ID C7Q4Q1_CATAD Unreviewed; 885 AA.
AC C7Q4Q1;
DT 13-OCT-2009, integrated into UniProtKB/TrEMBL.
DT 13-OCT-2009, sequence version 1.
DT 27-MAR-2024, entry version 61.
DE SubName: Full=Putative cell wall binding repeat 2-containing protein {ECO:0000313|EMBL:ACU72020.1};
GN OrderedLocusNames=Caci_3111 {ECO:0000313|EMBL:ACU72020.1};
OS Catenulispora acidiphila (strain DSM 44928 / JCM 14897 / NBRC 102108 / NRRL
OS B-24433 / ID139908).
OC Bacteria; Actinomycetota; Actinomycetes; Catenulisporales;
OC Catenulisporaceae; Catenulispora.
OX NCBI_TaxID=479433 {ECO:0000313|EMBL:ACU72020.1, ECO:0000313|Proteomes:UP000000851};
RN [1] {ECO:0000313|EMBL:ACU72020.1, ECO:0000313|Proteomes:UP000000851}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 44928 / JCM 14897 / NBRC 102108 / NRRL B-24433 / ID139908
RC {ECO:0000313|Proteomes:UP000000851};
RX PubMed=21304647; DOI=10.4056/sigs.17259;
RA Copeland A., Lapidus A., Glavina Del Rio T., Nolan M., Lucas S., Chen F.,
RA Tice H., Cheng J.F., Bruce D., Goodwin L., Pitluck S., Mikhailova N.,
RA Pati A., Ivanova N., Mavromatis K., Chen A., Palaniappan K., Chain P.,
RA Land M., Hauser L., Chang Y.J., Jeffries C.D., Chertkov O., Brettin T.,
RA Detter J.C., Han C., Ali Z., Tindall B.J., Goker M., Bristow J.,
RA Eisen J.A., Markowitz V., Hugenholtz P., Kyrpides N.C., Klenk H.P.;
RT "Complete genome sequence of Catenulispora acidiphila type strain (ID
RT 139908).";
RL Stand. Genomic Sci. 1:119-125(2009).
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DR EMBL; CP001700; ACU72020.1; -; Genomic_DNA.
DR AlphaFoldDB; C7Q4Q1; -.
DR STRING; 479433.Caci_3111; -.
DR KEGG; cai:Caci_3111; -.
DR eggNOG; COG2247; Bacteria.
DR eggNOG; COG3291; Bacteria.
DR HOGENOM; CLU_320490_0_0_11; -.
DR InParanoid; C7Q4Q1; -.
DR Proteomes; UP000000851; Chromosome.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:UniProt.
DR CDD; cd00146; PKD; 2.
DR Gene3D; 3.40.50.12090; -; 2.
DR Gene3D; 2.60.40.10; Immunoglobulins; 2.
DR Gene3D; 2.160.20.10; Single-stranded right-handed beta-helix, Pectin lyase-like; 1.
DR InterPro; IPR039448; Beta_helix.
DR InterPro; IPR007253; Cell_wall-bd_2.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR012334; Pectin_lyas_fold.
DR InterPro; IPR011050; Pectin_lyase_fold/virulence.
DR InterPro; IPR000601; PKD_dom.
DR InterPro; IPR035986; PKD_dom_sf.
DR PANTHER; PTHR30032; N-ACETYLMURAMOYL-L-ALANINE AMIDASE-RELATED; 1.
DR PANTHER; PTHR30032:SF4; STAGE II SPORULATION PROTEIN D; 1.
DR Pfam; PF13229; Beta_helix; 1.
DR Pfam; PF04122; CW_binding_2; 3.
DR Pfam; PF18911; PKD_4; 2.
DR SUPFAM; SSF51126; Pectin lyase-like; 1.
DR SUPFAM; SSF49299; PKD domain; 2.
DR PROSITE; PS50093; PKD; 2.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000000851}.
FT DOMAIN 407..465
FT /note="PKD"
FT /evidence="ECO:0000259|PROSITE:PS50093"
FT DOMAIN 497..549
FT /note="PKD"
FT /evidence="ECO:0000259|PROSITE:PS50093"
FT REGION 326..347
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 885 AA; 89610 MW; CF64449998F1CC67 CRC64;
MSTLTATAVT DLPARAAVAN AVYVFDNNFE CSDTAPDAGS EATPYCTLPA ALASSSVVSG
TTIMITGNVS GAIDITKSDI TIEGRGTRVV GGAYGISLVG RHHVTLNGVG YQYQTGEALR
IDSSTDITVN SFGAARSQDG STTPDPAMPA ISVTGSTRVT LSDGVLQANP GPGVLVQQSS
QVVVSDTIVN GSTGGIALAD STGVDVVSDT IDENCGAGIS VLGASTDVDI ADNIVSNALA
CGATLGTALT VDTTAAPPTV DANILTTAAG TDAVSWQGRT FADGPALDAA GDGAHDLTVD
PGFAIQVPAG SAHRSGWDLA PGSPAIDSAD SGAPNMPARD RDGAVRTDDL AVADTGTGPI
AYADRGAVEL ARQATPTLTV TATAGRTPSD YRTVSVAVQG DGGSWWPIVS YNVDFGDGTK
SGTRPYPEAG TAPSHTYGAD KTYNGTVTVT DAHGRVFTTP FTVTLAKRVF SPSLEVDQSG
PSLGDVTALI QTTNEDDPYL GSYAIDFGDH TPTVTWTSGG VLVPTDTLRH TYAASGTYTV
TLSATDNLGW PTAQPVVQKF TVTLPVPYQP PTPIPTTVHR IGGTDRYATA RLVSQAQWKA
GTASAVVLAR GDQAPDALSG VPLAAHVHGP LLLTSPGSLD AATRAEIDRV TGGPSTSKTV
YILGGASAIA PGIEDSLRKA GYQVVRYEGT DRYRTSLAVA GAFGSTAHVI VATGLDFPDA
LAAGPLGAVE NAPIILSKGD ALDPAVTPFV RSHQDIDPVG GAAQRAVAKI STTGRTVSHS
LAGATRYDTA AAVANAVMRI AGHTTFAIGV ASGKAFPDAL TGGAYAANAG MPLLITDPAV
LSSAVRGVLI EEYSTLRSVT LFGGNQAVSD GVEATIANEI SAKIQ
//