ID A0A0V0WID1_9BILA Unreviewed; 3654 AA.
AC A0A0V0WID1;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 24-JAN-2024, entry version 27.
DE SubName: Full=UDP-glucose:glycoprotein glucosyltransferase 1 {ECO:0000313|EMBL:KRX75381.1};
GN Name=mmaa-1 {ECO:0000313|EMBL:KRX75381.1};
GN ORFNames=T06_158 {ECO:0000313|EMBL:KRX75381.1};
OS Trichinella sp. T6.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Trichinellida; Trichinellidae; Trichinella.
OX NCBI_TaxID=92179 {ECO:0000313|EMBL:KRX75381.1, ECO:0000313|Proteomes:UP000054673};
RN [1] {ECO:0000313|EMBL:KRX75381.1, ECO:0000313|Proteomes:UP000054673}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ISS34 {ECO:0000313|EMBL:KRX75381.1};
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 -!- CATALYTIC ACTIVITY:
CC Reaction=N(4)-(alpha-D-Man-(1->2)-alpha-D-Man-(1->2)-alpha-D-Man-
CC (1->3)-[alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-[alpha-D-Man-(1->2)-
CC alpha-D-Man-(1->6)]-alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-beta-D-
CC GlcNAc-(1->4)-beta-D-GlcNAc)-L-asparaginyl-[protein] (N-glucan
CC mannose isomer 9A1,2,3B1,2,3) + UDP-alpha-D-glucose = H(+) + N(4)-
CC (alpha-D-Glc-(1->3)-alpha-D-Man-(1->2)-alpha-D-Man-(1->2)-alpha-D-
CC Man-(1->3)-[alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-[alpha-D-Man-
CC (1->2)-alpha-D-Man-(1->6)]-alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-
CC beta-D-GlcNAc-(1->4)-beta-D-GlcNAc)-L-asparaginyl-[protein] + UDP;
CC Xref=Rhea:RHEA:61304, Rhea:RHEA-COMP:14356, Rhea:RHEA-COMP:14357,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:58223, ChEBI:CHEBI:58885,
CC ChEBI:CHEBI:59080, ChEBI:CHEBI:139493;
CC Evidence={ECO:0000256|ARBA:ARBA00034426};
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000256|ARBA:ARBA00001913};
CC -!- PATHWAY: Protein modification; protein glycosylation.
CC {ECO:0000256|ARBA:ARBA00004922}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum lumen
CC {ECO:0000256|ARBA:ARBA00004319}.
CC -!- SIMILARITY: Belongs to the SIMIBI class G3E GTPase family. ArgK/MeaB
CC subfamily. {ECO:0000256|ARBA:ARBA00009625}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 8 family.
CC {ECO:0000256|ARBA:ARBA00006351}.
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:KRX75381.1}.
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DR EMBL; JYDK01000124; KRX75381.1; -; Genomic_DNA.
DR STRING; 92179.A0A0V0WID1; -.
DR UniPathway; UPA00378; -.
DR Proteomes; UP000054673; Unassembled WGS sequence.
DR GO; GO:0005788; C:endoplasmic reticulum lumen; IEA:UniProtKB-SubCell.
DR GO; GO:0005525; F:GTP binding; IEA:InterPro.
DR GO; GO:0003924; F:GTPase activity; IEA:InterPro.
DR GO; GO:0003980; F:UDP-glucose:glycoprotein glucosyltransferase activity; IEA:InterPro.
DR GO; GO:0006486; P:protein glycosylation; IEA:UniProtKB-UniPathway.
DR CDD; cd06432; GT8_HUGT1_C_like; 1.
DR CDD; cd03114; MMAA-like; 1.
DR Gene3D; 1.10.287.130; -; 1.
DR Gene3D; 1.20.5.170; -; 1.
DR Gene3D; 1.25.10.10; Leucine-rich Repeat Variant; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR Gene3D; 2.130.10.10; YVTN repeat-like/Quinoprotein amine dehydrogenase; 1.
