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Database: UniProt
Entry: W2EG94_9ACTN
LinkDB: W2EG94_9ACTN
Original site: W2EG94_9ACTN 
ID   W2EG94_9ACTN            Unreviewed;      1005 AA.
AC   W2EG94;
DT   19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT   19-MAR-2014, sequence version 1.
DT   27-MAR-2024, entry version 39.
DE   RecName: Full=ASPM-SPD-2-Hydin domain-containing protein {ECO:0008006|Google:ProtNLM};
GN   ORFNames=MPTA5024_39065 {ECO:0000313|EMBL:ETK30659.1};
OS   Microbispora sp. ATCC PTA-5024.
OC   Bacteria; Actinomycetota; Actinomycetes; Streptosporangiales;
OC   Streptosporangiaceae; Microbispora.
OX   NCBI_TaxID=316330 {ECO:0000313|EMBL:ETK30659.1, ECO:0000313|Proteomes:UP000018869};
RN   [1] {ECO:0000313|EMBL:ETK30659.1, ECO:0000313|Proteomes:UP000018869}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC PTA-5024 {ECO:0000313|EMBL:ETK30659.1,
RC   ECO:0000313|Proteomes:UP000018869};
RX   PubMed=24459268;
RA   Sosio M., Gallo G., Pozzi R., Serina S., Monciardini P., Bera A.,
RA   Stegmann E., Weber T.;
RT   "Draft Genome Sequence of the Microbispora sp. Strain ATCC-PTA-5024,
RT   Producing the Lantibiotic NAI-107.";
RL   Genome Announc. 2:e01198-13(2014).
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:ETK30659.1}.
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DR   EMBL; AWEV01000315; ETK30659.1; -; Genomic_DNA.
DR   AlphaFoldDB; W2EG94; -.
DR   STRING; 316330.MPTA5024_39065; -.
DR   PATRIC; fig|316330.3.peg.7516; -.
DR   HOGENOM; CLU_009451_0_0_11; -.
DR   OrthoDB; 5476529at2; -.
DR   Proteomes; UP000018869; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR   GO; GO:0030246; F:carbohydrate binding; IEA:InterPro.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:UniProt.
DR   CDD; cd04080; CBM6_cellulase-like; 1.
DR   Gene3D; 2.60.120.260; Galactose-binding domain-like; 3.
DR   Gene3D; 2.60.40.10; Immunoglobulins; 1.
DR   Gene3D; 2.160.20.10; Single-stranded right-handed beta-helix, Pectin lyase-like; 2.
DR   InterPro; IPR031549; ASH.
DR   InterPro; IPR006584; Cellulose-bd_IV.
DR   InterPro; IPR005084; CMB_fam6.
DR   InterPro; IPR000421; FA58C.
DR   InterPro; IPR008979; Galactose-bd-like_sf.
DR   InterPro; IPR013783; Ig-like_fold.
DR   InterPro; IPR006626; PbH1.
DR   InterPro; IPR012334; Pectin_lyas_fold.
DR   InterPro; IPR011050; Pectin_lyase_fold/virulence.
DR   NCBIfam; NF012200; choice_anch_D; 1.
DR   Pfam; PF15780; ASH; 1.
DR   Pfam; PF03422; CBM_6; 1.
DR   Pfam; PF00754; F5_F8_type_C; 1.
DR   SMART; SM00606; CBD_IV; 1.
DR   SMART; SM00231; FA58C; 1.
DR   SMART; SM00710; PbH1; 5.
DR   SUPFAM; SSF49785; Galactose-binding domain-like; 2.
DR   SUPFAM; SSF51126; Pectin lyase-like; 1.
DR   PROSITE; PS51175; CBM6; 1.
DR   PROSITE; PS50022; FA58C_3; 1.
PE   4: Predicted;
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW   Reference proteome {ECO:0000313|Proteomes:UP000018869};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           22..1005
FT                   /note="ASPM-SPD-2-Hydin domain-containing protein"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5004815148"
FT   DOMAIN          617..759
FT                   /note="CBM6"
FT                   /evidence="ECO:0000259|PROSITE:PS51175"
FT   DOMAIN          860..1005
FT                   /note="F5/8 type C"
FT                   /evidence="ECO:0000259|PROSITE:PS50022"
FT   REGION          873..894
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1005 AA;  101750 MW;  65266E3477BBF903 CRC64;
     MTAPAGAATT AAAAAATTAG ASLPFTSYEA EAGTPGGGAT TVALTAPPTT QYSSAALEAS
     GHSYVQLNGT GQSVQWTNGT GRPISAITVR VSIPDSAGGG GQTATLDLYV DNTFRQTLNL
     NSRQSWLYEG NDNYNGNSQN PANGNPRVFF DEARTFVTGT AIAPGSTFAL KKDGSNTAAF
     YYVDVVDVEN PPGPLSQPAG SISITGCGAV SDDTPTNGAA DGGAVDSTAA IQNCINQAQS
     QNKVLWIPPG TFYLKGTRGL DARGITIAGA GMWYSTIYRD VPLPNSVPLP ALFNLTSCTV
     QNLHLDSSAT SRASVDGAGG AMDTTGTDWV ADGIWSQHVL SGFWASGTGG TVRNSRLTSI
     WADGVNLNNV SLTSSVGSGL TATNNFVRGT GDDGMAINSV HYNTDSAGNR TYYTPMSHIT
     LTNNTIVAPW GGKGIGIYGG SAQDVEYNYI SDTARYIGLG AGRFGVNGDD LLSATVNGNV
     VVRSGGNAYN QGQPALHIGN GGDGQNTGVV DHVTATNNTV GDSLYDGIGF STSTNTLLQG
     NTVTSPWRNG VVVAPPFYPA PSGSATITGT TVTGLRSGTT AYVNNSGGFT ATVTGNSWQS
     GGGTGGPYGG TPAAVPGTVQ AENYDTGGQG VAYGVSSVNG TANGYRSDGV DLETTPDTGG
     GYNLGWTSAG QWFHYTVDVA SAGTYTLGLR VAAPAAVTGA LHVAGASGGN LTGAVTVPAT
     GGWQTWTTVT AQLTLPAGRQ TLTVYQDNGG WNINSLQFTA AGGGTAMLTA APSSLTFGGQ
     AVGTTSAAQA VTVRNTGTAT ASIGSVAASG DFAQTNTCGG SIAANASCTV NVTFRPTATG
     GRTGSLTITS TASNSPTVVA LSGTGGTASA NLAAGRPTAE SSHTDVYPSS KTTDGDQNTY
     WESANNAFPQ WVQVDLGSAQ QASRVVLQLP ASWGARDQTL SLLGSTDGTT FTTVKASAAY
     TFSPSSGNTV TITFPASTQR YWRVTVTANT GWPAGQVSEF QVWNQ
//
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