ID A0A0V1H262_9BILA Unreviewed; 3766 AA.
AC A0A0V1H262;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 41.
DE RecName: Full=Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit STT3A {ECO:0000256|ARBA:ARBA00040922};
DE EC=2.4.99.18 {ECO:0000256|ARBA:ARBA00012605};
DE EC=6.1.1.10 {ECO:0000256|ARBA:ARBA00012838};
GN Name=AGO2 {ECO:0000313|EMBL:KRZ04635.1};
GN ORFNames=T11_3251 {ECO:0000313|EMBL:KRZ04635.1};
OS Trichinella zimbabwensis.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Trichinellida; Trichinellidae; Trichinella.
OX NCBI_TaxID=268475 {ECO:0000313|EMBL:KRZ04635.1, ECO:0000313|Proteomes:UP000055024};
RN [1] {ECO:0000313|EMBL:KRZ04635.1, ECO:0000313|Proteomes:UP000055024}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ISS1029 {ECO:0000313|EMBL:KRZ04635.1};
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=a dolichyl diphosphooligosaccharide + L-asparaginyl-[protein]
CC = a dolichyl diphosphate + H(+) + N(4)-(oligosaccharide-(1->4)-N-
CC acetyl-beta-D-glucosaminyl-(1->4)-N-acetyl-beta-D-glucosaminyl)-L-
CC asparaginy-[protein]; Xref=Rhea:RHEA:22980, Rhea:RHEA-COMP:9529,
CC Rhea:RHEA-COMP:12635, Rhea:RHEA-COMP:12804, Rhea:RHEA-COMP:12805,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:50347, ChEBI:CHEBI:57497,
CC ChEBI:CHEBI:57570, ChEBI:CHEBI:132529; EC=2.4.99.18;
CC Evidence={ECO:0000256|ARBA:ARBA00034064};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000256|ARBA:ARBA00001936};
CC -!- PATHWAY: Protein modification; protein glycosylation.
CC {ECO:0000256|ARBA:ARBA00004922}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000256|ARBA:ARBA00004477}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004477}. Membrane
CC {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: Belongs to the STT3 family.
CC {ECO:0000256|ARBA:ARBA00010810}.
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:KRZ04635.1}.
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DR EMBL; JYDP01000159; KRZ04635.1; -; Genomic_DNA.
DR UniPathway; UPA00378; -.
DR Proteomes; UP000055024; Unassembled WGS sequence.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005768; C:endosome; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004579; F:dolichyl-diphosphooligosaccharide-protein glycotransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004825; F:methionine-tRNA ligase activity; IEA:UniProtKB-EC.
DR GO; GO:0035091; F:phosphatidylinositol binding; IEA:InterPro.
DR GO; GO:0004672; F:protein kinase activity; IEA:InterPro.
DR GO; GO:0003723; F:RNA binding; IEA:InterPro.
DR GO; GO:0008757; F:S-adenosylmethionine-dependent methyltransferase activity; IEA:InterPro.
DR GO; GO:0006431; P:methionyl-tRNA aminoacylation; IEA:InterPro.
DR GO; GO:0006486; P:protein glycosylation; IEA:UniProtKB-UniPathway.
DR CDD; cd02440; AdoMet_MTases; 1.
DR CDD; cd13337; FERM-like_C_SNX17; 1.
DR CDD; cd07061; HP_HAP_like; 1.
DR CDD; cd00814; MetRS_core; 1.
DR CDD; cd02846; PAZ_argonaute_like; 1.
DR CDD; cd04657; Piwi_ago-like; 1.
DR Gene3D; 2.170.220.10; -; 1.
DR Gene3D; 3.40.50.12610; -; 1.
DR Gene3D; 3.40.50.2300; -; 1.
DR Gene3D; 3.40.50.620; HUPs; 1.
DR Gene3D; 2.170.260.10; paz domain; 2.
DR Gene3D; 3.40.50.1240; Phosphoglycerate mutase-like; 1.
DR Gene3D; 3.30.1520.10; Phox-like domain; 1.
DR Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 1.
DR Gene3D; 3.30.420.10; Ribonuclease H-like superfamily/Ribonuclease H; 1.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR InterPro; IPR033379; Acid_Pase_AS.
DR InterPro; IPR014811; ArgoL1.
DR InterPro; IPR032472; ArgoL2.
DR InterPro; IPR032473; Argonaute_Mid_dom.
DR InterPro; IPR032474; Argonaute_N.
DR InterPro; IPR000560; His_Pase_clade-2.
DR InterPro; IPR029033; His_PPase_superfam.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR014758; Met-tRNA_synth.
DR InterPro; IPR015413; Methionyl/Leucyl_tRNA_Synth.
