ID A0A0V1NPH6_9BILA Unreviewed; 3684 AA.
AC A0A0V1NPH6;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 24-JAN-2024, entry version 26.
DE SubName: Full=UDP-glucose:glycoprotein glucosyltransferase 1 {ECO:0000313|EMBL:KRZ85614.1};
GN Name=Uggt1 {ECO:0000313|EMBL:KRZ85614.1};
GN ORFNames=T08_4522 {ECO:0000313|EMBL:KRZ85614.1};
OS Trichinella sp. T8.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Trichinellida; Trichinellidae; Trichinella.
OX NCBI_TaxID=92180 {ECO:0000313|EMBL:KRZ85614.1, ECO:0000313|Proteomes:UP000054924};
RN [1] {ECO:0000313|EMBL:KRZ85614.1, ECO:0000313|Proteomes:UP000054924}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ISS272 {ECO:0000313|EMBL:KRZ85614.1};
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:KRZ85614.1}.
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DR EMBL; JYDM01000137; KRZ85614.1; -; Genomic_DNA.
DR STRING; 92180.A0A0V1NPH6; -.
DR UniPathway; UPA00378; -.
DR Proteomes; UP000054924; Unassembled WGS sequence.
DR GO; GO:0005788; C:endoplasmic reticulum lumen; IEA:UniProtKB-SubCell.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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 Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000054924};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Signal {ECO:0000256|ARBA:ARBA00022729};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:KRZ85614.1};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 12..37
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 2060..2213
FT /note="Raptor N-terminal CASPase-like"
FT /evidence="ECO:0000259|SMART:SM01302"
FT REGION 2280..2359
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2834..2855
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2934..2974
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 3144..3193
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 3216..3258
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2305..2328
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2331..2354
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 3147..3192
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 3684 AA; 415258 MW; F21207E5F6A4380F CRC64;
MTVFCANFTV ESLLEATVYS MWVFPLIVVC FVSPVLVSPR KAHKNVIVSV RSKWPSTSLI
MEASEFMSKE SNEKFWQFIE AVIDKHQNSL GNKTDREVYN GILQIGDQIL KSKARLEFLK
LALTVRVHSA TVEMHRQIAA TSLDVQNGKS VYAVVHGKQI SDLQQLDTIL KHAEALARPV
TYEFDHIYPG SKQGSVCVLL YADIENPHFK PWHLQLKKLV QRDGISYILR HYPKMNDDMV
ALSGYAVELA IKSTEYKAVD DSDKQTGSES GVSSSEEEVT DLNGFNLHLL EADELTPLKV
