GenomeNet

Database: UniProt
Entry: F3U9F0_STRSA
LinkDB: F3U9F0_STRSA
Original site: F3U9F0_STRSA 
ID   F3U9F0_STRSA            Unreviewed;      1178 AA.
AC   F3U9F0;
DT   28-JUN-2011, integrated into UniProtKB/TrEMBL.
DT   28-JUN-2011, sequence version 1.
DT   27-MAR-2024, entry version 55.
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:EGJ40255.1};
GN   ORFNames=HMPREF9393_0253 {ECO:0000313|EMBL:EGJ40255.1};
OS   Streptococcus sanguinis SK1056.
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=888820 {ECO:0000313|EMBL:EGJ40255.1, ECO:0000313|Proteomes:UP000004171};
RN   [1] {ECO:0000313|EMBL:EGJ40255.1, ECO:0000313|Proteomes:UP000004171}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SK1056 {ECO:0000313|EMBL:EGJ40255.1,
RC   ECO:0000313|Proteomes:UP000004171};
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 (MAR-2011) 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:EGJ40255.1}.
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; AFFL01000001; EGJ40255.1; -; Genomic_DNA.
DR   RefSeq; WP_002920736.1; NZ_GL890990.1.
DR   AlphaFoldDB; F3U9F0; -.
DR   PATRIC; fig|888820.3.peg.254; -.
DR   HOGENOM; CLU_001042_2_2_9; -.
DR   Proteomes; UP000004171; 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:0051301; P:cell division; IEA:UniProtKB-KW.
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; 1.20.1060.20; -; 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|HAMAP-Rule:MF_01894};
KW   Cell cycle {ECO:0000313|EMBL:EGJ40255.1};
KW   Cell division {ECO:0000313|EMBL:EGJ40255.1};
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|ARBA:ARBA00023125, ECO:0000256|HAMAP-
KW   Rule:MF_01894}; Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_01894}.
FT   DOMAIN          518..637
FT                   /note="SMC hinge"
FT                   /evidence="ECO:0000259|SMART:SM00968"
FT   COILED          167..482
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT   COILED          674..939
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   1178 AA;  132670 MW;  5E8A8AD76BEC7A46 CRC64;
     MFLKEIEIQG FKSFADKTKV VFDQGVTAVV GPNGSGKSNI TESLRWALGE SSVKSLRGGK
     MPDVIFAGTE TRKPLNYASV VVVLDNSDQF IKDAANEIRV ERHIYRSGDS EYKIDGKKVR
     LRDVHDLFMD TGLGRDSFSI ISQGKVEEIF NSKPEERRAI FEEAAGVLKY KTRRKETENK
     LSQTQDNLDR LEDIIYELES QVKPLEKQAE TAKRFLSLDG QRRELYLDVL VAQLTANKER
     LTQAEEDLRN IQQELAAYYS KRDELEVENQ TLKAKRHELN QTLSDDQASL LELTRLISDL
     ERQIDLSKLE SSQAATSRRE NEERLAALSE KLAQIESNIE DKQAELSKIA AKLADNEESI
     AALEAELEDF SDDPDQLIEH LREQYVKLMQ EEANLSNDLT SLESQLASEL KLAESKKADY
     AKLQGDLEAS QTQEQAGLEE LEIARQALKG LLADYQSQIQ LVEKLEADYK HQQTKMFELL
     DDLKNKQARS NSLEAILKNH SNFYAGVKSV LQEAGRLGGI VGAVSEKLGF DPHYQTALEI
     ALGASSQNII VEDEAAATRA IEFLKKNRAG RATFLPLTTI KPRQLPDHNR ATIEKSAGFL
     GLASSLVSYE SSLDSIFQNL LGTTAIFDTV EHARAAARQV RYQVRMVTLD GTELRTGGSY
     AGGANRNNNT IFIKPELDAL LEEIKQKNIS LKEQEEAVQI LQNQLSQAKQ VLEQIKTDGE
     QARLAEQKAN LAYEQLAKRV EELTSLKNLQ EQELAGQSAL DISEEKDRLQ TRLTEIEQEK
     ADITAEIEQV KSNKDAVQAR FDKLSSRLAE LKLQRTELTS NQRFEKNDLE RLSEEKASLE
     KEQATLELLM EQKEQSSLQK VDITILEEQL ETAKQEKIEL DQRLIRLKFE LEDLEGQSDD
     IASRLEQARH QNEELIRRQA KAEAEKDKLM DVMRRLASNL TDDYQISFEE ASSQARPLES
     LPAAESQVKD LEKAIRALGP VNLEAVEQFE EVSNRLSFLN EQRDDVLSAK NLLLETIEEM
     NDEVKERFKS TFEAIRESFK VTFRQMFGGG SADLILTEGD LLTAGVEISV QPPGKKIQSL
     NLMSGGEKAL SALALLFSII RVKTIPFVIL DEVEAALDEA NVKRFGDYLN RFDKDSQFIV
     VTHRKGTMSA ADSIYGVTMQ ESGVSKIVSV KLKDLESM
//
DBGET integrated database retrieval system