CAZyme Information: KAG5438551.1

Basic Information

• Species: Pneumocystis canis
• Lineage: Ascomycota; Pneumocystidomycetes; ; Pneumocystidaceae; Pneumocystis; Pneumocystis canis
• CAZyme ID: KAG5438551.1
• CAZy Family: GT22
• CAZyme Description: unspecified product

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
1390	JACEFK010000007|CGC1	160530.38	8.8690

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_PcanisCanA	3113	N/A	38	3075

• Gene Location: location=JACEFK010000007:206053-210944(+)

Full Sequence      

MKIALVHPDLGIGGAERFIVDVAIGLQKQGHEIVIYTSYCDKKHCFEEVKKGLVDVRIYG
DKIPSKIFGKFSILCSIFRQFYLSISVLFEKRVYDVIIVDILSFSIPLLRWKCLKLLFYC
HFPDKLLANHNTLLRKIYRLPFDWIEGLTLSMADKILVNSYFTASIVEKTFPHIKNLTVL
YPSIDIYEENFLDDSVLICNNYRHLFVSINRFERKKDISLAIKSYYHLKNEDCFNQCYLI
IAGGYESRIQENVQYHNELVDLCDHLMLKSKTFQYPYEFPLDFSGYNIVFLLSIPAKLKN
YLLKKASVLLYTPPYEHFGIVPLEAMLHRTIVLAQNNGGPLETIDDGVTGWLRESNDMEW
ARILRKILFEFTDTKRIAMGEKGRQKVIRYFSRESMIQTLQCHIEKTNREIILKSNKLNN
KKEDQGNSVSKPLFSRSRTSLSFLGGKNEFKMINRVNSREFSPNHVFHHSPLFDERYDEV
FGDIYQEDDSFIQKMIDRYGTINFIRQLVRGLALRNTQVIENQKLSKDREIILKKMLLNV
GVSHLDIEKYLHESYGKSQESSSINNSNHVVSGLSYFESLDEKFMQTIRDDNMHKCMKIN
LDSDGKVSNSVKTTEHLSLQKNMNLNNQKKIIYVSQNHLNGKKLKTINGKNIDNLSPSIC
HEFHPKKDFVSNFKTFHIHSKLQSYSRSLNKIIPRMTSFDSSFEAFSKISGFGSYFKENV
SNLRYFHTLHFKAIALSACCVLLFKNFDKEFICQKGKSSMIIDFAWRLILPLVLDYHQFL
IQDYVSKSKSKVSNLNLDTILSKYFKELSDDNFDSKIFSVNCLYEKIIKLKLKKNHLYKN
FLLNDSILSNAYSQNQHISQPDQTDTNFPSVIKEMSASVLASKFWSFLSSYSAPRPLEMD
TIVPPECQPPTLLPSWNEYYRVDEKPLVDRFGFIYTFGSKKKSFDSKLIQSTKINNNCRS
QFEDIDYSSDVDFVKDKPDEEIELMSVSYLKKDSCVTSTNSSQKFIDVENKLLGHNGIPL
TTLTSLSSDSSIAQGFITVNLNKKSKGFATKFLLRSHLDTSKDDKAKQELWDIFLQKIQN
EKKSSIDPDIYGYEDSDLIGIPGLGIAGKVGKQRWKKFRNLVIGGIPMIWKECSGAYQLQ
QPGYYTDLLTMGKDIDPMVVAQIDMDIYRTMPNNVFFGKKGPGVFKLKNVLLAFSRHNIQ
IGYCQGMNVIAATLLLTHATEEDAFYVLVSIVENILPPHYFTPDLLASRADQRVLIRYVA
ELCPRVYAHLKKLSVDLEAVTFNWFLSVFTDCLPAEVLFRVFDLLFIEGNVYLFRVSIAI
IKSREKQILECTSPSSVYSLLKNLSIESFNIDSFIQATCENKKQIRIKDAMHFREIEIRK
LKAEMGNTVL

