CAZyme Information: EDK43685.1

Basic Information

• Species: Lodderomyces elongisporus
• Lineage: Ascomycota; Saccharomycetes; ; Debaryomycetaceae; Lodderomyces; Lodderomyces elongisporus
• CAZyme ID: EDK43685.1
• CAZy Family: GH3
• CAZyme Description: dolichyl-phosphate-mannose-protein mannosyltransferase 4

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
779		89711.09	9.3527

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_LelongisporusNRRLYB-4239	5908	379508	109	5799

• Gene Location: location=CH981525:1385062-1387401(+)

Full Sequence      

MSQAVRKRNTATKKQSNSDSTVFGGDDKNSNYKNNNINNSNNKVNDEFDDNNGKLKSGVG
LDKDPEQKYWLALVFVTILAIYTRFTKLGTPNKVVFDEVHFGKFASYYLERTYFFDLHPP
FAKLLIAFVGWLVGYNGKFKFDAIGDSYIENNVPYIAYRSLLAIQGTAIIPVMFLTMKTL
GFNVAACLLSSIIVCFDNAQVADSRLILLDATLILSVAATIFCYSKFSIYRKQPFTQKWW
KWLISTGVSLSCVISTKYVGVFTFFTIGIAVLHELWFLLDYRKGLTLQQFGKHFFARLWA
LIILPFTIYLFWFYLHFAILTKSGPGDAFMSAEFQETLLESPLAQHSKDVQYYDEITIKH
KDTGAFLHSHLHDYPLRYEDGRISSNLQQVTCVIEDDAKNDENNVWQIVPVIAEDDGKKG
KSVFTNDVVRFKHKGTGGFLLTHDVASPLKATNEEFTVVYNETASNRYNETLFRLRLNVP
GSNPKKQNQRKKVSTMATELRILHMDTVVAMWTHDDELLPEWAFQQQEVSGNKKIQDKDN
IWTFDSITNLAEHDSRSKYIPKKIKKIPFLKKWWELQGLMFHHNNQLSSSHPFASQPDAW
PLALSGVSFYNNNEEKKQIFFHGNVIGFWLEVCFLSVYVGILLADQITLRRNYHLLNDKA
RSRLYNTLGFLFIGWAAHYLPFFLMNRQKFLHHYLPAHLIAALFTGGLVEFICTNNSNDF
NRSSPQSKKIKMTVLVSLASIGIIWFFFYFRPITYGDVSLTPAEVQKRQWLDIKLHYAK

Enzyme Prediction     

EC	2.4.1.109:8

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GT39	76	317	3.5e-67	0.9910313901345291

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
224839	PMT1	0.0	68	772	22	691	Dolichyl-phosphate-mannose--protein O-mannosyl transferase [Posttranslational modification, protein turnover, chaperones].
396786	PMT	3.67e-80	74	321	1	245	Dolichyl-phosphate-mannose-protein mannosyltransferase. This is a family of Dolichyl-phosphate-mannose-protein mannosyltransferase proteins EC:2.4.1.109. These proteins are responsible for O-linked glycosylation of proteins, they catalyze the reaction:- Dolichyl phosphate D-mannose + protein <=> dolichyl phosphate + O-D-mannosyl-protein. Also in this family is Drosophila rotated abdomen protein which is a putative mannosyltransferase. This family appears to be distantly related to pfam02516 (A Bateman pers. obs.). This family also contains sequences from ArnTs (4-amino-4-deoxy-L-arabinose lipid A transferase). They catalyze the addition of 4-amino-4-deoxy-l-arabinose (l-Ara4N) to the lipid A moiety of the lipopolysaccharide. This is a critical modification enabling bacteria (e.g. Escherichia coli and Salmonella typhimurium) to resist killing by antimicrobial peptides such as polymyxins. Members such as undecaprenyl phosphate-alpha-4-amino-4-deoxy-L-arabinose arabinosyl transferase are predicted to have 12 trans-membrane regions. The N-terminal portion of these proteins is hypothesized to have a conserved glycosylation activity which is shared between distantly related oligosaccharyltransferases ArnT and PglB families.
406576	PMT_4TMC	1.03e-72	571	772	1	198	C-terminal four TMM region of protein-O-mannosyltransferase. PMT_4TMC is the C-terminal four membrane-pass region of protein-O-mannosyltransferases and similar enzymes.
397103	MIR	2.22e-13	359	542	4	183	MIR domain. The MIR (protein mannosyltransferase, IP3R and RyR) domain is a domain that may have a ligand transferase function.
197746	MIR	1.78e-09	349	411	3	57	Domain in ryanodine and inositol trisphosphate receptors and protein O-mannosyltransferases.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
CCE40454.1|GT39	0.0	62	779	50	767
CCG22319.1|GT39	0.0	1	779	1	768
CAX43831.1|GT39	0.0	47	779	24	755
AOW27618.1|GT39	0.0	45	779	22	755
CAG88909.2|GT39	0.0	49	779	23	754

