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Database: UniProt
Entry: A9A3B8_NITMS
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Original site: A9A3B8_NITMS 
ID   A9A3B8_NITMS            Unreviewed;      1174 AA.
AC   A9A3B8;
DT   15-JAN-2008, integrated into UniProtKB/TrEMBL.
DT   15-JAN-2008, sequence version 1.
DT   27-MAR-2024, entry version 83.
DE   SubName: Full=SMC domain protein {ECO:0000313|EMBL:ABX12547.1};
GN   OrderedLocusNames=Nmar_0651 {ECO:0000313|EMBL:ABX12547.1};
OS   Nitrosopumilus maritimus (strain SCM1).
OC   Archaea; Nitrososphaerota; Nitrososphaeria; Nitrosopumilales;
OC   Nitrosopumilaceae; Nitrosopumilus.
OX   NCBI_TaxID=436308 {ECO:0000313|EMBL:ABX12547.1, ECO:0000313|Proteomes:UP000000792};
RN   [1] {ECO:0000313|EMBL:ABX12547.1, ECO:0000313|Proteomes:UP000000792}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SCM1 {ECO:0000313|EMBL:ABX12547.1,
RC   ECO:0000313|Proteomes:UP000000792};
RX   PubMed=20421470; DOI=10.1073/pnas.0913533107;
RA   Walker C.B., de la Torre J.R., Klotz M.G., Urakawa H., Pinel N., Arp D.J.,
RA   Brochier-Armanet C., Chain P.S., Chan P.P., Gollabgir A., Hemp J.,
RA   Hugler M., Karr E.A., Konneke M., Shin M., Lawton T.J., Lowe T.,
RA   Martens-Habbena W., Sayavedra-Soto L.A., Lang D., Sievert S.M.,
RA   Rosenzweig A.C., Manning G., Stahl D.A.;
RT   "Nitrosopumilus maritimus genome reveals unique mechanisms for
RT   nitrification and autotrophy in globally distributed marine crenarchaea.";
RL   Proc. Natl. Acad. Sci. U.S.A. 107:8818-8823(2010).
CC   -!- SIMILARITY: Belongs to the SMC family. SMC3 subfamily.
CC       {ECO:0000256|ARBA:ARBA00005917}.
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DR   EMBL; CP000866; ABX12547.1; -; Genomic_DNA.
DR   AlphaFoldDB; A9A3B8; -.
DR   STRING; 436308.Nmar_0651; -.
DR   EnsemblBacteria; ABX12547; ABX12547; Nmar_0651.
DR   KEGG; nmr:Nmar_0651; -.
DR   eggNOG; arCOG00371; Archaea.
DR   HOGENOM; CLU_001042_2_2_2; -.
DR   InParanoid; A9A3B8; -.
DR   OrthoDB; 9143at2157; -.
DR   PhylomeDB; A9A3B8; -.
DR   Proteomes; UP000000792; Chromosome.
DR   GO; GO:0005694; C:chromosome; IEA:InterPro.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR   GO; GO:0051276; P:chromosome organization; IEA:InterPro.
DR   Gene3D; 1.20.1060.20; -; 1.
DR   Gene3D; 1.20.5.340; -; 1.
DR   Gene3D; 3.30.70.1620; -; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
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   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; 2.
DR   PIRSF; PIRSF005719; SMC; 1.
DR   SMART; SM00968; SMC_hinge; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR   SUPFAM; SSF75553; Smc hinge domain; 1.
DR   SUPFAM; SSF57997; Tropomyosin; 1.
PE   3: Inferred from homology;
KW   Coiled coil {ECO:0000256|ARBA:ARBA00023054, ECO:0000256|SAM:Coils};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000792}.
FT   DOMAIN          525..638
FT                   /note="SMC hinge"
FT                   /evidence="ECO:0000259|SMART:SM00968"
FT   REGION          824..849
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          183..217
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          271..340
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          390..480
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        834..849
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1174 AA;  133187 MW;  A55EF202055CE82B CRC64;
     MVHVKKVEIF GFKSFGFKNT TVQFEPGLVS ISGPNGSGKS NILDAIIFAM GENKPKVMRV
     DKLRSLIHDI EGNRRGPKMA RSSVHFDNSD RKIPVDSDNV EITREMDANG ENTYYLNKKK
     TNRSHILDLL DMANAGLGQL NAVQQGTVTR ISEFTSEEKR KTIEDLIGLS YFDEKKAESV
     KQLDEADRRL EIALAKMGEI KKRIDELEEE RNQKLRYDIL ERELNRYKAI AAANKLKVIS
     SQKESKESTL HSVTAEITTF DDERSILRTE IGTLESEKSK LMAEANDYTQ AKSALDTEIA
     TAMEQYEIDN SAISASKKRI EQIESRIPEI QKELEDVDSA RSDIDTQILK IKESIEQTNV
     KKNKINSDLE IVDSQRNKIL DEQSQAAAKK SEIDQKIKEL TTQLNDAKLK LSKLQHEKEE
     SKIKVESNTA KLQGLEQGIE ELTSSKTKLE SMIKNHNATI TELKSRIQKL QSKKSKIVSD
     MDEWGEILEK SNQAATRYES KIKTVKGFMH EDYTVAKLKE DAEQLGIEGL VYEMISWDKQ
     YERSILAVSS DWIKAIVVKD FATLLGIAEF ARSRKLSKLK IIPMDSIPKF KLKLPTDSGV
     IGVLSDFVRC KPAYAELKTF LFGNIILTET RESAYNVSQS GYKAVTMDGE YFEAKGGTVV
     IDIDSKISKL TKLISMSSDV DGLFQSINAV KKYLLLKKNA IKKLDDSIQL NSERLSISEQ
     SLASTNEHYS TLTPRIESAL NMKEQITTRI ADLTSRDQNI ESEVLTNESH VESLLERISI
     VEENYASGEQ ARIANELSRI NAKKAEVEKL YTTITNEYRD KASQLTTLET QDNREKSQSN
     RLHDEERSLS LEKEELQSKI NELEVQKESK NEVLVKLREK EQELIETSGS SIGQLKEFDD
     KLKVLSEKDR ELTKQINTLE RQSDSLNRDL RDLVENETKL QQILSAFGFD KDMETFDVES
     IVQGLSAELA SLNALNAKAP ETYLEVSYGY RSMSTRKNSL EEERNSIVKF IEDIEKDKRQ
     TFLDAFDKVD KEIKLIFNKM TGGNAWLELQ NEDDIFNSGI SYLIQFPNKP KRESTSISGG
     EKTLAAIVFV LALQKLKPSP FYLFDEVDAH LDAPNSERLS NILEERAKES QFIMVSLKDS
     VVQKAKLIYG VFPKNGVSNV VTYKDKRMPS VRTS
//
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