DR InterPro; IPR013216; Methyltransf_11.
DR InterPro; IPR033911; MetRS_core.
DR InterPro; IPR003674; Oligo_trans_STT3.
DR InterPro; IPR003100; PAZ_dom.
DR InterPro; IPR036085; PAZ_dom_sf.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR003165; Piwi.
DR InterPro; IPR045246; Piwi_ago-like.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR001683; PX_dom.
DR InterPro; IPR036871; PX_dom_sf.
DR InterPro; IPR012337; RNaseH-like_sf.
DR InterPro; IPR036397; RNaseH_sf.
DR InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR InterPro; IPR048763; SNX17-31_FERM_F1.
DR InterPro; IPR040842; SNX17/31_FERM.
DR InterPro; IPR037836; SNX17_FERM-like_dom.
DR InterPro; IPR048999; STT3-PglB_core.
DR InterPro; IPR048307; STT3_N.
DR InterPro; IPR009080; tRNAsynth_Ia_anticodon-bd.
DR NCBIfam; TIGR00398; metG; 1.
DR PANTHER; PTHR13872; DOLICHYL-DIPHOSPHOOLIGOSACCHARIDE--PROTEIN GLYCOSYLTRANSFERASE SUBUNIT; 1.
DR PANTHER; PTHR13872:SF43; DOLICHYL-DIPHOSPHOOLIGOSACCHARIDE--PROTEIN GLYCOSYLTRANSFERASE SUBUNIT STT3A; 1.
DR Pfam; PF08699; ArgoL1; 1.
DR Pfam; PF16488; ArgoL2; 1.
DR Pfam; PF16487; ArgoMid; 1.
DR Pfam; PF16486; ArgoN; 1.
DR Pfam; PF00328; His_Phos_2; 1.
DR Pfam; PF08241; Methyltransf_11; 1.
DR Pfam; PF02170; PAZ; 1.
DR Pfam; PF02171; Piwi; 1.
DR Pfam; PF00069; Pkinase; 1.
DR Pfam; PF00787; PX; 1.
DR Pfam; PF21273; SNX17-27-31_F1_FERM; 1.
DR Pfam; PF18116; SNX17_FERM_C; 1.
DR Pfam; PF02516; STT3; 1.
DR Pfam; PF21436; STT3-PglB_core; 1.
DR Pfam; PF09334; tRNA-synt_1g; 1.
DR PRINTS; PR01041; TRNASYNTHMET.
DR SMART; SM01163; DUF1785; 1.
DR SMART; SM00950; Piwi; 1.
DR SMART; SM00312; PX; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF47323; Anticodon-binding domain of a subclass of class I aminoacyl-tRNA synthetases; 1.
DR SUPFAM; SSF52374; Nucleotidylyl transferase; 1.
DR SUPFAM; SSF101690; PAZ domain; 1.
DR SUPFAM; SSF53254; Phosphoglycerate mutase-like; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR SUPFAM; SSF64268; PX domain; 1.
DR SUPFAM; SSF53098; Ribonuclease H-like; 1.
DR SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
DR PROSITE; PS00616; HIS_ACID_PHOSPHAT_1; 1.
DR PROSITE; PS50821; PAZ; 2.
DR PROSITE; PS50822; PIWI; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS50195; PX; 1.
PE 3: Inferred from homology;
KW Aminoacyl-tRNA synthetase {ECO:0000256|ARBA:ARBA00023146};
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Endoplasmic reticulum {ECO:0000256|ARBA:ARBA00022824};
KW Endosome {ECO:0000256|ARBA:ARBA00022753};
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Glycosyltransferase {ECO:0000256|ARBA:ARBA00022676};
KW Ligase {ECO:0000256|ARBA:ARBA00022598};
KW Lipid-binding {ECO:0000256|ARBA:ARBA00023121};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Manganese {ECO:0000256|ARBA:ARBA00023211};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917};
