ID A0A0V0WBW9_9BILA Unreviewed; 2185 AA.
AC A0A0V0WBW9;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 37.
DE SubName: Full=Coatomer subunit beta {ECO:0000313|EMBL:KRX73006.1};
GN Name=Copb2 {ECO:0000313|EMBL:KRX73006.1};
GN ORFNames=T06_14000 {ECO:0000313|EMBL:KRX73006.1};
OS Trichinella sp. T6.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Trichinellida; Trichinellidae; Trichinella.
OX NCBI_TaxID=92179 {ECO:0000313|EMBL:KRX73006.1, ECO:0000313|Proteomes:UP000054673};
RN [1] {ECO:0000313|EMBL:KRX73006.1, ECO:0000313|Proteomes:UP000054673}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ISS34 {ECO:0000313|EMBL:KRX73006.1};
RA Korhonen P.K., Edoardo P., Giuseppe L.R., Gasser R.B.;
RT "Evolution of Trichinella species and genotypes.";
RL Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|ARBA:ARBA00001947};
CC -!- SUBCELLULAR LOCATION: Golgi apparatus membrane
CC {ECO:0000256|ARBA:ARBA00004255}; Peripheral membrane protein
CC {ECO:0000256|ARBA:ARBA00004255}; Cytoplasmic side
CC {ECO:0000256|ARBA:ARBA00004255}. Membrane
CC {ECO:0000256|ARBA:ARBA00004287}; Peripheral membrane protein
CC {ECO:0000256|ARBA:ARBA00004287}; Cytoplasmic side
CC {ECO:0000256|ARBA:ARBA00004287}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 38 family.
CC {ECO:0000256|ARBA:ARBA00009792}.
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:KRX73006.1}.
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DR EMBL; JYDK01000189; KRX73006.1; -; Genomic_DNA.
DR Proteomes; UP000054673; Unassembled WGS sequence.
DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0030117; C:membrane coat; IEA:InterPro.
DR GO; GO:0004559; F:alpha-mannosidase activity; IEA:InterPro.
DR GO; GO:0030246; F:carbohydrate binding; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0005198; F:structural molecule activity; IEA:InterPro.
DR GO; GO:0006886; P:intracellular protein transport; IEA:InterPro.
DR GO; GO:0006013; P:mannose metabolic process; IEA:InterPro.
DR GO; GO:0016192; P:vesicle-mediated transport; IEA:UniProtKB-KW.
DR CDD; cd22947; Coatomer_WDAD_beta-like; 1.
DR CDD; cd10809; GH38N_AMII_GMII_SfManIII_like; 1.
DR CDD; cd00200; WD40; 1.
DR Gene3D; 1.25.40.470; -; 1.
DR Gene3D; 3.20.110.10; Glycoside hydrolase 38, N terminal domain; 1.
DR Gene3D; 1.20.1270.50; Glycoside hydrolase family 38, central domain; 1.
DR Gene3D; 2.60.40.1180; Golgi alpha-mannosidase II; 1.
DR Gene3D; 2.130.10.10; YVTN repeat-like/Quinoprotein amine dehydrogenase; 1.
DR InterPro; IPR006692; Coatomer_WD-assoc_reg.
DR InterPro; IPR020472; G-protein_beta_WD-40_rep.
DR InterPro; IPR011013; Gal_mutarotase_sf_dom.
DR InterPro; IPR011330; Glyco_hydro/deAcase_b/a-brl.
DR InterPro; IPR011682; Glyco_hydro_38_C.
DR InterPro; IPR015341; Glyco_hydro_38_cen.
DR InterPro; IPR037094; Glyco_hydro_38_cen_sf.
DR InterPro; IPR000602; Glyco_hydro_38_N.
DR InterPro; IPR027291; Glyco_hydro_38_N_sf.
DR InterPro; IPR028995; Glyco_hydro_57/38_cen_sf.
