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Database: UniProt
Entry: I3R9P4_HALMT
LinkDB: I3R9P4_HALMT
Original site: I3R9P4_HALMT 
ID   I3R9P4_HALMT            Unreviewed;       562 AA.
AC   I3R9P4;
DT   05-SEP-2012, integrated into UniProtKB/TrEMBL.
DT   05-SEP-2012, sequence version 1.
DT   27-MAR-2024, entry version 50.
DE   SubName: Full=(Chitin-binding domain type 3)-containing protein {ECO:0000313|EMBL:AFK20954.1};
DE   SubName: Full=Chitinase {ECO:0000313|EMBL:AHZ24178.1};
DE   SubName: Full=PKD domain-containing protein {ECO:0000313|EMBL:QCQ77129.1};
GN   Name=chiA3 {ECO:0000313|EMBL:AFK20954.1};
GN   OrderedLocusNames=HFX_5119 {ECO:0000313|EMBL:AFK20954.1};
GN   ORFNames=BM92_18415 {ECO:0000313|EMBL:AHZ24178.1}, E6P09_17510
GN   {ECO:0000313|EMBL:QCQ77129.1};
OS   Haloferax mediterranei (strain ATCC 33500 / DSM 1411 / JCM 8866 / NBRC
OS   14739 / NCIMB 2177 / R-4) (Halobacterium mediterranei).
OG   Plasmid HMPLAS2 {ECO:0000313|EMBL:AHZ24178.1,
OG   ECO:0000313|Proteomes:UP000027075},
OG   Plasmid pHM300 {ECO:0000313|EMBL:AFK20954.1,
OG   ECO:0000313|Proteomes:UP000006469}, and
OG   Plasmid pHME322 {ECO:0000313|EMBL:QCQ77129.1,
OG   ECO:0000313|Proteomes:UP000299011}.
OC   Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Haloferacales;
OC   Haloferacaceae; Haloferax.
OX   NCBI_TaxID=523841 {ECO:0000313|EMBL:AFK20954.1, ECO:0000313|Proteomes:UP000006469};
RN   [1] {ECO:0000313|EMBL:AFK20954.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=CGMCC 1.2087 {ECO:0000313|EMBL:AFK20954.1};
RX   PubMed=22247127; DOI=10.1128/AEM.07114-11;
RA   Cai S., Cai L., Liu H., Liu X., Han J., Zhou J., Xiang H.;
RT   "Identification of the haloarchaeal phasin (PhaP) that functions in
RT   polyhydroxyalkanoate accumulation and granule formation in Haloferax
RT   mediterranei.";
RL   Appl. Environ. Microbiol. 78:1946-1952(2012).
RN   [2] {ECO:0000313|EMBL:AFK20954.1, ECO:0000313|Proteomes:UP000006469}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 33500 / DSM 1411 / JCM 8866 / NBRC 14739 / NCIMB 2177 /
RC   R-4 {ECO:0000313|Proteomes:UP000006469}, and CGMCC 1.2087
RC   {ECO:0000313|EMBL:AFK20954.1};
RC   PLASMID=pHM300 {ECO:0000313|Proteomes:UP000006469};
RX   PubMed=22843593; DOI=10.1128/JB.00880-12;
RA   Han J., Zhang F., Hou J., Liu X., Li M., Liu H., Cai L., Zhang B., Chen Y.,
RA   Zhou J., Hu S., Xiang H.;
RT   "Complete genome sequence of the metabolically versatile halophilic
RT   archaeon Haloferax mediterranei, a poly(3-hydroxybutyrate-co-3-
RT   hydroxyvalerate) producer.";
RL   J. Bacteriol. 194:4463-4464(2012).
RN   [3] {ECO:0000313|EMBL:AHZ24178.1, ECO:0000313|Proteomes:UP000027075}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 33500 {ECO:0000313|EMBL:AHZ24178.1}, and ATCC 33500 / DSM
RC   1411 / JCM 8866 / NBRC 14739 / NCIMB 2177 / R-4
RC   {ECO:0000313|Proteomes:UP000027075};
RC   PLASMID=HMPLAS2 {ECO:0000313|EMBL:AHZ24178.1}, and Plasmid HMPLAS2
RC   {ECO:0000313|Proteomes:UP000027075};
RA   Bautista V.;
RT   "Transcriptional profiles of Haloferax mediterranei on the basis of
RT   nitrogen availability.";
RL   Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
RN   [4] {ECO:0000313|EMBL:AFK20954.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=CGMCC 1.2087 {ECO:0000313|EMBL:AFK20954.1};
RC   PLASMID=pHM300 {ECO:0000313|EMBL:AFK20954.1};
RA   Wang L., Yang H., Xiang H.;
RL   Submitted (MAY-2014) to the EMBL/GenBank/DDBJ databases.
