ID C7PXX1_CATAD Unreviewed; 1465 AA.
AC C7PXX1;
DT 13-OCT-2009, integrated into UniProtKB/TrEMBL.
DT 13-OCT-2009, sequence version 1.
DT 24-JAN-2024, entry version 69.
DE SubName: Full=Alpha-1,2-mannosidase {ECO:0000313|EMBL:ACU73431.1};
DE Flags: Precursor;
GN OrderedLocusNames=Caci_4569 {ECO:0000313|EMBL:ACU73431.1};
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:ACU73431.1, ECO:0000313|Proteomes:UP000000851};
RN [1] {ECO:0000313|EMBL:ACU73431.1, 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).
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP001700; ACU73431.1; -; Genomic_DNA.
DR STRING; 479433.Caci_4569; -.
DR CAZy; GH92; Glycoside Hydrolase Family 92.
DR KEGG; cai:Caci_4569; -.
DR eggNOG; COG3537; Bacteria.
DR HOGENOM; CLU_003690_2_0_11; -.
DR InParanoid; C7PXX1; -.
DR Proteomes; UP000000851; Chromosome.
DR GO; GO:0030246; F:carbohydrate binding; IEA:InterPro.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR Gene3D; 2.70.98.10; -; 2.
DR Gene3D; 1.20.1050.60; alpha-1,2-mannosidase; 1.
DR Gene3D; 3.30.2080.10; GH92 mannosidase domain; 1.
DR Gene3D; 2.60.40.10; Immunoglobulins; 1.
DR InterPro; IPR008928; 6-hairpin_glycosidase_sf.
DR InterPro; IPR014718; GH-type_carb-bd.
DR InterPro; IPR005887; GH92_a_mannosidase_put.
DR InterPro; IPR041371; GH92_N.
DR InterPro; IPR012939; Glyco_hydro_92.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR014756; Ig_E-set.
DR NCBIfam; TIGR01180; aman2_put; 1.
DR PANTHER; PTHR12143; PEPTIDE N-GLYCANASE PNGASE -RELATED; 1.
DR PANTHER; PTHR12143:SF39; SECRETED PROTEIN-RELATED; 1.
DR Pfam; PF07971; Glyco_hydro_92; 1.
DR Pfam; PF17678; Glyco_hydro_92N; 1.
DR SUPFAM; SSF81296; E set domains; 1.
DR SUPFAM; SSF48208; Six-hairpin glycosidases; 1.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000000851};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..39
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 40..1465
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5002980442"
FT DOMAIN 57..267
FT /note="Glycosyl hydrolase family 92 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF17678"
FT DOMAIN 385..846
FT /note="Glycosyl hydrolase family 92"
FT /evidence="ECO:0000259|Pfam:PF07971"
FT REGION 258..335
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 847..869
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 258..285
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 286..302
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 303..318
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1465 AA; 148826 MW; 4A70EF97E16B2B4B CRC64;
MARRVSVRRK MAKAAGAAVL TGALSVAAAL SGSAGTAFAA TGPDKGVSPV ANPAAAVNPF
LATGDGGAGG QADDFPGPDV PFGMMQWGPD TTPDRPEGGG YYYNDSNISG FSLTHMSGPG
CGAFGDVPIL PTVGALPANP SSVSAPFSHD AESASSDYYS VTTGTGASAV KTELTETARS
GIGRFTFPAG AQSNLLFKLT GSQNGDSATS AQVVGPNEIK GSVTSGHFCG ASNTYTLNFD
MVFDQPFTAN GTWTGSTVTP GTAPAAAKTT QKANTQASPN TAPGSSPTAS PSPNPTASPS
PSASPSPAAG SSTGGSTPAA PKAKPGALPA PTLHGAIPAA PKAATQKLAA NAAATGPDGL
YLTFDTSSDQ VVQAKVGISF TSGPNAQANL AAEQTGFAFD AVHAAGVKAW NAELGKIQIG
GGTAARQQVF YTGLYHSLLH PNIFSDTNGQ YVGFDNQVHT VQAGHIQVAN YSGWDIYRSQ
AQLEAIVDPA MASNAAQSIV NDAAQNNGMM PKWAMNNGES YVMVGDPADG ELADYYAFGA
HDFDTASALK YALAEANTPN NIRPDLADFE KYGYVPSDAA NTCCNFYGPV STTEEYGAAD
FALSQFAGAL GDKADATALQ TRSQDWQNLF SPATGLLEPR TTNGQYLPTT LSSSDNYVEG
DASQYRWQVG WNPSGLVTAM GGGQAVQKQL DTFFTQLDQG PPSPYAFLGN EPDMGVPWLY
DYTGAPWKAQ KIVNDVRTQI FTDDPKTSLG GNDDLGTTSA QGAFSMLGMF PEAAGSADMA
LNSPEFPLEI IHLANGKAIT VNAPGADSVK NFYVQSMKLN GSSWHSAWLP AAAFTHGATL
DVKMGSTPNK SWGAGKNDAP PSHTAGQQPA IGYLSDQQLR VTPGSSATVT VSAQDVAGDH
QKISVGATPP AGSGLTVKQS SSTLHLSPAG HDSLKLTINA PATAAQTFYT VPVQLTADGK
ALPPLKLTVL VAPAGSLLAS FDNNGIADDT QITVTNFDGS GNSYSAQALA GAGLTPGQPV
TVGGITYTWP LPAPGNPDNV VAAGQKVNVS AAAGTQELGL LGSADGGPSQ GVMTLNYSDG
STAQFWLGLS DWTLGAGKSK PSFGNGDAAT LSYRDCSSCA GGKDTTATHV FSTVFPVDPA
KTLTSVTLPN GTDQGRLHVF AVGTSTTAPT GAVTTSATPS PAAAGQQVTV HGSGFGATQG
TGYVAFSDQG INWGAPGNSA AFTVDSWSDT AVTFTVPTPS GTNGMFHVYP GSNAAVTVVN
AAGQVSDSQV LPMTPTANPA DYFDNIGTSA DSNQQCADFD GDGYSYSADA LAAAGIKPGG
TVTSDGVTYT WPNVQPCGAD NILPAGQTML VTGKAGATKL GLLGSSTNGG SAGPITLTYT
DGTSTTQTLT FNDWASGGDT TDTAIATMPY RNSDSGSSQS ITMYVFSTTV PLDTTKTLAS
VTFPNVASSV GSNTTAMHVF AVSEG
//