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Database: UniProt
Entry: A0A1Z4R0J2_9CYAN
LinkDB: A0A1Z4R0J2_9CYAN
Original site: A0A1Z4R0J2_9CYAN 
ID   A0A1Z4R0J2_9CYAN        Unreviewed;       563 AA.
AC   A0A1Z4R0J2;
DT   27-SEP-2017, integrated into UniProtKB/TrEMBL.
DT   27-SEP-2017, sequence version 1.
DT   27-MAR-2024, entry version 37.
DE   RecName: Full=Carboxysome assembly protein CcmM {ECO:0000256|ARBA:ARBA00023636};
DE   AltName: Full=Carbon dioxide concentrating mechanism protein CcmM {ECO:0000256|ARBA:ARBA00030397};
GN   ORFNames=NIES4101_71030 {ECO:0000313|EMBL:BAZ41141.1};
OS   Calothrix sp. NIES-4101.
OC   Bacteria; Cyanobacteriota; Cyanophyceae; Nostocales; Calotrichaceae;
OC   Calothrix.
OX   NCBI_TaxID=2005461 {ECO:0000313|EMBL:BAZ41141.1, ECO:0000313|Proteomes:UP000290974};
RN   [1] {ECO:0000313|EMBL:BAZ41141.1, ECO:0000313|Proteomes:UP000290974}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NIES-4101 {ECO:0000313|EMBL:BAZ41141.1,
RC   ECO:0000313|Proteomes:UP000290974};
RA   Hirose Y., Shimura Y., Fujisawa T., Nakamura Y., Kawachi M.;
RT   "Genome sequencing of cyanobaciteial culture collection at National
RT   Institute for Environmental Studies (NIES).";
RL   Submitted (JUN-2017) to the EMBL/GenBank/DDBJ databases.
CC   -!- SUBCELLULAR LOCATION: Carboxysome {ECO:0000256|ARBA:ARBA00023587}.
CC   -!- SIMILARITY: Belongs to the gamma-class carbonic anhydrase family.
CC       {ECO:0000256|ARBA:ARBA00023595}.
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DR   EMBL; AP018280; BAZ41141.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1Z4R0J2; -.
DR   Proteomes; UP000290974; Chromosome.
DR   GO; GO:0031470; C:carboxysome; IEA:UniProtKB-SubCell.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0043886; F:structural constituent of carboxysome shell; IEA:InterPro.
DR   CDD; cd00710; LbH_gamma_CA; 1.
DR   CDD; cd00307; RuBisCO_small_like; 3.
DR   Gene3D; 2.160.10.10; Hexapeptide repeat proteins; 1.
DR   Gene3D; 3.30.190.10; Ribulose bisphosphate carboxylase, small subunit; 3.
DR   InterPro; IPR047223; CA_gamma_LbH.
DR   InterPro; IPR017156; CcmM.
DR   InterPro; IPR001451; Hexapep.
DR   InterPro; IPR000894; RuBisCO_ssu_dom.
DR   InterPro; IPR036385; RuBisCO_ssu_sf.
DR   InterPro; IPR011004; Trimer_LpxA-like_sf.
DR   PANTHER; PTHR43360; CARBON DIOXIDE CONCENTRATING MECHANISM PROTEIN CCMM; 1.
DR   PANTHER; PTHR43360:SF1; CARBOXYSOME ASSEMBLY PROTEIN CCMM; 1.
DR   Pfam; PF00132; Hexapep; 1.
DR   Pfam; PF00101; RuBisCO_small; 3.
DR   PIRSF; PIRSF037250; CcmM; 2.
DR   SMART; SM00961; RuBisCO_small; 3.
DR   SUPFAM; SSF55239; RuBisCO, small subunit; 3.
DR   SUPFAM; SSF51161; Trimeric LpxA-like enzymes; 1.
PE   3: Inferred from homology;
KW   Bacterial microcompartment {ECO:0000256|ARBA:ARBA00023669};
KW   Carboxysome {ECO:0000256|ARBA:ARBA00023669};
KW   Disulfide bond {ECO:0000256|PIRSR:PIRSR037250-52};
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR037250-51};
KW   Reference proteome {ECO:0000313|Proteomes:UP000290974};
KW   Zinc {ECO:0000256|PIRSR:PIRSR037250-51}.
FT   DOMAIN          228..319
FT                   /note="Ribulose bisphosphate carboxylase small subunit"
FT                   /evidence="ECO:0000259|SMART:SM00961"
FT   DOMAIN          346..441
FT                   /note="Ribulose bisphosphate carboxylase small subunit"
FT                   /evidence="ECO:0000259|SMART:SM00961"
FT   DOMAIN          468..563
FT                   /note="Ribulose bisphosphate carboxylase small subunit"
FT                   /evidence="ECO:0000259|SMART:SM00961"
FT   REGION          323..356
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          444..472
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        328..356
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        58
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR037250-50"
FT   BINDING         77
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="ligand shared between two neighboring
FT                   subunits"
FT                   /note="in other chain"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR037250-51"
FT   BINDING         104
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="ligand shared between two neighboring
FT                   subunits"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR037250-51"
FT   BINDING         109
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="ligand shared between two neighboring
FT                   subunits"
FT                   /note="in other chain"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR037250-51"
FT   DISULFID        196..202
FT                   /evidence="ECO:0000256|PIRSR:PIRSR037250-52"
FT   DISULFID        272..290
FT                   /evidence="ECO:0000256|PIRSR:PIRSR037250-53"
FT   DISULFID        393..411
FT                   /evidence="ECO:0000256|PIRSR:PIRSR037250-53"
SQ   SEQUENCE   563 AA;  61246 MW;  1C063AF1774ED677 CRC64;
     MAVRSTAEAA PPTPWSRDLA EPSIHATAFV HSFSHIIGDV EIGANVIIAP GTSIRADEGA
     PFYIGENTNI QDGVVIHGLE QGRVIGDNKQ EYSVWVGKNT CLTHMALIHG PCYVGDNCFI
     GFRSTVFNAK IGAGCIVMMH ALIQDVEIPP GKYVGSGVVI TSQQQADRLP DVQAEDKEFA
     HHVVGINQAL RAGYLCAADN KCIAPIRNEL AKSYTDTSNG FSFAFERSDE VSSNRLGAQT
     VEQLRYLLEQ GFKIGTEHVD QRRFRTGSWN SCKPIEVRSL NDAIASLESC LADHSGEYVR
     LFGIDNGKRR VLETIIQRPD GTVDAPASTS FKAPTSSSSY NNGNGSSNGY SNGSAKISSD
     TIEKIRQLLS GGYRIGTEHV DERRFRTGSW QSCQPIESSS ANDVIAALEE CMIQHQGEYV
     RLIGIDTKAK RRVLESIIQR PNGVVTTASS SSSQSFTPAT SASSSSSSYS GSTATTTRLA
     SEVIDHLRQL LAGGYKISAE HVDQRRFRTG SWQSCGQIEA RSDRDAAAAL ESFLSEYQGE
     YVRLIGIDPK AKRRVLELII QRP
//
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