CAZyme Information: P170DRAFT_468143-t37_1-p1

Basic Information

• Species: Aspergillus steynii
• Lineage: Ascomycota; Eurotiomycetes; ; Aspergillaceae; Aspergillus; Aspergillus steynii
• CAZyme ID: P170DRAFT_468143-t37_1-p1
• CAZy Family: GT1
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
1402		149632.61	4.1992

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_AsteyniiIBT23096	13430	1392250	235	13195

• Gene Location: location=MSFO01000009:1064639-1068910(+)

Full Sequence      

MPLSLFLLSLVFSLFTFLSQASAGPTHDAWSRLWSPCPTDCSDSSPAEWAAYNGLSRLAA
CNGLSRLAACNQTMRLQFSLYNPSSSIRACSASSNPHSVQAALAPAFSEKFQSQEVSLEL
GWWDTPTSSSPAGVKAAVEEARKALMTSSNNKSTTTFSYSGKSLVGLYAGHGVLHSDAAT
TALQHFTQYLESQETIGRVLLQYCGINSNKALGIVVDTTGDFSAVQRIMRDWNEAKCQTD
FDGSKKLSTTALRLERPFTQANSTTDDLTRRHSHHHGAHHDHSIHRRATCETIQVASGDS
CGSLAKECGITGAKFEEYNPDKNLCSTLSVGQYVCCTAGDLPDLTPKPEPDGTCASTIVE
DGDYCSKIASANGISVEDLEDFNKKTWGWAGCDLLQPKQRICLSKGDPAMPESLDNAVCG
PQVPGTKQPTNGTDLADLNQCPLKSCCNIWGQCGITDDFCTITESETGAPGTAANGTYGC
ISNCGTDIVNNDSPPDSFITIGYFEAWNFERKCLNMDIAYFDTSAYSHLHFAFAEITKDY
KVDVSAVQSQFDSLLSMGEVHRVLSFGGWSFSTEVDSFPIFREGVTDANRELFATNVVNF
IVDNDLEGVDFDWEYPGAPDIPGIPAGDEGDGERYLQFLKLVREKLPKSKTLAIAAPASF
WYLKGFPIAEISEVVDYIVYMAYDLHGQWDYGNQYATSGCTKGDCLRSHVNLTETTSALS
MITKAGVSSDKIIVGLASYGRSFKMTKEGCTGPMCRFVGPDSGAAKGECTDTAGYISDAE
IYRILDEDDTAETFYDKSSDSNILVYGSTEWVAFMDADTRSSRTDYYEGLNMGGTTDWAV
DLQAVGFSGGGGGGSGDGGGTLNQSIVYISPSIWTDGEDPATVQCPAPCVLVLPDFPLSS
TSVISRPPYVTTLDVAWPTAATLTTGGSTVTTTTVTHILQETTIKAPAVTVSSLPMANLN
ITVPIDGNSTITITPRPRFPAQAVTITNDPNPLSITGVSHPPVTRSVTLPPWPQGTVIYY
PKDYVDDGRDDNNDDDDDNDDDDDDNGNDEDDGIDLPAIPIIVVKDGPGSPRCGADENCG
HVCSGPLSFCSCFICPNGGGAGDGGFSDPNDPNPPPRPPGDPVNNNNNNPDDPDRSCTKT
STETNYWVSCESLASTSTSCTTTSSMLAIGCDVTATTTTTGEGVCSSFNPDEDQGDANGR
PTSGGSTTVPTVSATATTTTNKEPSTSSKTTTTKTSTTSASPPSATAADGCSKVGGSSSS
TRRCWNKCDPGTGSPIGGDWAQNDPWCYISESGSDEYANCFKQSDCPTDFECAESWGCVV
PLARGCAPQGGKTQLGKTCWSSCNEKTGKRTNDEWEEGMAWCWLKNDRFFASCDEDDDCD
ATTECVPDSWSHGGCDTNDKAS

Enzyme Prediction     

EC	3.2.1.14:3	3.2.1.14:3	3.2.1.14:3	3.2.1.14:3

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH18	501	841	4.8e-52	0.918918918918919

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
119357	GH18_zymocin_alpha	0.0	501	843	3	345	Zymocin, alpha subunit. Zymocin is a heterotrimeric enzyme that inhibits yeast cell cycle progression. The zymocin alpha subunit has a chitinase activity that is essential for holoenzyme action from the cell exterior while the gamma subunit contains the intracellular toxin responsible for G1 phase cell cycle arrest. The zymocin alpha and beta subunits are thought to act from the cell's exterior by docking to the cell wall-associated chitin, thus mediating gamma-toxin translocation. The alpha subunit has an eight-stranded TIM barrel fold similar to that of family 18 glycosyl hydrolases such as hevamine, chitolectin, and chitobiase.
214753	Glyco_18	1.49e-57	501	842	3	333	Glyco_18 domain.
395573	Glyco_hydro_18	8.01e-47	500	841	2	305	Glycosyl hydrolases family 18.
119365	GH18_chitinase	2.52e-40	501	744	2	267	The GH18 (glycosyl hydrolases, family 18) type II chitinases hydrolyze chitin, an abundant polymer of N-acetylglucosamine and have been identified in bacteria, fungi, insects, plants, viruses, and protozoan parasites. The structure of this domain is an eight-stranded alpha/beta barrel with a pronounced active-site cleft at the C-terminal end of the beta-barrel.
225862	ChiA	2.20e-33	495	841	35	421	Chitinase, GH18 family [Carbohydrate transport and metabolism].

