CAZyme Information: KAG5438295.1

Basic Information

• Species: Pneumocystis canis
• Lineage: Ascomycota; Pneumocystidomycetes; ; Pneumocystidaceae; Pneumocystis; Pneumocystis canis
• CAZyme ID: KAG5438295.1
• CAZy Family: GT2
• CAZyme Description: unspecified product

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
1081		120740.35	5.9506

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=JACEFK010000008:46206-50260(-)

Full Sequence      

MEFRCQALVLHALIYVTLFVYGRVETIQRRGNFLFYSNGERFFIKGIAYQPQPSLGSTKH
YTDPLGDPKICSRDLPYFLDLGINTLRVYTVDPELDHTYCMNLFAESGIYVLLDLSEPRV
SIISTNPSWDVILLYRYIKVIDSMINYPNLIGFFAGNEVVLDTQNTHAAAFVKAAIRDIK
AYIKHKKYRNVLVGYAANDHHHTRIPSANYFACGDSDSAADFFGINIYEWCEPTTYETSG
YKDRVNDFSNFGIPLFFSEYGCNIVNGNLGVRTFKQIQYIYSRYMTSVFSGGIVYEWFQG
ENSYGLVDLLNDGTISPRKDYLNLKMQLNLLKSSPPDNLGDRPTFSSPQCPSINEYWSAS
TSLPPVPNSELCSCASSASSCVAVSDITNKEMEDIFSYVCSKISCRAISKDGKAGVYGAY
SVCNPIDQLNVILGLYHSNFNDDSACNFKGTTYPTEPRVSKTCSSLLRMVGPDGTGTITG
PPYATEHTKGDASQKHKGGSEKELSMKWKLILGLEIAIRRKIENELSKKKPTAARMHPSR
KMDPKTVLSLSPSPPLTVQSGITVSEASQLMAAKREDCVLVVDDNQHLMGIFTAKDLAFR
VVGMDMDPRNLLIEDIMTKNPLCARNDTSATDALDLMVHKGFRHLPVCDEDGNVSGILDI
TKCFHEAMKKVERAYTSSRQLYDALEGVQTEWGQIEQSEQIIQYVETLKQKMSGPNLASA
LDGTTPITVNIRTSVRDAAFLMRENHTTAVLVMDQMNISGIFTSKDIVLRVIAPGLDPAN
CSVVRVMTPHPDCVPMDMSIQEALKKMDEGRYLNLPVLDQESQVIGMVDVMKLTYLILEQ
IKNIGSPDGEGLIWNRFWNNLEDGDSESILSDNQLSTSQNYQSLLYASLPNNQQDIQVLS
PDTSATKLPQKNEWTSPTERPTFSGKNSPLLSQIPFVFKFKSLYGKTHRIQLIPQAGYAS
LRLAIIERLRSELEKLGGSDDLAISFIDDEGDSVSMTTDDDMFHAVELAYKNAEDKVNLI
IHHPNSSIINQKSDDLSSITENHHNEKASQSKSPKLTGYFVSISIAFCITTIAIVYKYIR
K

Enzyme Prediction     

EC	2.4.1.-:30	2.4.1.-:33

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH72	23	329	6.7e-120	0.9807692307692307