KW Reference proteome {ECO:0000313|Proteomes:UP000055024};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 2781..2801
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 2813..2832
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 2838..2856
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 2868..2901
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 2907..2927
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 2934..2954
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 2966..2984
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 2996..3018
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 3058..3077
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 3084..3102
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 3108..3131
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 3152..3173
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 1378..1489
FT /note="PX"
FT /evidence="ECO:0000259|PROSITE:PS50195"
FT DOMAIN 2083..2150
FT /note="PAZ"
FT /evidence="ECO:0000259|PROSITE:PS50821"
FT DOMAIN 2151..2175
FT /note="PAZ"
FT /evidence="ECO:0000259|PROSITE:PS50821"
FT DOMAIN 2379..2644
FT /note="Piwi"
FT /evidence="ECO:0000259|PROSITE:PS50822"
FT DOMAIN 3403..3678
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 1849..1893
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2648..2678
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1852..1886
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2653..2678
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 3766 AA; 430335 MW; 4395019892270DC8 CRC64;
MEIYPKSVEK MIGKPSTFLM KRLSEELQCP TSSMLGRLAS VMYLRKFKEI SSNVMNILNP
SADDRILEVG FGLGYGLLEA FKKVENGNGV VFGSERSQYM VKRARKIFAL EIHYGKLEVH
LSLASHLPYL NNSIDCIFHN DCFYYWPSVK NALLELKRVL KPGGRMLTSM SIERVKEWNS
RGLLQSSYCI DPLDYILYLE NTGFVDIKFE YHSSAGVQFQ TVTALKPPVE EDRGVNLDVE
EKNFEQEILE FEKLQRWRKL AKVENDNKFK QVLKARLLHR GISYFVTTPI YYANSGPHLG
HLYSSLIADA AHRWFKLKNP HQLTLFSSGT DEHGSKVENA ALKAEKNVDV YCSEISSAYR
ELFSKFGIQT TDFIRTVETR HHQSVQQFWE VLRKNNFIYK GKYSGWYCSA DECFYNESDL
CDDETKSCKT TTAGHTVEWV VEENYLFKLS EFLPEIEHWL QTSDVIQPSQ YLPFVMNQLK
QLSDVSISRD RQRLSWGIPV PDDCSQTIYV WFDALVNYLT VAGYPGELSR WPPDCHIIGK
DILKFHAILW PAMLLAANFP LPKQIFCHGH WLSDGVKMSK SLGNVVDPTL EAQQLTCQGL
RYFLLRQGVP TSDGNYSTPL AISVLNDELA NSIGNLINRT TSSRVLRGDR FTDFDESVIN
GPSIQQGPDL ITDLDNLPSI VGQQYDKMQF SNGINSIVTV VKKANAFVQH FSPWHLAKDK
NANSLLDTVL HLAHQTLRTC GILLKPIVPD IAGEMLNRLS VSSDESNYSD CSKAASKSRY
FSGKPFNRQK DLLLFPRISR YFGKLPIQIN CQIIQDAFHS CCTSCMELID ELFQFTVQMQ
LILVQTIWRH GHRTPIYLIP SDVENNASTW DIGLGELTKL GMRQCYELGQ MLGKRYIEQY
PLFKSSILNE IYIRSSDTNR TLMSAASVMA GFVESDSYGN YRNYTLPNFV RSPAGWTPLP
IHTVAYGADN LLNMKYYWNK TADLFRENLM KYQQFTKQNP DNAAKLAYVA NKSGFNNTLV
KNMWILADVV KIEKEGSSED WHSDQHKLPD WVTDEIYDWI EDTFKHWCKF AYQPDLLIQI
IAGELIFEIV DRIRQKQLSI KQGQNTNSWI EKIKFYSYSG HDINLLFLLY ILGQYDNAST
VEYEGYASCI VFETWLTEEN EIEIKVFLRR GPNSTQFQPI QVVGCPPIPS GCPLATFENR
