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CAZyme Information: KAG5438295.1

You are here: Home > Sequence: KAG5438295.1

Basic Information | Genomic context | Full Sequence | Enzyme annotations |  CAZy signature domains |  CDD domains | CAZyme hits | PDB hits | Swiss-Prot hits | SignalP and Lipop annotations | TMHMM annotations

Basic Information help

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 Start: 46206; End:50260  Strand: -

Full Sequence      Download help

MEFRCQALVL  HALIYVTLFV  YGRVETIQRR  GNFLFYSNGE  RFFIKGIAYQ  PQPSLGSTKH60
YTDPLGDPKI  CSRDLPYFLD  LGINTLRVYT  VDPELDHTYC  MNLFAESGIY  VLLDLSEPRV120
SIISTNPSWD  VILLYRYIKV  IDSMINYPNL  IGFFAGNEVV  LDTQNTHAAA  FVKAAIRDIK180
AYIKHKKYRN  VLVGYAANDH  HHTRIPSANY  FACGDSDSAA  DFFGINIYEW  CEPTTYETSG240
YKDRVNDFSN  FGIPLFFSEY  GCNIVNGNLG  VRTFKQIQYI  YSRYMTSVFS  GGIVYEWFQG300
ENSYGLVDLL  NDGTISPRKD  YLNLKMQLNL  LKSSPPDNLG  DRPTFSSPQC  PSINEYWSAS360
TSLPPVPNSE  LCSCASSASS  CVAVSDITNK  EMEDIFSYVC  SKISCRAISK  DGKAGVYGAY420
SVCNPIDQLN  VILGLYHSNF  NDDSACNFKG  TTYPTEPRVS  KTCSSLLRMV  GPDGTGTITG480
PPYATEHTKG  DASQKHKGGS  EKELSMKWKL  ILGLEIAIRR  KIENELSKKK  PTAARMHPSR540
KMDPKTVLSL  SPSPPLTVQS  GITVSEASQL  MAAKREDCVL  VVDDNQHLMG  IFTAKDLAFR600
VVGMDMDPRN  LLIEDIMTKN  PLCARNDTSA  TDALDLMVHK  GFRHLPVCDE  DGNVSGILDI660
TKCFHEAMKK  VERAYTSSRQ  LYDALEGVQT  EWGQIEQSEQ  IIQYVETLKQ  KMSGPNLASA720
LDGTTPITVN  IRTSVRDAAF  LMRENHTTAV  LVMDQMNISG  IFTSKDIVLR  VIAPGLDPAN780
CSVVRVMTPH  PDCVPMDMSI  QEALKKMDEG  RYLNLPVLDQ  ESQVIGMVDV  MKLTYLILEQ840
IKNIGSPDGE  GLIWNRFWNN  LEDGDSESIL  SDNQLSTSQN  YQSLLYASLP  NNQQDIQVLS900
PDTSATKLPQ  KNEWTSPTER  PTFSGKNSPL  LSQIPFVFKF  KSLYGKTHRI  QLIPQAGYAS960
LRLAIIERLR  SELEKLGGSD  DLAISFIDDE  GDSVSMTTDD  DMFHAVELAY  KNAEDKVNLI1020
IHHPNSSIIN  QKSDDLSSIT  ENHHNEKASQ  SKSPKLTGYF  VSISIAFCIT  TIAIVYKYIR1080
K1081

Enzyme Prediction      help

EC 2.4.1.-:30 2.4.1.-:33

CAZyme Signature Domains help

Created with Snap5410816221627032437843248654059464870275681086491897210264310GH72
Family Start End Evalue family coverage
GH72 23 329 6.7e-120 0.9807692307692307

CDD Domains      download full data without filtering help

Created with Snap54108162216270324378432486540594648702756810864918972102624329Glyco_hydro_72552669CBS_pair_MUG70_1723839CBS_pair_MUG70_2726832CBS_pair_MUG70_1553661CBS_pair_SF
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      help

Created with Snap54108162216270324378432486540594648702756810864918972102653514QSL64406.1|CBM43|GH7214514AAF05967.1|CBM43|GH7226480AWU75603.1|CBM43|GH7226480AWU49727.1|CBM43|GH7226480AOA61229.1|CBM43|GH72
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      download full data without filtering help

Created with Snap541081622162703243784324865405946487027568108649189721026215082W62_A215082W61_A215085FIH_A5566603FHM_A5586584GQY_A
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      download full data without filtering help

Created with Snap54108162216270324378432486540594648702756810864918972102624480sp|O13318|PHR2_CANAL9480sp|P56092|EPD1_CANMA24480sp|P22146|GAS1_YEAST24479sp|Q9P378|GAS1_SCHPO31451sp|O74137|EPD2_CANMA
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 help

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      download full data without filtering help

Start End
7 24
1057 1079