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
397351	Glyco_hydro_72	2.56e-140	24	329	9	312	Glucanosyltransferase. This is a family of glycosylphosphatidylinositol-anchored beta(1-3)glucanosyltransferases. The active site residues in the Aspergillus fumigatus example are the two glutamate residues at 160 and 261.
341417	CBS_pair_MUG70_1	1.33e-69	552	669	1	118	Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains similar to MUG70 repeat1. Two tandem repeats of the cystathionine beta-synthase (CBS pair) domain, present in MUG70. The MUG70 protein, encoded by the Meiotically Up-regulated Gene 70, plays a role in meiosis and contains, beside the two CBS pairs, a PB1 domain. The CBS domain, named after human CBS, is a small domain originally identified in cystathionine beta-synthase and is subsequently found in a wide range of different proteins. CBS domains usually occur in tandem repeats. They associate to form a so-called Bateman domain or a CBS pair based on crystallographic studies in bacteria. The CBS pair was used as a basis for this cd hierarchy since the human CBS proteins can adopt the typical core structure and form an intramolecular CBS pair. The interface between the two CBS domains forms a cleft that is a potential ligand binding site. The CBS pair coexists with a variety of other functional domains and this has been used to help in its classification here. It has been proposed that the CBS domain may play a regulatory role, although its exact function is unknown. Mutations of conserved residues within this domain are associated with a variety of human hereditary diseases, including congenital myotonia, idiopathic generalized epilepsy, hypercalciuric nephrolithiasis, and classic Bartter syndrome (CLC chloride channel family members), Wolff-Parkinson-White syndrome (gamma 2 subunit of AMP-activated protein kinase), retinitis pigmentosa (IMP dehydrogenase-1), and homocystinuria (cystathionine beta-synthase).
341418	CBS_pair_MUG70_2	6.01e-63	723	839	1	118	Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains similar to MUG70 repeat2. Two tandem repeats of the cystathionine beta-synthase (CBS pair) domain, present in MUG70. The MUG70 protein, encoded by the Meiotically Up-regulated Gene 70, plays a role in meiosis and contains, beside the two CBS pairs, a PB1 domain. The CBS domain, named after human CBS, is a small domain originally identified in cystathionine beta-synthase and is subsequently found in a wide range of different proteins. CBS domains usually occur in tandem repeats. They associate to form a so-called Bateman domain or a CBS pair based on crystallographic studies in bacteria. The CBS pair was used as a basis for this cd hierarchy since the human CBS proteins can adopt the typical core structure and form an intramolecular CBS pair. The interface between the two CBS domains forms a cleft that is a potential ligand binding site. The CBS pair coexists with a variety of other functional domains and this has been used to help in its classification here. It has been proposed that the CBS domain may play a regulatory role, although its exact function is unknown. Mutations of conserved residues within this domain are associated with a variety of human hereditary diseases, including congenital myotonia, idiopathic generalized epilepsy, hypercalciuric nephrolithiasis, and classic Bartter syndrome (CLC chloride channel family members), Wolff-Parkinson-White syndrome (gamma 2 subunit of AMP-activated protein kinase), retinitis pigmentosa (IMP dehydrogenase-1), and homocystinuria (cystathionine beta-synthase).
341417	CBS_pair_MUG70_1	1.23e-33	726	832	4	111	Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains similar to MUG70 repeat1. Two tandem repeats of the cystathionine beta-synthase (CBS pair) domain, present in MUG70. The MUG70 protein, encoded by the Meiotically Up-regulated Gene 70, plays a role in meiosis and contains, beside the two CBS pairs, a PB1 domain. The CBS domain, named after human CBS, is a small domain originally identified in cystathionine beta-synthase and is subsequently found in a wide range of different proteins. CBS domains usually occur in tandem repeats. They associate to form a so-called Bateman domain or a CBS pair based on crystallographic studies in bacteria. The CBS pair was used as a basis for this cd hierarchy since the human CBS proteins can adopt the typical core structure and form an intramolecular CBS pair. The interface between the two CBS domains forms a cleft that is a potential ligand binding site. The CBS pair coexists with a variety of other functional domains and this has been used to help in its classification here. It has been proposed that the CBS domain may play a regulatory role, although its exact function is unknown. Mutations of conserved residues within this domain are associated with a variety of human hereditary diseases, including congenital myotonia, idiopathic generalized epilepsy, hypercalciuric nephrolithiasis, and classic Bartter syndrome (CLC chloride channel family members), Wolff-Parkinson-White syndrome (gamma 2 subunit of AMP-activated protein kinase), retinitis pigmentosa (IMP dehydrogenase-1), and homocystinuria (cystathionine beta-synthase).
341358	CBS_pair_SF	5.67e-30	553	661	2	109	Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains superfamily. The CBS domain, named after human CBS, is a small domain originally identified in cystathionine beta-synthase and is subsequently found in a wide range of different proteins. CBS domains usually occur in tandem repeats. They associate to form a so-called Bateman domain or a CBS pair based on crystallographic studies in bacteria. The CBS pair was used as a basis for this cd hierarchy since the human CBS proteins can adopt the typical core structure and form an intramolecular CBS pair. The interface between the two CBS domains forms a cleft that is a potential ligand binding site. The CBS pair coexists with a variety of other functional domains and this has been used to help in its classification here. It has been proposed that the CBS domain may play a regulatory role, although its exact function is unknown. Mutations of conserved residues within this domain are associated with a variety of human hereditary diseases, including congenital myotonia, idiopathic generalized epilepsy, hypercalciuric nephrolithiasis, and classic Bartter syndrome (CLC chloride channel family members), Wolff-Parkinson-White syndrome (gamma 2 subunit of AMP-activated protein kinase), retinitis pigmentosa (IMP dehydrogenase-1), and homocystinuria (cystathionine beta-synthase).

