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Database: UniProt
Entry: A0A1T2L6P8_9GAMM
LinkDB: A0A1T2L6P8_9GAMM
Original site: A0A1T2L6P8_9GAMM 
ID   A0A1T2L6P8_9GAMM        Unreviewed;       876 AA.
AC   A0A1T2L6P8;
DT   10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT   10-MAY-2017, sequence version 1.
DT   24-JAN-2024, entry version 25.
DE   SubName: Full=Chromosome segregation protein SMC {ECO:0000313|EMBL:OOZ40785.1};
DE   Flags: Fragment;
GN   ORFNames=BOW52_05390 {ECO:0000313|EMBL:OOZ40785.1};
OS   Solemya elarraichensis gill symbiont.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; sulfur-oxidizing symbionts.
OX   NCBI_TaxID=1918949 {ECO:0000313|EMBL:OOZ40785.1, ECO:0000313|Proteomes:UP000190198};
RN   [1] {ECO:0000313|EMBL:OOZ40785.1, ECO:0000313|Proteomes:UP000190198}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Sp-SM6 {ECO:0000313|EMBL:OOZ40785.1};
RA   Russell S.L., Corbett-Detig R.B., Cavanaugh C.M.;
RT   "Mixed transmission modes and dynamic genome evolution in an obligate
RT   animal-bacterial symbiosis.";
RL   Submitted (NOV-2016) to the EMBL/GenBank/DDBJ databases.
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:OOZ40785.1}.
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DR   EMBL; MPRK01000077; OOZ40785.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1T2L6P8; -.
DR   OrthoDB; 9808768at2; -.
DR   Proteomes; UP000190198; Unassembled WGS sequence.
DR   GO; GO:0005694; C:chromosome; IEA:InterPro.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR   GO; GO:0030261; P:chromosome condensation; IEA:InterPro.
DR   GO; GO:0007062; P:sister chromatid cohesion; IEA:InterPro.
DR   CDD; cd03278; ABC_SMC_barmotin; 1.
DR   Gene3D; 1.10.287.1490; -; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 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   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
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   Cytoplasm {ECO:0000256|ARBA:ARBA00022490}.
FT   DOMAIN          3..428
FT                   /note="RecF/RecN/SMC N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02463"
FT   DOMAIN          525..614
FT                   /note="SMC hinge"
FT                   /evidence="ECO:0000259|Pfam:PF06470"
FT   REGION          321..340
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          806..855
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          170..218
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          244..285
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          652..805
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        806..827
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   NON_TER         876
FT                   /evidence="ECO:0000313|EMBL:OOZ40785.1"
SQ   SEQUENCE   876 AA;  99392 MW;  1BFBEDB4AA29B7D4 CRC64;
     MRLEKIKLAG FKSFVDPTTA DFPTNLVGVV GPNGCGKSNI IDAVRWVMGE SSAKMLRGES
     MADVIFNGSS SRKPVGTASI ELIFDNSDGG AGGQYASYSQ ISVKRQVSRD GQSNYYLNNT
     RCRRRDITDL FLGTGLGPRS YSIIEQGMIS RVIEARPEEL RVYLEEAAGI SKYKERRRET
     ENRIRHTREN LERLDDLIEE VGKQLKNLER QAATAEKYKT FKAEERQLRG ECLALRWKSM
     HDELDVHERE IAAQENKLEA EISTQRQIES EIEQLRSDHT DANDNFNKVQ GKFYALGAEI
     ARLEQTIQYA LESRARQQAD LSQMESSLQE LNRERQQDED RLESIATTLL TQQPLLDAAE
     IEEREASEQM AASETAMQNW QTEWDGFNQQ ANEPAQLAQV ERTKINHIES EAQKLQQRLQ
     RNSEERERLQ APDLVNEIDT LENKQREAQT RLEEKQSALD AAIGRIGNMR LEQESVNRKL
     NDARAELQSS KGRLASLEAL QQAAATEGRE GADWLQKQNL AEGKRLAQSI DVSSEWRKAV
     ETVLAQHLQA ICVDDFSRYS GAVVDLEEGL VELIESAGGS QQVADDSLLN KVDSKLDLSA
     LLGSVRMADS LHDALSRRNE LKGNESFITV DGIQIGKNWM RFGREAGAQK GILEREQQIR
     ELQKTQSELE SRVESLVKEL EQHGEAIASA EAQREQQQQD FNQVNRELAD TRSQLSAKKA
     RADHLKQRLE TVEQEHQELN AMIAEGNETI ESSKERLYEA LEVIETMSSK REALVQQRDR
     IREELEQARQ QVTVKRAEVH KLSVELSTMR SQHGSLEESS QRSRNQIEQM SGRREALAES
     LSGDDSPIEE QKQKLEEQLQ SRLKVEAQLA EARKLL
//
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