ID A0A0V0ULR6_9BILA Unreviewed; 2177 AA.
AC A0A0V0ULR6;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 38.
DE SubName: Full=Coatomer subunit beta {ECO:0000313|EMBL:KRX52350.1};
GN ORFNames=T09_5853 {ECO:0000313|EMBL:KRX52350.1};
OS Trichinella sp. T9.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Trichinellida; Trichinellidae; Trichinella.
OX NCBI_TaxID=181606 {ECO:0000313|EMBL:KRX52350.1, ECO:0000313|Proteomes:UP000054681};
RN [1] {ECO:0000313|EMBL:KRX52350.1, ECO:0000313|Proteomes:UP000054681}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ISS409 {ECO:0000313|EMBL:KRX52350.1};
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:KRX52350.1}.
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DR EMBL; JYDN01000253; KRX52350.1; -; Genomic_DNA.
DR Proteomes; UP000054681; 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:UP000054681};
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 1265..1306
FT /note="WD"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00221"
FT REPEAT 1308..1350
FT /note="WD"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00221"
FT REPEAT 1351..1394
FT /note="WD"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00221"
FT REPEAT 1395..1436
FT /note="WD"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00221"
FT REGION 2083..2177
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2155..2177
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2177 AA; 247834 MW; 194CD6C9B1B604FF CRC64;
MAYNGVTLKI ASRRRSEMRI FRRSVASAWK FGLAIIVVVF FISSVALYNI MDSVTPSSQK
LRYFGEYDLK RLETKLIKLE SEANRNEEIL GQIQRSLYYR LNRVRSRPPA STLSAVKKKE
RKQTYRKCNA GLLNTTVNVQ MLSVYETLEF DNPDGGHWKQ GWEINYDKNE 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 NNYEKLFDYM NRQDWNVQFG TLEDYYRALF
KRADVGGETF PTLSGDFFTY ADRNEDYWSG YYTSRPLYKR MERILASFLR GAEIMFNLAV
SDVRSKALGH QFPSQRLFNN LVIARRNLAL FQHHDGIAGT AKTPVVMDYA KRLWSSIELS
KATMATAILY FMRKASTSLL DADSIKLDFS ERIMDASHTS ENVVINVLDE NERSILVYNS
LPYFRSEIVC INVDTYKIAL YDAANNRLKI QISPVITKTS VGFIISVTTY QVCWTATMES
LSIIRYRLVS GDDPLDGEMV TISQREVVHS STFPRNVLSE EQFDIVSPVY VATFSTSTGL
LKELKHTNKD NKMNLQLEFF VYKSKSQSYT AGGAYLFLPK GEAEPLNNVD DVLLLEGDMF
ATVYSNLKNV LHQFTVVKLE VPGAESLHIR NTVDITTEIE DFEIVMRLKA DIHNSDHSFY
TDLNGLQMIK RKYFSKIPLQ GNFYPMTTAA FIEDSAHRLT LLSAQANGVT SIKPGWIEVF
LDRRTHVDDS RGVAQPMLDN VIVTSDFRLM LESLDSDAYK IGKNLPTINY LTLPAHHQSL
LLIYPVFVLY TASDFVEELR SHYQALQKPF PCDFHLINMR SVESKGAFDS KAEVESFLNE
TLLILLRLEN SCFSTQPPSI VCSLKDNDVP TAVDIFGTNV KAVKEMSLTA LYELNDTKLP
DEPLYVEPME IKTYKIEWKS AQDAAEHKSP LPLRLDVKRK LLARSDRVKC VDLHPTEPWM
LCSLYNGNVH AWNYETQTLL KSFEVCDLPV RSAKFVPRKS WVLTGSDDMQ VRVFNYNTLE
RVHQFEAHSD YLRSIAVHAT QPLVLTSSDD MTIKLWDWES NWQLKQTFEG HTHYVMQVLF
NPKDNNTFAS ASLDRTVKIW QLGSSHPNFT LEGHEKGVNC IDYYHGGDRP YLISGADDRL
VKIWDYQNKT CVATLEGHVQ NVSSVCFHPD LPVIITGSED NTVRIWHGST YRMETTLNYG
LDRVWTICAL KGQNVVAIGY DEGSIIVKLG REEPAVSMDA NGKLLWAKHA EIQQANLKAV
CNEAEYPDGA RLSLSAKDMG AIEFYPRSIQ HSPNGRFVVV RGESEYVIYT AMALRNKSYG
AAVEFVWAKE SNMYAIRDVS SSILVEIHKN FTRYKTVYAE ASIDCIFGGT LLGIRCGGQL
IFYDWETIHV IRRIDIKAHQ VYWSEKELLA ITTASEFYIL QFNEAEVISQ LSESETPSPD
GVEEAFDVIH TGTEDISTAY WVGDCLVYTT INNRLRYCVG SETVTIAHLD RGLYILGYLP
QENRLFLSDK DLNVVSYQLV LSVLEYQTAV MRHDFELADQ LLQNIPKEHL TRVAKFLERQ
GFLKQALAVS QEPEHRFELA LKVNNLNVAY DIALASEDDD KWRQLNQVAL AEGNFQLALK
SMCQDKDYSG QLLLASSLGD ADVMQRVANE SMQSKLYNIA FMAHLLLGNR KECLEILITT
GRLPEAAFFA RTYLPTEISR VVGLWKAKIM DKHPKLAESL ADPDGYPNLF PHYADALQSD
KLYEEIFSST ALDAACFPLL SVAKPFTNCT LENMVALVKD SKYSSGKNGI TKSNENEADV
QKITETLQNV NITAPLQSAQ EGASAEKTCT EFSPMKAISA LKAEKDGEKA PDVAQSSHRQ
PDLVPSVGGP DVLMHASTVE QSGGGVEDLQ VPVPKNEVNL DMENLDLSSA ELNQQSDNDD
DDDGGVDDND DDEFSAF
//