DR InterPro; IPR011989; ARM-like.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR040497; Glyco_transf_24.
DR InterPro; IPR005129; GTPase_ArgK.
DR InterPro; IPR029044; Nucleotide-diphossugar_trans.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR029347; Raptor_N.
DR InterPro; IPR009448; UDP-g_GGtrans.
DR InterPro; IPR040693; UGGT_TRXL_1.
DR InterPro; IPR040694; UGGT_TRXL_2.
DR InterPro; IPR040692; UGGT_TRXL_3.
DR InterPro; IPR040525; UGGT_TRXL_4.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR InterPro; IPR036322; WD40_repeat_dom_sf.
DR InterPro; IPR001680; WD40_rpt.
DR NCBIfam; TIGR00750; lao; 1.
DR PANTHER; PTHR11226; UDP-GLUCOSE GLYCOPROTEIN:GLUCOSYLTRANSFERASE; 1.
DR PANTHER; PTHR11226:SF0; UDP-GLUCOSE:GLYCOPROTEIN GLUCOSYLTRANSFERASE; 1.
DR Pfam; PF18404; Glyco_transf_24; 1.
DR Pfam; PF03308; MeaB; 1.
DR Pfam; PF14538; Raptor_N; 1.
DR Pfam; PF18400; Thioredoxin_12; 1.
DR Pfam; PF18401; Thioredoxin_13; 1.
DR Pfam; PF18402; Thioredoxin_14; 1.
DR Pfam; PF18403; Thioredoxin_15; 1.
DR Pfam; PF06427; UDP-g_GGTase; 1.
DR PRINTS; PR01547; YEAST176DUF.
DR SMART; SM01302; Raptor_N; 1.
DR SMART; SM00320; WD40; 4.
DR SUPFAM; SSF48371; ARM repeat; 1.
DR SUPFAM; SSF53448; Nucleotide-diphospho-sugar transferases; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF50978; WD40 repeat-like; 1.
PE 3: Inferred from homology;
KW Endoplasmic reticulum {ECO:0000256|ARBA:ARBA00022824};
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Reference proteome {ECO:0000313|Proteomes:UP000054673};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Signal {ECO:0000256|ARBA:ARBA00022729};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:KRX75381.1}.
FT DOMAIN 2030..2183
FT /note="Raptor N-terminal CASPase-like"
FT /evidence="ECO:0000259|SMART:SM01302"
FT REGION 2250..2329
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2804..2825
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2904..2944
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 3114..3163
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 3186..3228
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2275..2301