RN   [5] {ECO:0000313|EMBL:QCQ77129.1, ECO:0000313|Proteomes:UP000299011}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 33500 {ECO:0000313|EMBL:QCQ77129.1}, and ATCC 33500 / DSM
RC   1411 / JCM 8866 / NBRC 14739 / NCIMB 2177 / R-4
RC   {ECO:0000313|Proteomes:UP000299011};
RC   PLASMID=pHME322 {ECO:0000313|EMBL:QCQ77129.1,
RC   ECO:0000313|Proteomes:UP000299011};
RA   DasSarma S., DasSarma P., DasSarma S., Fomenkov A., Vincze T., Anton B.P.,
RA   Roberts R.J.;
RT   "Methylomes of two halophilic Archaea, Haloarcula marismortui and Haloferax
RT   mediterranei.";
RL   Submitted (APR-2019) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; CP001870; AFK20954.1; -; Genomic_DNA.
DR   EMBL; CP007553; AHZ24178.1; -; Genomic_DNA.
DR   EMBL; CP039141; QCQ77129.1; -; Genomic_DNA.
DR   RefSeq; WP_014732662.1; NZ_CP039141.1.
DR   AlphaFoldDB; I3R9P4; -.
DR   GeneID; 40158253; -.
DR   KEGG; hme:HFX_5119; -.
DR   HOGENOM; CLU_485412_0_0_2; -.
DR   OrthoDB; 8638at2157; -.
DR   Proteomes; UP000006469; Plasmid pHM300.
DR   Proteomes; UP000027075; Plasmid HMPLAS2.
DR   Proteomes; UP000299011; Plasmid pHME322.
DR   GO; GO:0005576; C:extracellular region; IEA:InterPro.
DR   GO; GO:0030246; F:carbohydrate binding; IEA:InterPro.
DR   GO; GO:0004553; F:hydrolase activity, hydrolyzing O-glycosyl compounds; IEA:InterPro.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR   CDD; cd12215; ChiC_BD; 1.
DR   CDD; cd00146; PKD; 1.
DR   Gene3D; 2.10.10.20; Carbohydrate-binding module superfamily 5/12; 1.
DR   Gene3D; 2.60.40.10; Immunoglobulins; 1.
DR   InterPro; IPR003610; CBM_fam5/12.
DR   InterPro; IPR036573; CBM_sf_5/12.
DR   InterPro; IPR013783; Ig-like_fold.
DR   InterPro; IPR022409; PKD/Chitinase_dom.
DR   InterPro; IPR000601; PKD_dom.
DR   InterPro; IPR035986; PKD_dom_sf.
DR   Pfam; PF02839; CBM_5_12; 1.
DR   Pfam; PF18911; PKD_4; 1.
DR   SMART; SM00495; ChtBD3; 1.
DR   SMART; SM00089; PKD; 1.
DR   SUPFAM; SSF51055; Carbohydrate binding domain; 1.
DR   SUPFAM; SSF49299; PKD domain; 1.
DR   PROSITE; PS50093; PKD; 1.
PE   4: Predicted;
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Plasmid {ECO:0000313|EMBL:AFK20954.1}.
FT   DOMAIN          87..172
FT                   /note="PKD"
FT                   /evidence="ECO:0000259|PROSITE:PS50093"
SQ   SEQUENCE   562 AA;  62563 MW;  21E16C1A61F7AB01 CRC64;
     MKQNRREYLR NASVLFTSIA GASVTVSGAE SPPQWDSDTT YTGGDRVVHE GYIWEAKWWT
     HGTEPSTKTG NPWKQIREEG GGSGEELKAV IEMSATTVTV DEDVTLDASK STGDIDTYEW
     TVDDRDPITG VETTVSFDTT GDHTVTLTVT NTDEDTATAE KTVTVESDGG GSGDLTPETT
     IKEFFPKYED RYIPDIFLDF MPGENDGGHG SHGGHSTTTV KWTDAEKAAD FNVDLDAIRN
     NVSDGSLTFD SLGTQALDWA KQFRSKGLPD HAIAQLLPRL MLLPDKTEDP TFQGPGRAEA
     WDETAGPVPA SNDPSLFYQE QWPTDARNEK EEEVKERDRV YFQAKNDPAW SDDFEYIDNY
     DSALLDTLQN DTHPATGDPL GGDRFTANAP MEANAEIHGS DWFWHQVLLF KNTSPVPYHL
     DGAVIWWLGP ANFGKTMSAG AYNNEQRPRP GYGHPQRDII EITLEDKHVP EDYADIDSTL
     SAYAVRLAYH DSPYNMRTAY PGQYWSIEVS VGEPLTNKFD TPEKRQRVVD MIAETAHVEL
     ETDMDLNDDV VDAIELYNRV GN
//
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