Enzyme Prediction     

EC	2.4.1.257:6	2.4.1.132:6

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GT4	203	368	7.3e-29	0.875

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
340834	GT4_ALG2-like	8.32e-170	1	396	1	388	alpha-1,3/1,6-mannosyltransferase ALG2 and similar proteins. This family is most closely related to the GT4 family of glycosyltransferases. ALG2, a 1,3-mannosyltransferase, in yeast catalyzes the mannosylation of Man(2)GlcNAc(2)-dolichol diphosphate and Man(1)GlcNAc(2)-dolichol diphosphate to form Man(3)GlcNAc(2)-dolichol diphosphate. A deficiency of this enzyme causes an abnormal accumulation of Man1GlcNAc2-PP-dolichol and Man2GlcNAc2-PP-dolichol, which is associated with a type of congenital disorders of glycosylation (CDG), designated CDG-Ii, in humans.
214540	TBC	4.93e-52	1124	1329	3	216	Domain in Tre-2, BUB2p, and Cdc16p. Probable Rab-GAPs. Widespread domain present in Gyp6 and Gyp7, thereby giving rise to the notion that it performs a GTP-activator activity on Rab-like GTPases.
366170	RabGAP-TBC	6.20e-48	1162	1329	14	180	Rab-GTPase-TBC domain. Identification of a TBC domain in GYP6_YEAST and GYP7_YEAST, which are GTPase activator proteins of yeast Ypt6 and Ypt7, implies that these domains are GTPase activator proteins of Rab-like small GTPases.
227535	COG5210	1.33e-38	1114	1344	201	442	GTPase-activating protein [General function prediction only].
340831	GT4_PimA-like	1.00e-36	2	400	1	361	phosphatidyl-myo-inositol mannosyltransferase. This family is most closely related to the GT4 family of glycosyltransferases and named after PimA in Propionibacterium freudenreichii, which is involved in the biosynthesis of phosphatidyl-myo-inositol mannosides (PIM) which are early precursors in the biosynthesis of lipomannans (LM) and lipoarabinomannans (LAM), and catalyzes the addition of a mannosyl residue from GDP-D-mannose (GDP-Man) to the position 2 of the carrier lipid phosphatidyl-myo-inositol (PI) to generate a phosphatidyl-myo-inositol bearing an alpha-1,2-linked mannose residue (PIM1). Glycosyltransferases catalyze the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds. The acceptor molecule can be a lipid, a protein, a heterocyclic compound, or another carbohydrate residue. This group of glycosyltransferases is most closely related to the previously defined glycosyltransferase family 1 (GT1). The members of this family may transfer UDP, ADP, GDP, or CMP linked sugars. The diverse enzymatic activities among members of this family reflect a wide range of biological functions. The protein structure available for this family has the GTB topology, one of the two protein topologies observed for nucleotide-sugar-dependent glycosyltransferases. GTB proteins have distinct N- and C- terminal domains each containing a typical Rossmann fold. The two domains have high structural homology despite minimal sequence homology. The large cleft that separates the two domains includes the catalytic center and permits a high degree of flexibility. The members of this family are found mainly in certain bacteria and archaea.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QSL65107.1|GT4	0.0	1	1390	1	1398
EGX43020.1|GT4	4.52e-111	3	412	7	432
BAO40563.1|GT4	7.43e-108	2	407	14	439
QGN16293.1|GT4	7.43e-108	2	407	14	439
BAP72044.1|GT4	7.43e-108	2	407	14	439

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
4P17_A	5.84e-25	1117	1343	59	291	Crystal structure of the Chlamydomonas flagellar RabGAP TBC domain. [Chlamydomonas reinhardtii],4P17_B Crystal structure of the Chlamydomonas flagellar RabGAP TBC domain. [Chlamydomonas reinhardtii]
3QYB_A	9.42e-24	1153	1343	84	277	X-ray Crystal Structure of Human TBC1D4 (AS160) RabGAP domain [Homo sapiens]
3QYE_A	1.60e-20	1116	1343	50	287	Crystal Structure of Human TBC1D1 RabGAP domain [Homo sapiens],3QYE_B Crystal Structure of Human TBC1D1 RabGAP domain [Homo sapiens]
4NC6_A	3.23e-19	1114	1329	20	237	Tbc domain of human rab gtpase-activating protein 1 [Homo sapiens]
3HZJ_A	1.00e-18	1114	1330	22	240	Crystal structure of the RabGAP domain of the RABGAP1L protein [Homo sapiens],3HZJ_B Crystal structure of the RabGAP domain of the RABGAP1L protein [Homo sapiens],3HZJ_C Crystal structure of the RabGAP domain of the RABGAP1L protein [Homo sapiens]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|Q96WW6|ALG2_SCHPO	8.41e-108	1	404	17	423	Alpha-1,3/1,6-mannosyltransferase alg2 OS=Schizosaccharomyces pombe (strain 972 / ATCC 24843) OX=284812 GN=alg2 PE=3 SV=2
sp|Q6BVA4|ALG2_DEBHA	1.30e-101	2	408	11	442	Alpha-1,3/1,6-mannosyltransferase ALG2 OS=Debaryomyces hansenii (strain ATCC 36239 / CBS 767 / BCRC 21394 / JCM 1990 / NBRC 0083 / IGC 2968) OX=284592 GN=ALG2 PE=3 SV=2
sp|P43636|ALG2_YEAST	2.12e-101	3	406	9	432	Alpha-1,3/1,6-mannosyltransferase ALG2 OS=Saccharomyces cerevisiae (strain ATCC 204508 / S288c) OX=559292 GN=ALG2 PE=1 SV=2
sp|Q09830|YAD4_SCHPO	1.73e-100	870	1360	320	744	TBC domain-containing protein C4G8.04 OS=Schizosaccharomyces pombe (strain 972 / ATCC 24843) OX=284812 GN=SPAC4G8.04 PE=1 SV=1
sp|Q59LF2|ALG2_CANAL	3.75e-98	2	400	9	438	Alpha-1,3/1,6-mannosyltransferase ALG2 OS=Candida albicans (strain SC5314 / ATCC MYA-2876) OX=237561 GN=ALG2 PE=3 SV=2

SignalP and Lipop Annotations

This protein is predicted as OTHER

Other	SP_Sec_SPI	CS Position
1.000041	0.000000

TMHMM  Annotations     

There is no transmembrane helices in KAG5438551.1.