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
BCS25711.1|CBM18|CBM50|GH18	0.0	2	1395	6	1387
UCK57077.1|CBM18|CBM50|GH18	0.0	1	1401	1	1395
QMW24763.1|CBM18|CBM50|GH18	0.0	1	1397	1	1396
QRD89348.1|CBM18|CBM50|GH18	0.0	1	1401	1	1419
EGX48217.1|CBM18|CBM50|GH18	3.47e-253	17	844	15	842

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
1HKK_A	2.90e-23	503	848	6	348	High resoultion crystal structure of human chitinase in complex with allosamidin [Homo sapiens]
1HKI_A	2.95e-23	503	848	6	348	Crystal structure of human chitinase in complex with glucoallosamidin B [Homo sapiens],1HKJ_A Crystal structure of human chitinase in complex with methylallosamidin [Homo sapiens],1HKM_A High resolution crystal structure of human chitinase in complex with demethylallosamidin [Homo sapiens]
1LG1_A	3.96e-23	503	848	6	348	Crystal Structure Of Human Chitotriosidase In Complex With Chitobiose [Homo sapiens],1LG2_A Crystal Structure Of Human Chitotriosidase In Complex With Ethylene Glycol [Homo sapiens],1LQ0_A Crystal Structure Of Human Chitotriosidase At 2.2 Angstrom Resolution [Homo sapiens],6ZE8_A Crystal structure of human chitotriosidase-1 (hCHIT) catalytic domain in complex with compound OATD-01 [Homo sapiens],6ZE8_B Crystal structure of human chitotriosidase-1 (hCHIT) catalytic domain in complex with compound OATD-01 [Homo sapiens],6ZE8_C Crystal structure of human chitotriosidase-1 (hCHIT) catalytic domain in complex with compound OATD-01 [Homo sapiens],6ZE8_D Crystal structure of human chitotriosidase-1 (hCHIT) catalytic domain in complex with compound OATD-01 [Homo sapiens],6ZE8_E Crystal structure of human chitotriosidase-1 (hCHIT) catalytic domain in complex with compound OATD-01 [Homo sapiens],6ZE8_F Crystal structure of human chitotriosidase-1 (hCHIT) catalytic domain in complex with compound OATD-01 [Homo sapiens]
1GUV_A	4.03e-23	503	848	6	348	Structure of human chitotriosidase [Homo sapiens]
4WJX_A	4.75e-23	503	848	6	348	Crystal structure of human chitotriosidase-1 catalytic domain at 1.0 A resolution [Homo sapiens],4WK9_A Crystal structure of human chitotriosidase-1 catalytic domain in complex with chitobiose (0.3mM) at 1.10 A resolution [Homo sapiens],4WKA_A Crystal structure of human chitotriosidase-1 catalytic domain at 0.95 A resolution [Homo sapiens],4WKF_A Crystal structure of human chitotriosidase-1 catalytic domain in complex with chitobiose (2.5mM) at 1.10 A resolution [Homo sapiens],4WKH_A Crystal structure of human chitotriosidase-1 catalytic domain in complex with chitobiose (1mM) at 1.05 A resolution [Homo sapiens],5NR8_A Crystal structure of human chitotriosidase-1 (hCHIT) catalytic domain in complex with compound 7a [Homo sapiens],5NRA_A Crystal structure of human chitotriosidase-1 (hCHIT) catalytic domain in complex with compound 7g [Homo sapiens],5NRF_A Crystal structure of human chitotriosidase-1 (hCHIT) catalytic domain in complex with compound 7i [Homo sapiens]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|P09805|KTXA_KLULA	8.38e-109	210	841	133	710	Killer toxin subunits alpha/beta OS=Kluyveromyces lactis (strain ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 / WM37) OX=284590 PE=1 SV=1
sp|Q95M17|CHIA_BOVIN	1.01e-22	527	843	52	365	Acidic mammalian chitinase OS=Bos taurus OX=9913 GN=CHIA PE=1 SV=1
sp|Q13231|CHIT1_HUMAN	7.22e-22	503	848	27	369	Chitotriosidase-1 OS=Homo sapiens OX=9606 GN=CHIT1 PE=1 SV=1
sp|Q6RY07|CHIA_RAT	2.44e-20	527	843	52	365	Acidic mammalian chitinase OS=Rattus norvegicus OX=10116 GN=Chia PE=2 SV=1
sp|P36362|CHIT_MANSE	4.22e-20	527	843	53	375	Endochitinase OS=Manduca sexta OX=7130 PE=2 SV=1

SignalP and Lipop Annotations

This protein is predicted as SP

Other	SP_Sec_SPI	CS Position
0.000285	0.999680	CS pos: 23-24. Pr: 0.9705

TMHMM  Annotations     

There is no transmembrane helices in P170DRAFT_468143-t37_1-p1.