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
6P25_A	3.98e-94	74	771	51	724	Structure of S. cerevisiae protein O-mannosyltransferase Pmt1-Pmt2 complex bound to the sugar donor and a peptide acceptor [Saccharomyces cerevisiae W303],6P2R_A Structure of S. cerevisiae protein O-mannosyltransferase Pmt1-Pmt2 complex bound to the sugar donor [Saccharomyces cerevisiae W303]
6P25_B	4.58e-91	74	756	69	734	Structure of S. cerevisiae protein O-mannosyltransferase Pmt1-Pmt2 complex bound to the sugar donor and a peptide acceptor [Saccharomyces cerevisiae W303],6P2R_B Structure of S. cerevisiae protein O-mannosyltransferase Pmt1-Pmt2 complex bound to the sugar donor [Saccharomyces cerevisiae W303]
6P28_A	1.72e-08	364	549	22	195	Crystal structure of the MIR domain (aa 337-532) of the S. cerevisiae mannosyltransferase Pmt2 [Saccharomyces cerevisiae]
6ZQP_A	2.26e-08	364	549	39	212	Structure of the Pmt2-MIR domain with bound ligands [Saccharomyces cerevisiae]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|Q59X23|PMT4_CANAL	0.0	45	779	22	755	Dolichyl-phosphate-mannose--protein mannosyltransferase 4 OS=Candida albicans (strain SC5314 / ATCC MYA-2876) OX=237561 GN=PMT4 PE=2 SV=2
sp|P46971|PMT4_YEAST	5.96e-268	64	779	47	762	Dolichyl-phosphate-mannose--protein mannosyltransferase 4 OS=Saccharomyces cerevisiae (strain ATCC 204508 / S288c) OX=559292 GN=PMT4 PE=1 SV=1
sp|O42933|PMT4_SCHPO	4.00e-200	67	772	56	768	Dolichyl-phosphate-mannose--protein mannosyltransferase 4 OS=Schizosaccharomyces pombe (strain 972 / ATCC 24843) OX=284812 GN=ogm4 PE=3 SV=1
sp|F1Q8R9|POMT2_DANRE	1.22e-100	73	756	71	732	Protein O-mannosyl-transferase 2 OS=Danio rerio OX=7955 GN=pomt2 PE=1 SV=1
sp|Q9UKY4|POMT2_HUMAN	1.79e-94	69	772	57	746	Protein O-mannosyl-transferase 2 OS=Homo sapiens OX=9606 GN=POMT2 PE=1 SV=2

SignalP and Lipop Annotations

This protein is predicted as OTHER

Other	SP_Sec_SPI	CS Position
1.000061	0.000002

TMHMM  Annotations     

Start	End
69	86
113	135
156	175
179	196
208	230
258	277
298	320
625	644
664	686
690	712
733	755