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2302..2324
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 3117..3162
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 3654 AA; 411524 MW; 3041A4BC03679210 CRC64;
MEVLIFHLEN SNPLNLIESE VICGNESCFI TELSSMTVFC ANFTVESLLD ATVRSMWVFP
LIVVCFVSPV LVSPRKAHKN VIVSVRSKWP STSLIMEASE FMSKESNEKF WQFIEAVIDK
HQNSLGNKTD REVYNGILQI GDQILKSKAR LEFLKLALTV RVHSATVEMH RQIAATSLDV
QNGKSVYAVV HGKQISDLQQ LDTILKHAEA LARPVTYEFD HIYPGSKQGS VCVLLYADIE
NPHFKPWHLQ LKKLVQRDGI SYILRHYPKM NDDMVALSGY AVELAIKSTE YKAVDDSDKQ
TGSESGVSSS EEEVTDLNGF NLHLLEADEL TPLKVWQLQH LSFQAGQRVI LAPKEEALRV
LRDISQNFPI MARSLTRMSI NPNFKNEVEE NQADAFSKLN IEPGDSAFFI DGIVIDLEEK
DIFNLIELLK NEEMLISGLL KLGIRRKDFT LLYAMKGNDP NAEYAVDYTQ WSPHYINNLE
SDAAYRNWGN SIHAILQPYF PGMIRPIAKN FFTLIFVLRL GDRASQNLLS TAYQMYEHVL
PIRIGFIFVV NNDKSVSGYD DAGVAMLNAF NFIKEDRSVS KAIMFLIKIY NTSMRETISV
EDVHKLFKSS YRDENLKSVF NSEEYNQGRS SGVDFIKESG LSMVPMVLMN GYPFTAEEIS
PEHIEEAILS KVMRFTVDIQ KDVYEGNLKE NMDVQQHLLK KPTVLPKLNY NILQMENIFL
DMTDTSKYGA MSVEKFSHLD SSGKTQFIIE SILYLTKNDD DILRPVTLWI VADVESDDGQ
QFFLNAIKYL KYSVDMRIAL IHNPKSEAQA TKGTASLVQA CIQFLPLYQS KAVIGKIFAN
KITTLEDLIN LSPSGISWPE FKKAYNSMSD IWMQLHVHYA KFVLNLDPGV EAIVANGKVL
APLSASDFNS LKDFNFIERY LLTSGCNDIA QHLKIIPYLD KSPKALSDLV MRLYAFLRRY
NANEKRHWPI IENYHHSCVQ IEASDPTAAQ FDIVAIVDPL SPAAQKMSHL LVILSSVLNV
HMKVCMNCKS KLSEIPLKNF FRMVLPRELE FADDGSLKAQ SSARFSALPQ KQLFTLNIIA
PQSWMVESVE AVYDLDNIKM EEVKGDVVAK FQLEYILLEG RCFDERSGSP PRGLQFTLGT
FHEPFMFDTI VMANLGYFQL KANPGAWILA LREGKSAEIY EVKSVDGVVQ NQTTSVVILD
GFSGRMIHVK VAKKNDQLEN ELLAESEDAE SESLWQSISK TFQSGEKYDV INIFSLASGH
LYERFLRIMM LSVLKHTKTA VKFWLLKNYL SPGFKEFLPY MAGHYNFSYE LVQYKWPRWL
HQQTEKQRIM WGYKILFLDV LFPLDVKKII FVDADQVVRT DMLNLMELDL EGAPYAYTPF
CDSRKEMDGY RFWKQGYWEN HLAGRKYHIS ALYVVDLKKF RQVAAGDRLR GQYHFLSRDP
NSLSNLDQDL PNNMIHQVKI KSLPQEWLWC ETWCDDKSKK FAKTIDLNRN YNRQCELLKN
GKITIQKSKI YLIKERKIIV DIGFQFTAYF LVFLEESWNR AMNKENQVQD NRKAEITRRV
LESCFAGLKC FPAYYSDQKV KNDSVDCSRN SDKFKNYYRK HWDTDITVED ETVVGLKNRI
LKGDRSALAS AITLVESNHP TKRAQGECLL QSMLKISKKR FDEHGPKSLI FRIAITGAPG
AGKSTFIESF GLYLTRELKK KIAVLTIDPS SVRTGGSIMG DVARMNELSK EPNCYIRPSA