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QSL64406.1|CBM43|GH72	8.91e-215	53	514	12	474
AAF05967.1|CBM43|GH72	1.53e-212	14	514	14	531
AWU75603.1|CBM43|GH72	7.76e-142	26	480	28	478
AWU49727.1|CBM43|GH72	5.41e-138	26	480	28	478
AOA61229.1|CBM43|GH72	4.58e-137	26	480	18	472

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
2W62_A	9.95e-106	21	508	30	522	Saccharomyces cerevisiae Gas2p in complex with laminaripentaose [Saccharomyces cerevisiae],2W63_A Saccharomyces Cerevisiae Gas2p In Complex With Laminaritriose And Laminaritetraose [Saccharomyces cerevisiae],5O9O_A Crystal structure of ScGas2 in complex with compound 7. [Saccharomyces cerevisiae S288C],5O9P_A Crystal structure of Gas2 in complex with compound 10 [Saccharomyces cerevisiae S288C],5O9Q_A Crystal structure of ScGas2 in complex with compound 6 [Saccharomyces cerevisiae S288C],5O9R_A Crystal structure of ScGas2 in complex with compound 9 [Saccharomyces cerevisiae S288C],5O9Y_A Crystal structure of ScGas2 in complex with compound 11 [Saccharomyces cerevisiae S288C],5OA2_A Crystal structure of ScGas2 in complex with compound 8 [Saccharomyces cerevisiae S288C],5OA2_B Crystal structure of ScGas2 in complex with compound 8 [Saccharomyces cerevisiae S288C],5OA2_C Crystal structure of ScGas2 in complex with compound 8 [Saccharomyces cerevisiae S288C],5OA6_A Crystal structure of ScGas2 in complex with compound 12 [Saccharomyces cerevisiae S288C]
2W61_A	2.69e-105	21	508	30	522	Saccharomyces cerevisiae Gas2p apostructure (E176Q mutant) [Saccharomyces cerevisiae]
5FIH_A	7.26e-105	21	508	30	522	SACCHAROMYCES CEREVISIAE GAS2P (E176Q MUTANT) IN COMPLEX WITH LAMINARITETRAOSE AND LAMINARIPENTAOSE [Saccharomyces cerevisiae]
3FHM_A	7.74e-09	556	660	38	141	Crystal structure of the CBS-domain containing protein ATU1752 from Agrobacterium tumefaciens [Agrobacterium fabrum str. C58],3FHM_B Crystal structure of the CBS-domain containing protein ATU1752 from Agrobacterium tumefaciens [Agrobacterium fabrum str. C58],3FHM_C Crystal structure of the CBS-domain containing protein ATU1752 from Agrobacterium tumefaciens [Agrobacterium fabrum str. C58],3FHM_D Crystal structure of the CBS-domain containing protein ATU1752 from Agrobacterium tumefaciens [Agrobacterium fabrum str. C58]
4GQY_A	6.58e-08	558	658	19	145	Crystal structure of CBSX2 in complex with AMP [Arabidopsis thaliana],4GQY_B Crystal structure of CBSX2 in complex with AMP [Arabidopsis thaliana],4GQY_C Crystal structure of CBSX2 in complex with AMP [Arabidopsis thaliana],4GQY_D Crystal structure of CBSX2 in complex with AMP [Arabidopsis thaliana]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|O13318|PHR2_CANAL	9.53e-131	24	480	25	478	pH-responsive protein 2 OS=Candida albicans (strain SC5314 / ATCC MYA-2876) OX=237561 GN=PHR2 PE=2 SV=2
sp|P56092|EPD1_CANMA	1.00e-126	9	480	10	478	Protein EPD1 OS=Candida maltosa OX=5479 GN=EPD1 PE=3 SV=1
sp|P22146|GAS1_YEAST	7.73e-125	24	480	25	479	1,3-beta-glucanosyltransferase GAS1 OS=Saccharomyces cerevisiae (strain ATCC 204508 / S288c) OX=559292 GN=GAS1 PE=1 SV=2
sp|Q9P378|GAS1_SCHPO	3.63e-123	24	479	21	473	1,3-beta-glucanosyltransferase gas1 OS=Schizosaccharomyces pombe (strain 972 / ATCC 24843) OX=284812 GN=gas1 PE=1 SV=1
sp|O74137|EPD2_CANMA	3.71e-120	31	451	33	461	Protein EPD2 OS=Candida maltosa OX=5479 GN=EPD2 PE=3 SV=1

SignalP and Lipop Annotations

This protein is predicted as SP

Other	SP_Sec_SPI	CS Position
0.162451	0.837541	CS pos: 22-23. Pr: 0.7721

TMHMM  Annotations     

Start	End
7	24
1057	1079