TGKFFPKPNK VDVDRCSSAA FSIFNNFLSI RSKRMAIVNG STPRLPMALP LRPTLMPTRF
PARKACLSLT RIDHQCNDIF QFFYMLPLKD KKLCALSMGD HFHYLWTSVA FDLIIINYFG
CSMTDSHSTL HHCSIIVFNP MLDGESATRS RITNAATDCR QLAKLSDVQV PSMEASSHLV
MLHISIPCSR QATDSSGKAY TIFEIYINNA YHCSSRYSQL LRLHEIIKKI LPKDVPNFPP
KYINALAGDR LLNERREALQ EYLRTVFSIK EVIRNIRVQQ FFLDAQRESA SLAARQLSNE
VPVYLLDGSK YIIQCCPGDS TNVVLERLAV IVGLPIELTR YFGLFIVTKS EVFPYKIIRW
LENFECPLLS LFYVAKLGIK AKIILKKKYF DSSIESSLIK KEQALRILYS QAVFDVKIFL
SRQGCLTFAS RKCRWQLIDE KYFPSLMKNT DAVNSPDEYL RCCQEQPWYG FVFFEQCLCS
YPKMNTVAHV AVGNRRLLIL HEGEIKEITF RVTRIRSWRL SIIVFVEQEF FTMLIIAEKS
FFQSIHGSQD LSFEYLFSNN HLEWITLRSS QSVLISCCLQ SMIEEIVNSQ SDAIASASSK
KMMPIVESGV ILNESSLESS LNSSLKPKRS LHDTFEAIRW SCCCFTVKPG PSKSSAKPST
SKDPVNSNTN GSQYSGSQQQ NEEPTPRRPN FGKLGDQICL RANHFQVRIP SGNLYHYELV
IEPERYHRDI IETMIQTYQK VFSNGRPVYD GKKSLFCKEM LPIGRDWVEL DVTMPTERED
RRYQVGIKLT SQVSLCRLQD ALDGRTRFLP QDTVDALDII LRHLPSLKYT PVGRSFFSPP
ERFFHPLGGG REVWFGFHQS IRPSQWKMML NIDVSATAFY KSMTVIDFLA EVLDAPHIPE
SRRALSDAQR VKFTKEIKGL KVEITHCGQM RRRYRVCNVT RRPAQTQTYP HLPCLQVGLE
QKHTYLPLEV CNLVPGQRCI KKLTDTQTSS MIKATARSAP DREQEINELV KRADFNNDPF
AREFGISISP FMAEVYGRVL APPKLLYGGR TRATALPEKG VWDMRGKQFH TGVDIRNWAI
ACFTPPHMCR EDNLRTFIQQ LQKISHDAGM SIVGQPCFCK YAAGADQVEP MFRYLKSQYP
QLQLVIVILP GKTPVYAEVK RVGDTLLGVA SQCVQAKNIN VKLGGVNNIL LPSIRPKVFN
EPVIFMGADI THPPAGDGRK PSIAAVVGSM DAHPSRYGAS VRMQYPRRVP DERTGRMKDE
RPEKIEDLAI MVKELLIQFY QSTRFKPTRI ILYRDGVSEG QFYQVLQHEL GAMREACIML
ERGYQPGITY VAVQKRHHTR LFCAEKRDMQ GKSGNIPAGT AVDSGITHPQ EFDFYLCSHA
GIQGTSRPSY YHVLWDDNNF SADEMQQLTY QLCHTYVRCT RSVSIPAPAY YAHLVAFRAR
YHLVDRDHDS GEGSVNSAAT ENGENGGEEG SPSSSSSSLS RAVVIHPNST RVICKFAFLF
NHAEGVFKAC IAASGDVAED DGFGFGSPFS TRLFSVLRFE SVIHEFDPYF NYRTTRYLTE
EGFYKFHNWF DDQAWYPLGR IIGGTIYPGL MVTSTFIYRI LHFFNITLHI REICVFLAPL
FSSFTTLITY LLTSEFKGDG AGLIAAGMIA IIPGYISRSV AGSYDNEGIA IFCMLLTYYF
WIKAVKTGSI FWSTLCALAY FYMVSSWGGY VFLINLIPLH VLTLLCCSRF SHRIYIAYSV
VYTLGTILSM QIPFVGFQPV STSEHMAAFG VFGIVQIYAF FAYIRSKSTD AQFNYLFRTI
ITFVAIAGIS VILLAEFFGK IAPWTGRFYS LLDPSYAKNH IPIIASVSEH QPTTWSSFYL
DTHISVFLFP AGLYFCFKNL NDANIFIILY AVTSIYFAGV MVRLMLVLAP VMCVISGIAA
SSIFESFLRN FSPSTSTGLE KKSKKHENGY SWKNEVATTV VFILTLFFIN YTFHCTTITE
TAYSSPSIVL SARSGHGNPI IFDDFREAYY WLRMNTPPDS KIMSWWDYGY QITAMANRTV
LVDNNTWNNT HISRVGQAMS SPEDKAYEIM QELDVDYVLV IFGGLIGYAS DDINKFLWMI
RIGGSTEKGK HIKEEDYYSA TGEYRVDKEG SKTMLNSMMY KFSYYRFGDV YTEMDKPSGY
DRVRGSEIGN KKIQFQHFEE AFTSEHWLDT SLVHLNEVVD ERYKVKKLLG KGGFGAVYQV
LDQNTNKMGA MKIEMSSQDF KSLKMEVLVL KELVANESRN CCDLFSVGNK PNYSYIVMTL
VGPSLHSLAQ SIGSKRLSLR SSIHLGIRCL RALEDLHFCG YVHRDVKPMN YAIGREPEYR
RVFILDFGMC RKYVRDDGAH KRPRSECGFR GTLWYASPMS LSGQEQSRRD DLWSWYFTIL
ELLTGTVPWQ NVQIKRGASF AEKKQVFMEK KMEFIKNPAD GLRGLPREFV AIMEYLATLQ
YFDCPNYGYI YQLIMTTFRR HSYDIDQPLD WEPTGQFHEE TIMAPDHNML PGNNTEHRAH
FLQKFKLFGS FCTDDLKLFA ERKARTSVLR HVQAPLWKGF RAKNIK
//
