ID A0A0B7NC98_9FUNG Unreviewed; 876 AA.
AC A0A0B7NC98;
DT 01-APR-2015, integrated into UniProtKB/TrEMBL.
DT 01-APR-2015, sequence version 1.
DT 03-MAY-2023, entry version 34.
DE RecName: Full=Dolichyl-phosphate-mannose--protein mannosyltransferase {ECO:0000256|ARBA:ARBA00012839, ECO:0000256|RuleBase:RU367007};
DE EC=2.4.1.109 {ECO:0000256|ARBA:ARBA00012839, ECO:0000256|RuleBase:RU367007};
GN Name=PARPA_10442.1 scaffold 40485 {ECO:0000313|EMBL:CEP16196.1};
OS Parasitella parasitica.
OC Eukaryota; Fungi; Fungi incertae sedis; Mucoromycota; Mucoromycotina;
OC Mucoromycetes; Mucorales; Mucorineae; Mucoraceae; Parasitella.
OX NCBI_TaxID=35722 {ECO:0000313|EMBL:CEP16196.1, ECO:0000313|Proteomes:UP000054107};
RN [1] {ECO:0000313|EMBL:CEP16196.1, ECO:0000313|Proteomes:UP000054107}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 412.66 {ECO:0000313|EMBL:CEP16196.1,
RC ECO:0000313|Proteomes:UP000054107};
RA Ellenberger Sabrina;
RL Submitted (SEP-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Transfers mannose from Dol-P-mannose to Ser or Thr residues
CC on proteins. {ECO:0000256|RuleBase:RU367007}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a dolichyl beta-D-mannosyl phosphate + L-seryl-[protein] = 3-
CC O-(alpha-D-mannosyl)-L-seryl-[protein] + a dolichyl phosphate + H(+);
CC Xref=Rhea:RHEA:17377, Rhea:RHEA-COMP:9517, Rhea:RHEA-COMP:9527,
CC Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:13546, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:29999, ChEBI:CHEBI:57683, ChEBI:CHEBI:58211,
CC ChEBI:CHEBI:137321; EC=2.4.1.109;
CC Evidence={ECO:0000256|ARBA:ARBA00034032,
CC ECO:0000256|RuleBase:RU367007};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a dolichyl beta-D-mannosyl phosphate + L-threonyl-[protein] =
CC 3-O-(alpha-D-mannosyl)-L-threonyl-[protein] + a dolichyl phosphate +
CC H(+); Xref=Rhea:RHEA:53396, Rhea:RHEA-COMP:9517, Rhea:RHEA-COMP:9527,
CC Rhea:RHEA-COMP:11060, Rhea:RHEA-COMP:13547, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:30013, ChEBI:CHEBI:57683, ChEBI:CHEBI:58211,
CC ChEBI:CHEBI:137323; EC=2.4.1.109;
CC Evidence={ECO:0000256|ARBA:ARBA00033990,
CC ECO:0000256|RuleBase:RU367007};
CC -!- PATHWAY: Protein modification; protein glycosylation.
CC {ECO:0000256|ARBA:ARBA00004922, ECO:0000256|RuleBase:RU367007}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000256|ARBA:ARBA00004477, ECO:0000256|RuleBase:RU367007}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004477,
CC ECO:0000256|RuleBase:RU367007}. Membrane
CC {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 39 family.
CC {ECO:0000256|ARBA:ARBA00007222, ECO:0000256|RuleBase:RU367007}.
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DR EMBL; LN732886; CEP16196.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0B7NC98; -.
DR STRING; 35722.A0A0B7NC98; -.
DR OrthoDB; 5489060at2759; -.
DR UniPathway; UPA00378; -.
DR Proteomes; UP000054107; Unassembled WGS sequence.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0004169; F:dolichyl-phosphate-mannose-protein mannosyltransferase activity; IEA:UniProtKB-UniRule.
DR Gene3D; 2.80.10.50; -; 1.
DR InterPro; IPR027005; GlyclTrfase_39-like.
DR InterPro; IPR003342; Glyco_trans_39/83.
DR InterPro; IPR036300; MIR_dom_sf.
DR InterPro; IPR016093; MIR_motif.
DR InterPro; IPR032421; PMT_4TMC.