WQLQHLSFQA GQRVILAPKE EALRVLRDIS QNFPIMARSL TRMSINPNFK NEVEENQADA
FSKLNIEPGD SAFFIDGIVI DLEEKDIFNL IELLKNEEML ISGLLKLGIR RKDFTLLYAM
KGNDPNAEYA VDYTQWSPQY INNLESDAAY RNWGNSIHAI LQPYFPGMIR PIAKNFFTLI
FVLRLGDRAS QNLLSTAYQM YEHVLPIRIG FIFVVNNDKS VSGYDDAGVA MLNAFNFIKE
DRSVSKAVMF LIKIYNTSMR ETISVEDVHK LFKSSYRDEN LKSVFNSEEY NQGRSSGVDF
IKESGLSMVP MVLMNGYPFT AEEISPEHIE EAILSKVMRF TVDIQKDVYE GNLKENMDVQ
QHLLKKPTVL PKLNYNILQM ENIFLDMTDT SKYGAMSVEK FSHLDSSGKT QFIIESILYL
TKNDDDILRP VTLWIVADVE SDDGQQFFLN AIKYLKYSVD MRIALIHNPK SEAQATKGTA
SLVQACIQFL PLYQSKAVIG KIFANKITTL EDLINLSPSG ISWPEFKKAY NSMSDIWMQL
HVHYAKFVLN LDPGVGAIVA NGKVLAPLSA SDFNSLKDFN FIERYLLTSG CNDIAQHLKI
IPYLDKSPKA LSDLVMRLYA FLRRYNANEK RHWPIIENYH HSCIQIEASD PTAAQFDIVA
IVDPLSPAAQ KMSHLLVILS SVLNVHMKVC MNCKSKLSEI PLKNFFRMVL PRELEFADDG
SLKAQPSARF SALPQKQLFT LNIIAPQSWM VESVEAVYDL DNIKMEEVKG DVVAKFQLEY
ILLEGRCFDE RSGSPPRGLQ FTLGTFHEPF MFDTIVMANL GYFQLKANPG AWILALREGK
SAEIYEVKSV DGVVQNQTTS VVILDGFSGR MIHVKVAKKN DQLENELLAE SEDAESESLW
QSISKTFQSG EKYDVINIFS LASGHLYERF LRIMMLSVLK HTKTAVKFWL LKNYLSPGFK
EFLPYMAGHY NFSYELVQYK WPRWLHQQTE KQRIMWGYKI LFLDVLFPLD VKKIIFVDAD
QVVRTDMLNL MELDLEGAPY AYTPFCDSRK EMDGYRFWKQ GYWENHLAGR KYHISALYVV
DLKKFRQVAA GDRLRGQYHF LSRDPNSLSN LDQDLPNNMI HQVKIKSLPQ EWLWCETWCD
DKSKKFAKTI DLCNNPMTKE PKLQSAMRII EEWKDYDSEI KDLLDQRTKD KWNITEQKIV
DIGFQFTVYF LVFLEESWNR AMNKENQVQD NQSDDLPQAT ESINNATEMK ARQRGMIEKK
LRKYVVGIKN QNSLMKLRIM PANSLGTLRL SNRRLSKKSC GKLLCSDQKM KNDSVDCSRN
RDKFKNYYRK HWDTDITVED ETVVGLKNRI LKGDRSALAS AITLVESNHP TKRAQGECLL
QSMLKISKKR FDEHGPKSLI YRIAITGAPG AGKSTFIESF GLYLTRELKK KIAVLTIDPS
SERTGGSIMG DVARMNELSK EPNCYIRPSA TAGTLGGVRR GTHESVVLCE GAGYDVVLIE
TVGVGQSESA VANIADMVVL LLSPALGDEL QGIKRGIMEM ADLILVTKAD 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
QAYRCSLAAR RKESTKTTVE FEPGVDLFQA DDARQAELDR SRRRKTGLDC VSSKPLEVNF
RSSSMVPDGP KIETNNKATA KDASKHLAGN SSGNNNVRNG QHKNDGNNDD 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 TATIVGNNNN
NNNNSNNHNH HNLSNGSSNS IASFSPQQQQ RTRNFGISSS PVAANVDSST LVKSTSLLFQ
PLLTAVSSSL NSSSNSMINI PLVRPSSRKS VSWLFGLARS SQENQKADNS KQEQSSQETI
TVLSRREVRR HRSIGPAALV NVNNVYVSVW RAVLKFLYDP DIEVSRLAHR LFKYVDRSVQ
NLRLLSSVGH QDSVDSLPVR RRSTAGYFHS SPDNGTAGQH PSPRPKFSFS GTHDHHQQQL
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
AAGDFRSIIL WDAHTELKLA ELKVGAGGDT YVCTLSADSN GHHLTAAGCS DGSVRLFDRR
LPTSDSRIMT LRDLGRAVFK VHLEQASVGG GGGGGGRLVA ASRSGQLCIW EPRMYREPVL
FRDVGVRCRS SFDVHRYYPL IAAWNGAQVD LINFDGKSMG LFRPDVLNMT TTLGRLAALR
FHPVQVSIGL AEQDGQFSLY GLRP
//
