ID A0A0V1KQT1_9BILA Unreviewed; 2186 AA.
AC A0A0V1KQT1;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 36.
DE SubName: Full=Coatomer subunit beta {ECO:0000313|EMBL:KRZ49479.1};
GN Name=Copb2 {ECO:0000313|EMBL:KRZ49479.1};
GN ORFNames=T02_13415 {ECO:0000313|EMBL:KRZ49479.1};
OS Trichinella nativa.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Trichinellida; Trichinellidae; Trichinella.
OX NCBI_TaxID=6335 {ECO:0000313|EMBL:KRZ49479.1, ECO:0000313|Proteomes:UP000054721};
RN [1] {ECO:0000313|EMBL:KRZ49479.1, ECO:0000313|Proteomes:UP000054721}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ISS10 {ECO:0000313|EMBL:KRZ49479.1};
RA Korhonen P.K., Edoardo P., Giuseppe L.R., Gasser R.B.;
RT "Evolution of Trichinella species and genotypes.";
RL Submitted (MAY-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:KRZ49479.1}.
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DR EMBL; JYDW01000310; KRZ49479.1; -; Genomic_DNA.
DR STRING; 6335.A0A0V1KQT1; -.
DR Proteomes; UP000054721; 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; 2.
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:UP000054721};
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 1272..1313
FT /note="WD"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00221"
FT REPEAT 1315..1357
FT /note="WD"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00221"
FT REPEAT 1358..1401
FT /note="WD"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00221"
FT REPEAT 1402..1443
FT /note="WD"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00221"
FT REGION 2093..2186
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2164..2186
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2186 AA; 248897 MW; 50AB61F74BCC3649 CRC64;
MAYNGVTLKI ASKRRSEMRI FRRSVASAWK FGLAIIVVVF FISSVALYNI MDSVTPSSQK
LRYFGEYDLK RLETKLIKLE SEANRNEEIL GQIQRSLYYR LNRVRNRPPA STLSAVKKKE
RKQTYRKCNA GLLNTTVNVQ MLSVYETLEF 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 GAEIMFNLAV
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 GDAQHAKLPG AESLHIRNTV DITTEIEDFE IVMRLKADIH
NSDHSFYTDL NGLQMIKRKY FSKIPLQGNF YPMTTAAFIE DSAHRLTLLS AQANGVTSIK
PGWIEVFLDR RTHVDDSRGV AQPMLDNVIV TSDFRLMLES LDGDAYKIGK NLPTINYLTL
PAHHQSLLLI YPVFVLYTAN DFVEELRSHY QALQKPFPCD FHLINMRSVE SKGAFDSKAE
VESFLNETLL ILLRLENSCF STQPPSIVCS LKDNDVPTAV DIFGTNVKAV KEMSLTALYQ
LNDTKLPDEP LYVEPMEIKT YKIEWKSAQD AAEHKSPLPL RLDVKRKLLA RSDRVKCVDL
HPTEPWMLCS LYNGNVHAWN YETQTLLKSF EVCDLPVRSA KFVPRKSWVL TGSDDMQVRV
FNYNTLERVH QFEAHSDYLR SIAVHATQPL VLTSSDDMTI KLWDWESNWQ LKQTFEGHTH
YVMQVLFNPK DNNTFASASL DRTVKIWQLG SSHPNFTLEG HEKGVNCIDY YHGGDRPYLI
SGADDRLVKI WDYQNKTCVA TLEGHVQNVS SVCFHPDLPV IITGSEDNTV RIWHGSTYRM
ETTLNYGLDR VWTICALKGQ NVVAIGYDEG SIIVKLGREE PAVSMDANGK LLWAKHAEIQ
QANLKAVCNE AEYPDGARLS LSAKDMGAIE FYPRSIQHSP NGRFVVVRGE SEYVIYTSMA
LRNKSYGAAV EFVWAKESNM YAIRDVSSSI LVEIHKNFTR YKTVYAEASI DCKCIFGGTL
LGIRCGGQLI FYDWETIHVI RRIDIKAHQV YWSEKELLAI TTASEFYILQ FNEAEVISQL
SESETPSPDG VEEAFDVIHT GTEDISTAYW VGDCLVYTTI NNRLRYCVGS ETVTIAHLDR
GLYILGYLPQ ENRLFLSDKD LNVVSYQLVL SVLEYQTAVM RHDFELADQL LQNIPKEHLT
RVAKFLERQG FLKQALAVSQ EPEHRFELAL KVNNLNVAYD IALASEDDDK WRQLNQVALA
EGNFQLALKS MCQDKDYSGQ LLLASSLGDA DVMQRVANES MQSKLYNIAF MAHLLLGNRK
ECLEILITTG RLPEAAFFAR TYLPTEISRV VGLWKAKIMD KHPKLAESLA DPDGYPNLFP
HYADALQSDK LYEEIFSSTA LDAACFPLLS VAKPFRNCTL ENMVALVKDS KYSSGKNGIT
KSNENEGDVQ KITETLQNVN ITAPLQSAQE GASAEKTCTE FSPMRAISAL KAEKDGEKAP
DVAQSSHRQP DLVPSVGGPD VLMHASTVEQ SGGGVEDVQV PVPKSAVNLD MENLDLSSAE
LNQQSDNDDD DDGGVDDNDD DEFSAF
//
