ID A0A087EKC0_9BIFI Unreviewed; 1906 AA.
AC A0A087EKC0;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 24-JAN-2024, entry version 36.
DE SubName: Full=Endo-alpha-N-acetylgalactosaminidase {ECO:0000313|EMBL:KFJ08221.1};
DE EC=3.2.1.97 {ECO:0000313|EMBL:KFJ08221.1};
GN ORFNames=BITS_0556 {ECO:0000313|EMBL:KFJ08221.1};
OS Bifidobacterium tsurumiense.
OC Bacteria; Actinomycetota; Actinomycetes; Bifidobacteriales;
OC Bifidobacteriaceae; Bifidobacterium.
OX NCBI_TaxID=356829 {ECO:0000313|EMBL:KFJ08221.1, ECO:0000313|Proteomes:UP000029080};
RN [1] {ECO:0000313|EMBL:KFJ08221.1, ECO:0000313|Proteomes:UP000029080}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JCM 13495 {ECO:0000313|EMBL:KFJ08221.1,
RC ECO:0000313|Proteomes:UP000029080};
RA Ventura M., Milani C., Lugli G.A.;
RT "Genomics of Bifidobacteria.";
RL Submitted (MAR-2014) to the EMBL/GenBank/DDBJ databases.
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:KFJ08221.1}.
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DR EMBL; JGZU01000003; KFJ08221.1; -; Genomic_DNA.
DR STRING; 356829.BITS_0556; -.
DR eggNOG; COG0366; Bacteria.
DR Proteomes; UP000029080; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0030246; F:carbohydrate binding; IEA:InterPro.
DR GO; GO:0033926; F:glycopeptide alpha-N-acetylgalactosaminidase activity; IEA:UniProtKB-EC.
DR GO; GO:0050110; F:mucinaminylserine mucinaminidase activity; IEA:UniProtKB-EC.
DR GO; GO:0008152; P:metabolic process; IEA:UniProtKB-KW.
DR CDD; cd14244; GH_101_like; 1.
DR Gene3D; 2.60.120.870; -; 1.
DR Gene3D; 2.70.98.10; -; 1.
DR Gene3D; 1.20.1270.90; AF1782-like; 2.
DR Gene3D; 2.60.40.1120; Carboxypeptidase-like, regulatory domain; 1.
DR Gene3D; 1.20.1270.70; Designed single chain three-helix bundle; 2.
DR Gene3D; 2.60.120.260; Galactose-binding domain-like; 3.
DR Gene3D; 3.20.20.80; Glycosidases; 1.
DR Gene3D; 2.60.40.1180; Golgi alpha-mannosidase II; 1.
DR InterPro; IPR013784; Carb-bd-like_fold.
DR InterPro; IPR025706; Endoa_GalNAc.
DR InterPro; IPR000421; FA58C.
DR InterPro; IPR040633; Gal_mutarotas_3.
DR InterPro; IPR008979; Galactose-bd-like_sf.
DR InterPro; IPR014718; GH-type_carb-bd.
DR InterPro; IPR049314; GH101_dom-5.
DR InterPro; IPR040502; GH101_dom-6.
DR InterPro; IPR040575; GH101_N.
DR InterPro; IPR035364; Glyco_hyd_101_beta.
DR InterPro; IPR013780; Glyco_hydro_b.
DR InterPro; IPR048842; SpGH101_helical.
DR Pfam; PF13620; CarboxypepD_reg; 1.
DR Pfam; PF00754; F5_F8_type_C; 1.
DR Pfam; PF07554; FIVAR; 3.
DR Pfam; PF18080; Gal_mutarotas_3; 1.
DR Pfam; PF17974; GalBD_like; 1.
DR Pfam; PF21466; GH101_dom-5; 1.
DR Pfam; PF17995; GH101_N; 1.
DR Pfam; PF17451; Glyco_hyd_101C; 1.
DR Pfam; PF12905; Glyco_hydro_101; 1.
DR Pfam; PF20909; SpGH101_helical; 1.
DR SUPFAM; SSF49785; Galactose-binding domain-like; 1.
DR SUPFAM; SSF49452; Starch-binding domain-like; 1.
DR PROSITE; PS50022; FA58C_3; 1.