DR InterPro; IPR013780; Glyco_hydro_b.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR InterPro; IPR036322; WD40_repeat_dom_sf.
DR InterPro; IPR001680; WD40_rpt.
DR PANTHER; PTHR11607; ALPHA-MANNOSIDASE; 1.
DR PANTHER; PTHR11607:SF3; LYSOSOMAL ALPHA-MANNOSIDASE; 1.
DR Pfam; PF09261; Alpha-mann_mid; 1.
DR Pfam; PF04053; Coatomer_WDAD; 1.
DR Pfam; PF07748; Glyco_hydro_38C; 1.
DR Pfam; PF01074; Glyco_hydro_38N; 1.
DR Pfam; PF00400; WD40; 5.
DR PRINTS; PR00320; GPROTEINBRPT.
DR SMART; SM00872; Alpha-mann_mid; 1.
DR SMART; SM00320; WD40; 6.
DR SUPFAM; SSF88688; Families 57/38 glycoside transferase middle domain; 1.
DR SUPFAM; SSF74650; Galactose mutarotase-like; 1.
DR SUPFAM; SSF88713; Glycoside hydrolase/deacetylase; 1.
DR SUPFAM; SSF50978; WD40 repeat-like; 1.
DR PROSITE; PS50082; WD_REPEATS_2; 4.
DR PROSITE; PS50294; WD_REPEATS_REGION; 4.
PE 3: Inferred from homology;
KW ER-Golgi transport {ECO:0000256|ARBA:ARBA00022892};
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295};
KW Hydrolase {ECO:0000256|ARBA:ARBA00023295};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000054673};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius};
KW Transport {ECO:0000256|ARBA:ARBA00022892};
KW WD repeat {ECO:0000256|ARBA:ARBA00022574, ECO:0000256|PROSITE-
KW ProRule:PRU00221}; Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT TRANSMEM 28..51
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 506..593
FT /note="Glycoside hydrolase family 38 central"
FT /evidence="ECO:0000259|SMART:SM00872"
FT REPEAT 1273..1314
FT /note="WD"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00221"
FT REPEAT 1316..1358
FT /note="WD"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00221"
FT REPEAT 1359..1402
FT /note="WD"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00221"
FT REPEAT 1403..1444
FT /note="WD"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00221"
FT REGION 2092..2119
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2150..2185
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2163..2185
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2185 AA; 248848 MW; 1E14D23A96C84FBC CRC64;
MAYNGVTLKI ASKRRSEMRI FRRSVASAWK FGLAIIVVVF FISSVALYNI MDSVTPSSQK
LRYFGEYDLK RLETKLIKLE SEANRNEEIL GQIQRSLYYR LNRVRNRPPA STLSAVKKKE
