CAZyme Information: KAG5421636.1

Basic Information

• Species: Candida metapsilosis
• Lineage: Ascomycota; Saccharomycetes; ; Debaryomycetaceae; Candida; Candida metapsilosis
• CAZyme ID: KAG5421636.1
• CAZy Family: GT57
• CAZyme Description: PMT4

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
1206	JAEOAQ010000001|CGC1	135699.06	9.2795

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_CmetapsilosisBP57	5743	N/A	17	5726

• Gene Location: location=JAEOAQ010000001:1645330-1649436(-)

Full Sequence      

MRDIMVLGGSSHPLLTKAICRNLTIEPGKLDSHKFANGETSIIVKDSVREKDVFIVQSGC
GPVNDTFIELLITIAACKTASSKRVTAVLPLFPYSRQPDVPFMPNSTGAPSISTTKDSCT
FESAPTTPRPLSKDRKGYFNEANAAGTKENPRVDTLKQQQYPKYTPKSVITNSAATHFLP
QIDSQGKTDSGYKQWISPNGTLIANLLTTAGADRVITMDLHDPQFQGFFNIPVDNLHSRP
LMKRYIIDYIPNYRECVIVSPDSGGAKRATAIADSIGCTFALIHKERRAKLPKGPPQTSS
SMGSGLAISQPVQNAVPQSPYHQGTPKMVATTMLVGDVKDKVCVLIDDLVDTSYTITRAA
KLLKDEGAKYVYALVTHGIFSGDAINRISKSQIDKVVTTNSVPQSENVAILKEKIEVLDV
SRIFAEAIRRINNGESVSKMSQAVKKRTTAGRKTQPVSDTIIDVPVRDQNSNSKRNKNSL
KEVDAYASAEVEPDYKYWIALSFITAVAFYVRFTKLGTPDKVVFDEVHFGKFASYYLERT
YFFDLHPPFAKLLIAFVGWLIGYNGKFKFDAIGDSYTENNVPYIAYRSLSALQGTAVVPV
MFLTMKTLGFSVAACLFSSIIVCFDTAQVLDSRLILLDATLILSVALTMFCYCKFSTFRR
DPFGKKWWTWLLATGVSLSCVISTKYVGVFTYFTIGIAVCHELWILLDYQRGLTLQQFSK
HFFARLWALIIIPFVIYLTWFYIHFAILTKSGPGDTFMSSEFQETLQESPLAKLSKQVQY
YDQITIKHKETGAFLHSHDHVYPLRYEDGRISSNKQQVTCVDGDNASSDPNNQWEIIPVQ
AENDGAKGKDVYTNDVVRFKHVGTGGFLLTHDVASPLKATNEEFIVVFDDVAEKRYNETL
FRLKLDVPGSSPKKQNQRKKIKTMATSLKVLHMDTVVAMWTHDDELLPEWGFNQQEVSGN
KNIKSKENVWTFDVITNLDESDPRSKYVPKKIKSIPFLKKWWELQGLMFHHNNQLSASHP
FASQPDSWPLALSGVSFFNDNEAKKQIFFVGNVIGFWLEVCFLSIYVGLVLADQITRRRN
YHLLSDKARSRLYNTLGFLFIGWCAHYFPFYLMNRQKFLHHYLPAHLIAALFSGGLVEFV
CSNNSTSANTSQGRKKIKMTFLVVLASIGIIWFFFYFRPIIYGDVSLTPAEVQARQWLDI
KLHYAK

Enzyme Prediction     

EC	2.4.1.109:8

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GT39	504	745	2.1e-68	0.9910313901345291

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
224839	PMT1	0.0	496	1199	22	691	Dolichyl-phosphate-mannose--protein O-mannosyl transferase [Posttranslational modification, protein turnover, chaperones].
223538	PrsA	4.34e-120	1	440	2	312	Phosphoribosylpyrophosphate synthetase [Nucleotide transport and metabolism, Amino acid transport and metabolism].
234929	PRK01259	9.98e-109	4	440	1	307	ribose-phosphate diphosphokinase.
273523	ribP_PPkin	1.73e-95	4	440	1	306	ribose-phosphate pyrophosphokinase. Alternate name: phosphoribosylpyrophosphate synthetase In some systems, close homologs lacking enzymatic activity exist and perform regulatory functions. The model is designated subfamily rather than equivalog for this reason. [Purines, pyrimidines, nucleosides, and nucleotides, Purine ribonucleotide biosynthesis]
396786	PMT	7.18e-83	502	749	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.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
CCG22319.1|GT39	0.0	440	1206	1	768
CCE40454.1|GT39	0.0	440	1206	1	767
CAX43831.1|GT39	0.0	440	1206	1	755
AOW27618.1|GT39	0.0	440	1206	1	755
CAG88909.2|GT39	0.0	440	1206	1	754

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
6P25_A	2.78e-87	501	1198	56	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	2.19e-81	505	1183	72	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]
4LYG_A	7.22e-78	1	438	1	310	Crystal structure of human PRS1 E43T mutant [Homo sapiens],4LYG_B Crystal structure of human PRS1 E43T mutant [Homo sapiens]
2H06_A	1.36e-77	1	438	1	310	Crystal structure of human phosphoribosyl pyrophosphate synthetase 1 [Homo sapiens],2H06_B Crystal structure of human phosphoribosyl pyrophosphate synthetase 1 [Homo sapiens],2HCR_A crystal structure of human phosphoribosyl pyrophosphate synthetase 1 in complex with AMP(ATP), cadmium and sulfate ion [Homo sapiens],2HCR_B crystal structure of human phosphoribosyl pyrophosphate synthetase 1 in complex with AMP(ATP), cadmium and sulfate ion [Homo sapiens],3EFH_A Crystal structure of human phosphoribosyl pyrophosphate synthetase 1 [Homo sapiens],3EFH_B Crystal structure of human phosphoribosyl pyrophosphate synthetase 1 [Homo sapiens],3S5J_A 2.0A Crystal structure of human phosphoribosyl pyrophosphate synthetase 1 [Homo sapiens],3S5J_B 2.0A Crystal structure of human phosphoribosyl pyrophosphate synthetase 1 [Homo sapiens]
2H07_A	1.36e-77	1	438	1	310	Chain A, Ribose-phosphate pyrophosphokinase I [Homo sapiens],2H07_B Chain B, Ribose-phosphate pyrophosphokinase I [Homo sapiens]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|Q59X23|PMT4_CANAL	0.0	440	1206	1	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	1.67e-261	490	1206	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	9.65e-191	438	1199	3	768	Dolichyl-phosphate-mannose--protein mannosyltransferase 4 OS=Schizosaccharomyces pombe (strain 972 / ATCC 24843) OX=284812 GN=ogm4 PE=3 SV=1
sp|Q12265|KPR5_YEAST	2.00e-135	1	438	3	489	Ribose-phosphate pyrophosphokinase 5 OS=Saccharomyces cerevisiae (strain ATCC 204508 / S288c) OX=559292 GN=PRS5 PE=1 SV=1
sp|P87171|KPR5_SCHPO	8.51e-102	1	438	1	331	Ribose-phosphate pyrophosphokinase 5 OS=Schizosaccharomyces pombe (strain 972 / ATCC 24843) OX=284812 GN=SPBC3D6.06c PE=3 SV=1

SignalP and Lipop Annotations

This protein is predicted as OTHER

Other	SP_Sec_SPI	CS Position
1.000053	0.000000

TMHMM  Annotations     

Start	End
726	748
1048	1070
1091	1113
1118	1140
1160	1182
497	514
541	563
600	622
634	652
667	689