PE 4: Predicted;
KW Glycosidase {ECO:0000313|EMBL:KFJ08221.1};
KW Hydrolase {ECO:0000313|EMBL:KFJ08221.1};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000029080};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 1881..1900
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 1452..1616
FT /note="F5/8 type C"
FT /evidence="ECO:0000259|PROSITE:PS50022"
FT REGION 1847..1871
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1851..1866
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1906 AA; 205870 MW; 546F9DA7EBA3C8A4 CRC64;
MNSASAVAVA DRAATDIGWT IDSATSKGGE VLEITDGVWR HLKAGASNGN STTDASQYPI
VAANDGTFDF TQAGEYHAII KSPQDGSKNR FGFYLGYKNP NSGLFIGFDK DGWFWQRYGG
DGTWYSGSRV AAPAANVETQ VDITWTGTTA TLTVDGTKAF DVPYSAMVGI MSDKLAMKAS
AWGSELTDMY LRDQSETQST YAISGVVRKS DGTPISGARV RMSGQTTVTT GADGAWSFAD
LPAGEYTITV GASGYQEASK TVQVVDADVS GQDVTLSAAA AYETEKISSE DMDVLINKHF
PSVQQYTMKK LDNRIMYGQA NDIRKVNING TEMQLTDDNV TLDVAGSKAT YVLTVQNQEQ
HIDAKITVVM EVKGNALHFD VTKIENKAGD EHPIQTLSFP EHSLISVRSS QQDAQFTGAR
MSSNTTVNGD TNFPVNDDTT IGDKGDYAYG FISADSLSAG LWSNSEHDGT TAANGIAGGS
QNTRVQANTQ VVDGDNSLGL SSAPWYYQRV VKDSKKRSYT VSETDMPKMA VAITGDENSD
GVVNWQDGAL AYRTIMNNPY KSEEVPELVA WRIAMNFGGQ AQNPFLTTLD NVKKVALNTD
GLGQSVLLKG YGNEGHDSGH PDYGDIGQRI GGATDMNTLM TEGAKYGARF GVHVNASEMY
PEAKAFDEDM VRRNASGGLR YGWNWLDQGV GIDGIYDLAS NSRLNRFAEL KAEVGDNMDF
IYLDVWGNQT SGTEDSWETR KMSKMINDNG WRMTTEWGAG NEYDSTFQHW AADLTYGGKG
MKGENSQVMR FLRNHQKDSW VGDYPNYGGA ANAPLLGGYN MKDFEGWQGR NDYDAYVTNL
FTHDVSTKFI QHFKVNRWVN SPLDPSSVQD PSVNNGNEFI ELKDDSGNVV TLARGSNNSS
DAAYRNRTIT LNGTVISTGA VSRGDGTGTG NESYLLPWLW DAQTGEFVAD KDQKLYHWNT
AGGTTEWTLP SDWQNLSNVK VYKLTDLGRA DEQVVAVANG KITLTADAET PYVVVKGDAA
PKQINVTWST GMHLVDAGFN GGEQALGEDW AIDGDGQATI AKSQYSNPML KLTGTVSATQ
QLTDLTPGTR YAVYVGVDNR SDGDATMTVM HDGKVLATNA TARSIAKNYI KAYTHNTNSA
TVDGTSYFQN MYVFFDAPES GEVTLNLAHK GDGDVYYDDV RVVANAYNGI TTDSSGSLVS
LTNDFENNAQ GIWPFVISGS EGVEDNRVHL SELHAPYTQA GWDVKKMDDV LQGDWSVKIN
GLTQKGTLVY QTIPQNVKFD AGRKYKISFD YQSGSDGAYA LAVGQGEFAT NGAQLTDLEK
HLGDTGHYEF EITGDVNGDS WFGIYSTSNA PDTQGTSGNA ANFGGYKDFV LDNLKVERVD
EEAKDKDAVE EKLKAVTDVY DTKEADVSAE AWVTYQKTLA KVRAMIDKNG ANSDDFTRAY
GLLEALESYM QNAPNNDGSD AYDVAADQYT VSAGSAQQGY PDEGPVDLAQ DGLPGTIWHT
EWGVDSLSRG NAWYQFNLNE PTTITGLRYL PRSGGDNMNG KIKKFNITLT FADGATQQII
TDGTFNTATK WQKVTFPSDT MTRPASSAGV ANVTSVRITA TETAGSGETQ INMFASAAEL
RLTTDRDVDP VEIPVDKTDL NALIASTESL VESDYTEDSW AELSEALAAA KTESGDEDAE
LYDVLLAQYN LETAIKGLVR TNPSSDVDKS ALQTQVNAVQ ALKEADYTTE SWKAFSAALT
AANGVLANAD VAQDEVDAAL QALRAAAQAL VPVKTEPEEP GQVTKSELQA AVNQAKALDL
QAYTNASAAA LRKAMLAAQA VLDNEQATQE EVDAALQSVQ DALKALEQRP AEQSSENKDD
SGKGSNSTRR ISKLSRTGSD IAVIAALSII AAVAGAVALG RRRFRR
//
