ID A0A0B7N5H3_9FUNG Unreviewed; 894 AA.
AC A0A0B7N5H3;
DT 01-APR-2015, integrated into UniProtKB/TrEMBL.
DT 01-APR-2015, sequence version 1.
DT 22-FEB-2023, entry version 33.
DE RecName: Full=dolichyl-phosphate-mannose--protein mannosyltransferase {ECO:0000256|ARBA:ARBA00012839};
DE EC=2.4.1.109 {ECO:0000256|ARBA:ARBA00012839};
GN Name=PARPA_06623.1 scaffold 22734 {ECO:0000313|EMBL:CEP12652.1};
OS Parasitella parasitica.
OC Eukaryota; Fungi; Fungi incertae sedis; Mucoromycota; Mucoromycotina;
OC Mucoromycetes; Mucorales; Mucorineae; Mucoraceae; Parasitella.
OX NCBI_TaxID=35722 {ECO:0000313|EMBL:CEP12652.1, ECO:0000313|Proteomes:UP000054107};
RN [1] {ECO:0000313|EMBL:CEP12652.1, ECO:0000313|Proteomes:UP000054107}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 412.66 {ECO:0000313|EMBL:CEP12652.1,
RC ECO:0000313|Proteomes:UP000054107};
RA Ellenberger Sabrina;
RL Submitted (SEP-2014) to the EMBL/GenBank/DDBJ databases.
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 -!- 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 -!- 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 glycosyltransferase 39 family.
CC {ECO:0000256|ARBA:ARBA00007222}.
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DR EMBL; LN728061; CEP12652.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0B7N5H3; -.
DR STRING; 35722.A0A0B7N5H3; -.
DR OrthoDB; 1357182at2759; -.
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-EC.
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 PANTHER; PTHR10050; DOLICHYL-PHOSPHATE-MANNOSE--PROTEIN MANNOSYLTRANSFERASE; 1.
DR PANTHER; PTHR10050:SF51; PROTEIN O-MANNOSYL-TRANSFERASE 1; 1.
DR Pfam; PF02815; MIR; 1.
DR Pfam; PF02366; PMT; 1.
DR SMART; SM00472; MIR; 3.
DR SUPFAM; SSF82109; MIR domain; 1.
DR PROSITE; PS50919; MIR; 2.
PE 3: Inferred from homology;
KW Endoplasmic reticulum {ECO:0000256|ARBA:ARBA00022824};
KW Glycosyltransferase {ECO:0000256|ARBA:ARBA00022676};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000054107};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
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 93..111
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 131..150
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 180..199
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 238..256
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 268..287
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 603..620
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 653..673
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 679..697
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 322..376
FT /note="MIR"
FT /evidence="ECO:0000259|PROSITE:PS50919"
FT DOMAIN 386..444
FT /note="MIR"
FT /evidence="ECO:0000259|PROSITE:PS50919"
FT REGION 857..894
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 894 AA; 101386 MW; 741D3EC226A33688 CRC64;
MFSVRSRKIA EKTNDPFVVN DNDEKYEKKG VAYKETSWTA TIQDQLRLTV LSFLGLYLRI
MKLGFPAYIT DIELETTKQV NWYMAGKFFI GKFPPLTGLV STGLARLAGY YGSEELGYPG
QPFVEFPVVA LRRFSAILGA SLVPLAYMTM RNMGHSRAAA TLASALIIFE NGIVTQSRYA
TPEIFVLFFS ALATCSWTLM NKYTQESYGK LTTQAGFWQI ISGISIGCAV SSKWTGMMVI
PVIWVSILHG AWIKLCEKHN KIRMIVKNMF VSMLSTMLLP LCVYLAIFQF HFNLIPNAGD
HDLLVSSRLK YSLQGNSLEP SQPNIAYGSQ IVIRHENTVG GYLHSHRKRF TGGSTQQEVT
LYPHVDINNI WTVHKNNQIW NSSQPIEFVR NLDQIRLEHF ASTRKLHSHD HRPQMTNKKE
HNEVTAYGDR LIQDSHDYWT LRIIGDDNLA EKNKNVTWKA LNQRFRLTHV RGCALISHNA
YFAPPNGENH QEVTCMAGAA SHVSSWIVES SYHEQLEGMQ TISYGDISTK QKFQEVHKLM
AKYPSVVYDR LQTGSHSDGA ANPKFYREEN ANKWFFQRAS FRIWSELAGY SAHLVLNPIV
QRLILSTMIA YFGFLGLNAF QLQRQIKLPS YLGWLHIIGM DTLINDFYTR SIVFLYSACV
IHVMCLRFLP HHITTMPDIL GSIYYGIGLS VAFLEACTSR LSSTFRRTVL YGLLLISIVK
FSQLSHLSYG GEKWYRADCI KSDFDIDCIR FPPHEAELAE IVQNSGRTQN STLLTIYVEM
AGNTQQPFRY NQGQEAEADN HVAILKQQAY LKESQTATGT LRYHRVVPTV AMTPEDAAKW
AKEVYDGAVN RKKTAEEAAL KTEKGKKGSN APRKKTKAKK SNVNGGPIMN LEKK
//