DR PANTHER; PTHR10050; DOLICHYL-PHOSPHATE-MANNOSE--PROTEIN MANNOSYLTRANSFERASE; 1.
DR PANTHER; PTHR10050:SF50; DOLICHYL-PHOSPHATE-MANNOSE--PROTEIN MANNOSYLTRANSFERASE 1-RELATED; 1.
DR Pfam; PF02815; MIR; 1.
DR Pfam; PF02366; PMT; 1.
DR Pfam; PF16192; PMT_4TMC; 1.
DR SMART; SM00472; MIR; 3.
DR SUPFAM; SSF82109; MIR domain; 1.
DR PROSITE; PS50919; MIR; 3.
PE 3: Inferred from homology;
KW Endoplasmic reticulum {ECO:0000256|ARBA:ARBA00022824,
KW ECO:0000256|RuleBase:RU367007};
KW Glycosyltransferase {ECO:0000256|ARBA:ARBA00022676,
KW ECO:0000256|RuleBase:RU367007};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU367007};
KW Reference proteome {ECO:0000313|Proteomes:UP000054107};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU367007};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW ECO:0000256|RuleBase:RU367007};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|RuleBase:RU367007}.
FT TRANSMEM 93..114
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU367007"
FT TRANSMEM 134..155
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU367007"
FT TRANSMEM 184..203
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU367007"
FT TRANSMEM 215..248
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU367007"
FT TRANSMEM 269..290
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU367007"
FT TRANSMEM 587..608
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU367007"
FT TRANSMEM 628..649
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU367007"
FT TRANSMEM 661..679
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU367007"
FT TRANSMEM 686..703
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU367007"
FT DOMAIN 322..376
FT /note="MIR"
FT /evidence="ECO:0000259|PROSITE:PS50919"
FT DOMAIN 396..456
FT /note="MIR"
FT /evidence="ECO:0000259|PROSITE:PS50919"
FT DOMAIN 458..514
FT /note="MIR"
FT /evidence="ECO:0000259|PROSITE:PS50919"
FT REGION 1..27
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 784..876
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 784..809
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 825..839
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 876 AA; 98795 MW; 7A1394B4ED4D4F4B CRC64;
MSISTLEMRQ RKPPVASLVT APQDKQQRNN DLRKHLVKKT NNYNSSSKDC LLAAVLFIVS
LPVRLKNISN PDQVVFDEVH YGQYASYYIT QRFFFDIHPP LAKMLIAWIA WIAGYDGQFD
FNETGSYPSS VPYATIRAFG ALLGCLVVPL AFLTIRNAGH SRVAATITAL AICSENGLIT
NNRLILLDSY LLCFIAFSIY AYTRFYRQSA FGQSWWIWLF FTGVGLGCAV SSKWVGLFTL
ATVGLSASKH LWEILGDIQI TKRQYGIHLC ARLACLCVIP LAVYLAAFYA HFALLSKPGP
GDSFMEIETQ NELRGLAPVD TPVPVAYGSL ITMRHRATTG GYLHSHAANY AEGSGQQQVT
LYPYKDENNW WRILKAQEDD VVDKLDLLGS DNATSLEYVR HGDLVRLEHV ATAPRKLHSH
NVPAPVTDTD YHFEVSGYGF ENYTGDSNDF WHVQIDTGKY LEARRSLFRL EHINQDCHLY
STVERLPDWG FGQQEVSCIQ EGLKAKTMWM IDETEHPLLP LGVAIEHERR PGFLAKLAHL
HRAMWSVISA DLLTDAQQQQ QQHGVSYYWQ ASSGTAPAQI ISLRNPIVFW TSTTAVAAFG
LLFGLLQLCD KRGFLSKDYY CHFQGKRAYY EASAGFFALG WALHCIPLYY TTADHRQQHD
YIPALYFAVL TLGVGIDLVL SRFHRALRMT LAVAVSVCII YAYRTYTPII YGEPWSVAAC
QQATLLDFWD LNCALYDTEA SLPHHHYQMV RLDKANDFHD SSSGSIASEN VSQEEFLVVN
EVDDEYGDEE YNHDDGGYGE EEEEGDSPTE PPMIAEPEPE FVDGKEVYGD DDDDDDEYPK
TIYGVDPEAD QNDDDDGQED DRFPLKPRDI PSTIHV
//