RKQTYRKCNA GLLNTTVNVQ MLSMYELLEF DNPDGGHWKQ GWEITYDKNE VKERPHLQVF
VVPHSHTDPG WIKTFDEYYS ESTKHIFENM IEKLSQKSQM KFIYAEMSFF EKWWREVDTA
KRMLTKRLLD IGQLEIVTGA WVMTDEANAH YFSMIDQMTE GHQWLLNHLD YKPKNHWSID
PFGLSATTAY FVGLSGLKTM SVQRIHYAVK KHLALNKNLE FYWRQLWKRD SSSDIFCHVF
PFYSYDIPHT CGPDPAVCCQ FDFHRSQVGS LPCPWGIPAL PIDMENIGER AFALLDQYRK
HAELYKLNVL LVPLGDDFRY TTSMEWQQQY NNYEKLFEYM NRQDWNVQFG TLEDYYRALF
KRADVGGETF PTLSGDFFTY ADRNEDYWSG YYTSRPLYKR MERILASFLR GAEIMFNLAM
SDVRSKALEH QFPSQRLFNN LVIARRNLAL FQHHDGIAGT AKTPVVMDYA KRLWSSIELS
KATMATAILY FMRKASTSLL DADSIKLDFS ERIMDASHTS ENVVINVLDE NERSILVYNS
LPYFRSEIVC INVDTYKIAL YDAANNRLKI QISPVITKTS VGFIISVTTY QVCWTATMES
LSIIRYRLVS GDDPLDGEMV TISQREVVHS STFPRNVLSE EQFDIVSPVY VATFSTSTGL
LKELKHRNKD NKMNLQLEFF VYKSKSQSYT AGGAYLFLPK GEAEPLNNVD DVLLLEGDMF
ATVYSNLKNV LHQFTVVKLE VPGAESLHIR NTVDITTEIE DFEIVMRLKA DIHNSDHSFY
TDLNGLQMIK RKYFSKIPLQ GNFYPMTTAA FIEDSAHRLT LLSAQANGVT SIKPGWIEVF
LDRRTHVDDS RGVAQPMLDN VIVTSDFRLM LESLDGDAYK IGKNLPTINY LTLPAHHQSL
LLIYPVFVLY TANDFVEGSR FCYISELRSH YQALQKPFPC DFHLINMRSV ESKGAFDSKA
EVESFLNETL LILLRLENSC FSTQPPSVVC SLKDNDVPTA VDIFGTNVKA VKEMSLTALY
QLNDTKLPDE PLYVEPMEIK TYKIEWKSAQ DAAEHKSPLP LRLDVKRKLL ARSDRVKCVD
LHPTEPWMLC SLYNGNVHAW NYETQTLLKS FEVCDLPVRS AKFVPRKSWV LTGSDDMQVR
VFNYNTLERV HQFEAHSDYL RSIAVHATQP LVLTSSDDMT IKLWDWESNW QLKQTFEGHT
HYVMQVLFNP KDNNTFASAS LDRTVKIWQL GSSHPNFTLE GHEKGVNCID YYHGGDRPYL
ISGADDRLVK IWDYQNKTCV ATLEGHVQNV SSVCFHPDLP VIITGSEDNT VRIWHGSTYR
METTLNYGLD RVWTICALKG QNVVAIGYDE GSIIVKLGRE EPAVSMDANG KLLWAKHAEI
QQANLKAVCN EAEYPDGARL SLSAKDMGAI EFYPRSIQHS PNGRFVVVRG ESEYVIYTAM
ALRNKSYGAA VEFVWAKESN MYAIRDVSSS ILVEIHKNFT RYKTVYAEAS IDCIFGGTLL
GIRCGGQLIF YDWETIHVIR RIDIKAHQVY WSEKELLAIT TASEFYILQF NEAEVISQLS
ESETPSPDGV EEAFDVIHTG TEDISTAYWV GDCLVYTTIN NRLRYCVGSE TVTIAHLDRG
LYILGYLPQD NRLFLSDKDL NVVSYQLVLS VLEYQTAVMR HDFELADQLL QNIPKEHLTR
VAKFLERQGF LKQALAVSQE PEHRFELALK VNNLNVAYDI ALASEDDDKW RQLNQVALAE
GNFQLALKSM CQDKDYSGQL LLASSLGDAD VMQRVANESM QSKLYNIAFM AHLLLGNRKE
CLEILITTGR LPEAAFFART YLPTEISRVV GLWKAKIMDK HPKLAESLAD PDGYPNLFPH
YADALQSDKL YEEIFSSTAL DAACFPLLSV AKPFTNCTLE NMVALVKDSK YSSGKNGITK
SNENEGDVQK ITETLQNVNI TAPLQSAQEG ASAEKTCTEF SPMKVISALK AEKDGEKAPD
VAQSSHRQPD LVPSVGGPDV LMHASTVEQS GGGVEDLQVP VPKSAVNLDM ENLDLSSAEL
NQQSDNDDDD NGGVDDNDDD EFSAF
//
