ID A0A0G8AX56_9SYNE Unreviewed; 1197 AA.
AC A0A0G8AX56;
DT 16-SEP-2015, integrated into UniProtKB/TrEMBL.
DT 16-SEP-2015, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE RecName: Full=Chromosome partition protein Smc {ECO:0000256|HAMAP-Rule:MF_01894};
GN Name=smc {ECO:0000256|HAMAP-Rule:MF_01894};
GN ORFNames=TQ37_02980 {ECO:0000313|EMBL:KKZ13895.1};
OS Candidatus Synechococcus spongiarum 15L.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Synechococcales; Synechococcaceae;
OC Synechococcus.
OX NCBI_TaxID=1608419 {ECO:0000313|EMBL:KKZ13895.1, ECO:0000313|Proteomes:UP000035037};
RN [1] {ECO:0000313|EMBL:KKZ13895.1, ECO:0000313|Proteomes:UP000035037}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=15L {ECO:0000313|EMBL:KKZ13895.1};
RA Slaby B., Hentschel U.;
RL Submitted (FEB-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KKZ13895.1, ECO:0000313|Proteomes:UP000035037}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=15L {ECO:0000313|EMBL:KKZ13895.1};
RA Burgsdorf I., Slaby B.M., Handley K.M., Haber M., Blom J., Marshall C.W.,
RA Gilbert J.A., Hentschel U., Steindler L.;
RT "Lifestyle Evolution in Cyanobacterial Symbionts of Sponges.";
RL Submitted (MAY-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Required for chromosome condensation and partitioning.
CC {ECO:0000256|HAMAP-Rule:MF_01894}.
CC -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_01894}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01894}.
CC Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC -!- DOMAIN: Contains large globular domains required for ATP hydrolysis at
CC each terminus and a third globular domain forming a flexible hinge near
CC the middle of the molecule. These domains are separated by coiled-coil
CC structures. {ECO:0000256|HAMAP-Rule:MF_01894}.
CC -!- SIMILARITY: Belongs to the SMC family. {ECO:0000256|HAMAP-
CC Rule:MF_01894}.
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:KKZ13895.1}.
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; JYFQ01000064; KKZ13895.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0G8AX56; -.
DR STRING; 431041.FLM9_1266; -.
DR PATRIC; fig|1608419.3.peg.2035; -.
DR Proteomes; UP000035037; Unassembled WGS sequence.
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; 1.20.1060.20; -; 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 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 ATP-binding {ECO:0000256|HAMAP-Rule:MF_01894};
KW Coiled coil {ECO:0000256|ARBA:ARBA00023054, ECO:0000256|HAMAP-
KW Rule:MF_01894};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_01894};
KW DNA-binding {ECO:0000256|HAMAP-Rule:MF_01894};
KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_01894}.
FT DOMAIN 539..658
FT /note="SMC hinge"
FT /evidence="ECO:0000259|SMART:SM00968"
FT REGION 675..700
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 205..236
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT COILED 283..339
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT COILED 420..524
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT COILED 777..804
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT COILED 841..959
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT COILED 1004..1031
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT BINDING 33..40
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
SQ SEQUENCE 1197 AA; 135446 MW; BBC6978386583C65 CRC64;
MVYVQQVKIS CFKSFGGSVE VPLNPGFTVI TGPNGSGKSN IIDGILFCLG LASSRGMRAE
RLPDLINHRM VRQGKAAEAS VSVTFALGDW QPPEVEPDAV EVAAGPWIDP KQQEVMISRR
IRLAPGGTYS SIYAIGEEPC SLSQLQVQLR RLRIDPTGSN VVMQGDVTRI VSMGGRERRE
IIDELAGVAL FDQRIEQCRG KLTDVREHEE RCHIVEAELR NSRQRLEKDC EKARRYQQLR
HELHQSRQQE LVLLWEKSCR QRDDLVIRQA QNRQDQNVLR TRREQFTEEH HRTIRQLQEI
QDQVKALGED RLLSVQATLA GLQGRERELQ RSLQNQNQAD IEQRQHDWRS RCRQLQAAAE
ALAGANHAAQ LEVVEARCMD SERAVEQQRQ RQGALADRSG NWLQAYQQRQ QAMAALRTGI
QPLRTEQLQL QERLKQEEQQ LQDWRTQQQQ AETGHRLDQA RLDELAARKA QLRKTLEALR
TECNEGNSTL RLLQRSRQRS ERDQVQLEQD LAKLESRREA LQESRGTAAL RLILESGLPG
IHGPVAKLGE VDSPHRLALE VAAGARLNHV VVDDDQVAAQ AIALLKRHRA GRLTFLPLNR
LRAPAAQSAT ARGSLRLQGL VDRAVNLVHF EPVYGQVFAH VLGETLVFET LNQARRLLGQ
HRCVTLEGEL LERSGAMTGG SLQRRQDRPG FSRREQADEA EPLRQRLLEL GHRLSACRRE
ETEQSQTVDA VQTRLTDISC RLAAVDAEHS SVLAQQGPLA STLDQQQRHI AASAARITER
QARLQALDKE LRAQQSRLGS LEASTEDDDA QDANMVGGQW RRLQEDLKAA EAQHTANLAQ
RETLRSALRE HQLNEQRLAD QRQLLTQEGE QLKRERQALD QRRQELAAEQ RQLEKERLTM
QARLQELQQA LGERRQQRDR LEAAVAQLNR KIHESTWQQQ QLEEKQQALK DQQTGLEEQI
RLRQADLPDP CPRISDELRA AGPEALQQHV HTLEQRLNAL EPVNMLALEE LAELETRLAA
IAERLTVLQE EREGVLQRIE TMASLRKKAF MEAFTAVNGH FQQIFTQLSD GEGHLQLDDE
ADPLSGGLTL VAHPKGKVMR RLSAMSGGEK SLTALSFLFA LQRFRPSPFY ALDEVDSFLD
GVNVENLARL IAQQAQLAQF LVVSHRRPMI AASQRTIGVT QARGAHTQVI GLPTRAA
//
