES PROTEIN 3; 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. DR SUPFAM; SSF57997; Tropomyosin; 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 //