TAGTLGGVRR GTHESVVLCE GAGYDVVLIE TVGVGQSESA VANIADMVVL LLSPALGDEL
QGIKRGIMEI ADLILITKAD GDLLNQARLT RAEFSSALKY SRSRFHCWRP QVLLVSSRTN
KGITEIWNEM EHFRNALSEN GVLLQQRHQQ MLRWMWNHID HVLSGLFRHH PDVVKMLPQL
IREIQNDNVT PVTAGEKMEH FKKEHWKFRQ EKNMLEIKVS KAAEKVYTDG FDLANASGSV
NLKKNVRMSE ENDLHEEEPE RVPVSFADLR REQCEADNKI DPEFWRNRER MKTVSVALVL
CLNIGIDPPD TVKPKPCART ECWIDPQCMP MQKALESIGT ALQRQYQWWQ PRARYKQALD
PTVDDVRRLC ISMRKNAKEE RVLFHYNGHG VPRPTKNCEI WVFNKMFTQY IPLAIYDLQT
WMGAPGVYVW DCNGAAQAIR AFKTCAKKQI QAYRCSLAAM RKESTKTTVE FEPGVDLFQA
DDARQAELDR SRRRKTGLDC VSSKPLEVNF RSSSMVPDGP KIETSNKATA KDASKHLAGN
SSGNNNVRNG QHKNDGNNDG NTNGNDDDDD DDGDYDDDGE DDFDDDDPRK PKFKHCIQLA
ACARDQTLPT DPALPADLFT CCLTTPIRMA VMYYILQNKL TDRYPVCIAD RIPGSTGDRR
SPLGELNWIF TAITDTIAWN LLPSETFQRL FRQDLLIASL YRNYLLADRV MRSYYCTPVS
SPRLPPTHEH VMWQAWDMVV ESVLEQLDVQ ALVAEVEANE ATVMLPPGVP TAAGHGGAGV
GAGASTAVAA AAMPGGGTAT TGVSDAGSRA VGNDPTLTAG QQAQHDKVVA SVDYKNSPFF
SNQLIAFEVW LQYGFYQGSA PQQLPIVLQV LLSQVLRVRA LELLARFVDL GPKAVEQALA
VGIFPYILRL LQSVSRDMRP LLTFIWAKIL AVDNSCRLML LKDHVHRYFL VHLNDPTVEV
RRKLFAVFAL ARLMADCRQF QEAALCNGFV ATCSDLFSDC NDAPMRQWLA LALGHLWTDY
EAAKWQAIRC SLHQTLIGLL EDRLASVRAA AVFALGRLIS TGGAGDKENK QNDGDQGNHC
PNDEQSTNLA HSVAMSLVQH VCADSSATVR REALLGFFAF VRRFYPQFVT IAYEIDRELA
SSVPSRRHQH HELVSSYTVT TATVVGNNNN NNNNSNNHNH HNLSNGSSNS IASFSPQQQQ
RTRNFGISSS PVAANVDSST LVKSTSLLFQ PLLTAVSSSL NSSSNSMINI PLVRPSSRKS
VSWLFGLARA SQEHQKADNS KQEQSSQETI TVLSRREVRR HRSIGPAALV NVNNVYVSVW
RAVLKFLYDP DIEVSRLAHR LFKYVDRSVQ NLRLLSSVGH QDSVDSLPVR RRSTAGYFHS
SPDNGTAGQH PSPRPKFSFS GTHDHQQQQL VNDGNGNSGG YESPMGASPI ALCTYSAIYT
NPRRPVFGDG PASESSVHSS EASPETRRHL APEREIGTTA ASILSPPVDS EPVMKTDYLS
TCAQQFRSPM FYLLSESCAP SPAALNAQPR TTQRILPSFI ADRISLIHQH SSIEWNLLSD
KRKKYGKLWT YKNDFPATCM EFLPLEPLLC IGERDSVTVW NCNKGSVVAH FDNSSTSYTG
QSGSDLSGNL VYLTFVNPYT HGFILTGTDC GEVRVWDVRL INEPDLTSKV PKGSIDFALL
TAWMCADDAR RFHTKPFTCY FWEQDPGLLF AAGDFRNIIL WDAHTELKLA ELKVGAGGDT
YVCTLSADSN GHHLTAAGCS DGSVRLFDRR LPTSDSRIMT LRDLGRAVFK VHLEQASVGG
GGGGGGRLVA ASRSGQLCIW EPRMYREPVL FKDVGVRCRS SFDVHRYYPL IAAWNGAQVD
LINFDGKSMG LFRPDVSNMT TTLGRLAALR FHPVQVSIGL AEQDGQFSLY GLRP
//
