ID A0A1H4Z1N4_9ACTN Unreviewed; 1194 AA.
AC A0A1H4Z1N4;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, 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=SAMN05216482_6593 {ECO:0000313|EMBL:SED24073.1};
OS Streptomyces sp. PAN_FS17.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1855351 {ECO:0000313|EMBL:SED24073.1, ECO:0000313|Proteomes:UP000199275};
RN [1] {ECO:0000313|Proteomes:UP000199275}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PAN_FS17 {ECO:0000313|Proteomes:UP000199275};
RA Varghese N., Submissions S.;
RL Submitted (OCT-2016) 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 -!- 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}.
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DR EMBL; FNTN01000001; SED24073.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1H4Z1N4; -.
DR STRING; 1855351.SAMN05216482_6593; -.
DR OrthoDB; 9808768at2; -.
DR Proteomes; UP000199275; 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 CDD; cd03278; ABC_SMC_barmotin; 2.
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; TIGR02168; SMC_prok_B; 1.
DR PANTHER; PTHR43977:SF2; STRUCTURAL MAINTENANCE OF CHROMOSOMES PROTEIN; 1.
DR PANTHER; PTHR43977; 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.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW 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|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW Rule:MF_01894}; Reference proteome {ECO:0000313|Proteomes:UP000199275}.
FT DOMAIN 512..633
FT /note="SMC hinge"
FT /evidence="ECO:0000259|SMART:SM00968"
FT REGION 309..334
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 949..975
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 167..201
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT COILED 241..275
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT COILED 664..698
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT COILED 748..775
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT COILED 821..890
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT COILED 981..1043
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT COMPBIAS 315..334
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 32..39
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
SQ SEQUENCE 1194 AA; 129648 MW; FB06AC7C7D0A758B CRC64;
MHLKALTLRG FKSFASATTL RFEPGITCVV GPNGSGKSNV VDALSWVMGE QGAKSLRGGK
MEDVIFAGTT GRPPLGRAEV SLTIDNSDGA LPIEYSEVTI TRIMFRNGGS EYQINGDTCR
LLDIQELLSD SGIGREMHVI VGQGQLDSVL HADPMGRRAF IEEAAGVLKH RKRKEKALRK
LDAMQANLAR VQDLTDELRR QLKPLGRQAA VARRAAVIQA DLRDARLRLL ADDLVRLREA
LRTEVADEAA LKERKEAAEQ ELKKALQREA LLEDEVRRLT PRLQQAQQTW YELSQLAERV
RGTISLADAR VKSATSAPPE ERRGRDPEDM EREAARIREQ EAELEAALEA AERALEDTVA
HRAELERELG LEERRLKDVA RAIADRREGL ARLNGQVNAA RSRAASAQSE IDRLAAARDE
AQERAFAAQE EYEALKAEVD GLDAGDAELG ERHDAAKAQL AEAEAALTAA REAATAAERR
RAATQARHEA LALGLRRKDG TGALLGAKDR LTGLLGPAAE LLTVTPGHEV ALAAAFGAAA
DAIAVTSPSA AAEAIRLLRK QDAGRASLLL AGSPEAPLRG AGNGAIGHEE PAPAGRQHAA
DLVRGPSDLM PAVRRLLHGI VVVGTLEDAE DLVYAHPQLT AVTAEGDLLG AHFAHGGSAG
APSLLEVQAS VDEAAAELEE LAVRCEELTE AQHAAAERRK ASVTLVEELG ERRRAADREK
STVAQQLGRL AGQARGAAGE AERSVAAAAR AQEALDKALM DAEELAERLA VAEEMPVDEE
PDTSVRDRLA ADGANARQTE MEARLQVRTH EERVKGLAGR ADSLDRAARA EREARARAEQ
RRARLRHEAA VAEAVASGAR QLLAHVEVSL ARAEEERGAA EAAKALREQE LTAARGAGRD
LKAELDKLTD SVHRGEVLGA EKRMRIEQLE TKALEELGVE PAGLVSEYGP HQLVPPSLAA
EGEQLPDDPE HPRNQPKAFV RAEQEKRLKA AERAYQQLGK VNPLALEEFA ALEERHKFLS
EQLEDLKKTR ADLLQVVKEV DERVEQVFTE AYWDTAREFE GVFSRLFPGG EGRLILTDPD
NMLTTGVDVE ARPPGKKVKR LSLLSGGERS LTAVAMLVSI FKARPSPFYV MDEVEAALDD
TNLQRLIRIM QELQEASQLI VITHQKRTME VADALYGVSM QGDGVSKVIS QKLR
//
