ID E0QT14_9ACTO Unreviewed; 1199 AA.
AC E0QT14;
DT 02-NOV-2010, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2010, sequence version 1.
DT 27-MAR-2024, entry version 59.
DE RecName: Full=Chromosome partition protein Smc {ECO:0000256|HAMAP-Rule:MF_01894};
GN Name=smc {ECO:0000256|HAMAP-Rule:MF_01894,
GN ECO:0000313|EMBL:EFM45353.1};
GN ORFNames=HMPREF0580_2042 {ECO:0000313|EMBL:EFM45353.1};
OS Mobiluncus mulieris ATCC 35239.
OC Bacteria; Actinomycetota; Actinomycetes; Actinomycetales; Actinomycetaceae;
OC Mobiluncus.
OX NCBI_TaxID=871571 {ECO:0000313|EMBL:EFM45353.1, ECO:0000313|Proteomes:UP000003045};
RN [1] {ECO:0000313|EMBL:EFM45353.1, ECO:0000313|Proteomes:UP000003045}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 35239 {ECO:0000313|EMBL:EFM45353.1,
RC ECO:0000313|Proteomes:UP000003045};
RA Muzny D., Qin X., Deng J., Jiang H., Liu Y., Qu J., Song X.-Z., Zhang L.,
RA Thornton R., Coyle M., Francisco L., Jackson L., Javaid M., Korchina V.,
RA Kovar C., Mata R., Mathew T., Ngo R., Nguyen L., Nguyen N., Okwuonu G.,
RA Ongeri F., Pham C., Simmons D., Wilczek-Boney K., Hale W., Jakkamsetti A.,
RA Pham P., Ruth R., San Lucas F., Warren J., Zhang J., Zhao Z., Zhou C.,
RA Zhu D., Lee S., Bess C., Blankenburg K., Forbes L., Fu Q., Gubbala S.,
RA Hirani K., Jayaseelan J.C., Lara F., Munidasa M., Palculict T., Patil S.,
RA Pu L.-L., Saada N., Tang L., Weissenberger G., Zhu Y., Hemphill L.,
RA Shang Y., Youmans B., Ayvaz T., Ross M., Santibanez J., Aqrawi P.,
RA Gross S., Joshi V., Fowler G., Nazareth L., Reid J., Worley K.,
RA Petrosino J., Highlander S., Gibbs R.;
RL Submitted (AUG-2010) 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. SMC3 subfamily.
CC {ECO:0000256|ARBA:ARBA00005917}.
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:EFM45353.1}.
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DR EMBL; AEET01000044; EFM45353.1; -; Genomic_DNA.
DR RefSeq; WP_004017115.1; NZ_GL405260.1.
DR AlphaFoldDB; E0QT14; -.
DR STRING; 871571.HMPREF0580_2042; -.
DR GeneID; 66608189; -.
DR HOGENOM; CLU_001042_2_2_11; -.
DR Proteomes; UP000003045; 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; 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.
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:UP000003045}.
FT DOMAIN 511..638
FT /note="SMC hinge"
FT /evidence="ECO:0000259|SMART:SM00968"
FT REGION 576..595
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 208..275
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT COILED 398..481
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT COILED 676..787
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT COILED 817..844
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT COILED 887..946
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT BINDING 32..39
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
SQ SEQUENCE 1199 AA; 128477 MW; C9BF7E1C2286380F CRC64;
MYLKNLTLKG FKSFANTVHM SLEPGVTCVV GPNGSGKSNV VDALAWVMGE QGAKNLRGGQ
MSDVIFAGTK TKAPLGRAEV QLTVDNTDGA LPIEYSEVTI SRTMFRSGGS EYAINGTPVR
LLDIQELLSD TGMGRQMHVI VGQGQLDTVL SASEAERRAF VEEAAGVLKH RQRKDRALRK
LESLAVNLSR VQDLTNDVGK RLGPLGKQAE AARKAARVQA ELSDATARLL ADSVSQYREK
AQSQTTSKAQ IAAHIQEVET KIAALNQKLS AVKITFDQVV PDLENLTQTW AELNQVAERL
DSLGNQAAER VKALDTAADV AQNHQVDTSE LEERLAQTLS DIAAAQALVE TRQKEVAASI
EAENTAKIAE LEVRKSIESI QRARADRREA LERLRGIVAT ATSLAEESTQ KIARLEESRR
ETQQRAAAAA AELAEISDTV PNPQQGENPL VKAEEAVAGK VATTESQVAE LRTTLASAQA
DAARWAARRE VLAGTLKPQD AGQAVLAADL SGIQGSLPEA LVVQDGWEEA IGAVFGAWSG
ALLANGIEAA ADTIRFVREH ESGQLHLLVA NPGGASCLGN PSDSPSENRE PPGKLPEGAH
WAVDLVAAHP GQKLPRVVTQ LLSGVVACAD LGTARELVGA GQATVAVTQV GDYLSTTRVL
GGGDPQAGIL RRATEFNEAS EESELATREV DKLNASLEKS KTNLRDLKTQ HQQLVAELKA
QDAQMAAAAA KVAAAKARQA TVGAEAERVA KDIAAAREEA AKRQEKLAAA QAELEAAQSQ
SGQSEETQIG ELETALTQAI AGVSAAQSAK ANAVIESSRA TDSLQSLESR AESLRRNIGK
EKAAAAAAAS AARLREKRRH RAEYVLRQSQ VASELAHAAG AAAAAQREVA QNNRESLNQE
IEMLRANLDD LQRQRGELND ASLQDQLKLT EVNAKLESLL EKAQNECGLD EDTLISEFGP
HNLVPVFDES GETVEHVPYV REEQVARKSK AAAELKRIGK VNPLALEEHA ALVARHQFLA
DQLADLKKSR NDLLDVVAEV DRQVVEVFGA AFTDVAAAFT KIFEVLFPGG EGRLELTDAK
DLLNTGIDIH ARPAGKNVKR MSLLSGGERS LAALAFLFAI FQARPSPFYV LDEVEAALDD
VNLSRLLGVF EILRQNSQLI IITHHKRTME IADALYGVTM RDGTTTVISQ RLASPHEKG
//
