CAZyme Information: QSL65107.1

Basic Information

• Species: Pneumocystis wakefieldiae
• Lineage: Ascomycota; Pneumocystidomycetes; ; Pneumocystidaceae; Pneumocystis; Pneumocystis wakefieldiae
• CAZyme ID: QSL65107.1
• CAZy Family: GT20
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
1403		160947.94	8.7887

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_Pwakefieldiae2A	3223	N/A	41	3182

• Gene Location: location=CP054536:115585-120390(-)

Full Sequence      

MKIAFIHPDLGIGGAERFTVDAAAGLQALGHEVVLFTSHCDKGHCFDEIKRGLLPVEVYG
DWIPARIFGKCSVLCAIFRQLFLSLVLIFKMESYDAIVMDVLSFGLPLLRWKSRRILFYC
HFPDKLLARRNGMLRRVYRLPFDVAENLSLLMSDRILVNSYFTASVVHKTFINIRDLTVL
YPGIDTCDDGPENAPLVTQSHVYFILSMNRFERKKNIDLAVKSYSHLRKDARFDQCCLII
AGGYESRIRENVQYHKELVDLCSDFSLRSKTFMAPYQFPLDFSGYNVVFLLSIPTDLKNY
LLRNATILLYTPPYEHFGIVPLEAMFRQTIVLAQDNGGPLETIDDGVTGWLKKSDDTEWA
KVLRNVLFQMSDAERATMGKRSKEKVNLNLSKMEESCIYKIQKDVQGEDPLALNSSDRQE
SLENLKLDIFEKIQDKSLKRSPFQGSKGLPNIGFEKGGIKSIDELYSGLASNHTFDVSSF
DQEFGLVPENIYLEDNYFIEKLIDRYGAVNFIRLLLRDLALKDLQIIENQKQSKNSEIVL
KKMLLNAGISYLDIEKRLYESFEKTRGFLFMNNGDHMVSDTYYMKSCNERLESLLLNDDA
SKRKKTRLPVYNKVSSYLFKTMGTGKLRKNIDMYDQRKSEHIFQDGHDKDAFNIIKRSNN
YPSLTHKFYFKGLPNSEKVHINSKAQSYSSSFNKIITRMALFDSFGSFESFLKMPGFGSY
FKEKTRFPRYPHTTHFKSISMAACCVLLYQNSSRSFLCKKKMSSMVVEFAWRLVFPLVLD
YHQHLIQDYISKSKLKITGLNLSTLLSKCFKELNIDHTDSKTFSVDSLYEKIIKLKSKTG
YFSKGFSNKLTFDTSSHGQNISQSDQSDTHSSSVIRETATPTFTTASRSCLFSDSVPRPL
EMDTIVPPERQPPTLLPSWNEYYRLDEKPLADRFGFIYNFSSKIKNLNSKSAQPIEANNK
SNCNHSESLDYLEHIDFSKNKRNDEFKSSDISLKNDSLITSTSSLHKIMNMENTPLNNNA
ISSATSTTLNNDNSIAQGFITLDLDKKSKSFEAKFLLRSQLDIYGDSKTKQELWDSFLRK
VQNEKRRNINPNFHGYEGSELIGISELGIAGKVGKQRLKEFRNLVIGGIPIIYRPKIWGE
CSGAYQLHQPGYYNDLLTLGKDIDPIVVVQIDMDVYRTMPNNVFFGGKGPGVLKLKNVLL
AFSRHNTQIGYCQGMNVIAAMLLLTHATEEDAFYVLVSIVENILPPYYFTPDLLASRADQ
RVLTRYVSELCPRIHNHFKKLSVDLEAVTFNWFLTVFTDCLSPEVLFRVFDLLFIEGNVY
LFRVSIAIIKNIEKQILACTSPASVYSLLKNLSLEHFNIDSFIRETYENKKQIRTKDVMR
LRDIEIRKLKLEIENSKLQEAVN

Enzyme Prediction     

EC	2.4.1.257:6	2.4.1.132:6

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GT4	203	367	9.3e-31	0.86875

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
340834	GT4_ALG2-like	7.78e-163	1	386	1	379	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	3.25e-57	1127	1337	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	3.51e-50	1170	1337	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	1.88e-44	919	1381	27	465	GTPase-activating protein [General function prediction only].
340831	GT4_PimA-like	3.42e-33	2	391	1	353	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	1403	1	1403
NP_595621.3|GT4	7.77e-108	1	391	17	411
BAA21387.2|GT4	7.77e-108	1	391	17	411
CAC37504.3|GT4	7.77e-108	1	391	17	411
EGX43020.1|GT4	2.21e-105	3	392	7	410

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
4P17_A	2.88e-26	1120	1369	59	309	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	5.21e-24	1118	1351	39	277	X-ray Crystal Structure of Human TBC1D4 (AS160) RabGAP domain [Homo sapiens]
4NC6_A	2.02e-21	1117	1337	20	237	Tbc domain of human rab gtpase-activating protein 1 [Homo sapiens]
3HZJ_A	2.07e-20	1096	1337	6	239	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]
3QYE_A	3.17e-19	1118	1351	49	287	Crystal Structure of Human TBC1D1 RabGAP domain [Homo sapiens],3QYE_B Crystal Structure of Human TBC1D1 RabGAP domain [Homo sapiens]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|Q96WW6|ALG2_SCHPO	1.38e-108	1	391	17	411	Alpha-1,3/1,6-mannosyltransferase alg2 OS=Schizosaccharomyces pombe (strain 972 / ATCC 24843) OX=284812 GN=alg2 PE=3 SV=2
sp|Q59LF2|ALG2_CANAL	2.05e-97	2	386	9	425	Alpha-1,3/1,6-mannosyltransferase ALG2 OS=Candida albicans (strain SC5314 / ATCC MYA-2876) OX=237561 GN=ALG2 PE=3 SV=2
sp|Q09830|YAD4_SCHPO	3.83e-97	1056	1393	436	770	TBC domain-containing protein C4G8.04 OS=Schizosaccharomyces pombe (strain 972 / ATCC 24843) OX=284812 GN=SPAC4G8.04 PE=1 SV=1
sp|Q6CWQ0|ALG2_KLULA	1.25e-96	2	363	10	393	Alpha-1,3/1,6-mannosyltransferase ALG2 OS=Kluyveromyces lactis (strain ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 / WM37) OX=284590 GN=ALG2 PE=3 SV=1
sp|Q6BVA4|ALG2_DEBHA	1.35e-95	2	387	11	422	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

SignalP and Lipop Annotations

This protein is predicted as OTHER

Other	SP_Sec_SPI	CS Position
1.000091	0.000000

TMHMM  Annotations     

There is no transmembrane helices in QSL65107.1.