CAZyme Information: GAQ04191.1

Basic Information

• Species: Aspergillus lentulus
• Lineage: Ascomycota; Eurotiomycetes; ; Aspergillaceae; Aspergillus; Aspergillus lentulus
• CAZyme ID: GAQ04191.1
• CAZy Family: CBM21
• CAZyme Description: Protein kinase domain-containing protein [Source:UniProtKB/TrEMBL;Acc:A0A0S7DH20]

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
1510	BCLY01000004|CGC33	168413.80	8.2487

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_AlentulusIFM54703	9916	N/A	259	9657

• Gene Location: location=BCLY01000004:664891-671317(+)

Full Sequence      

MEVASLVLAVAGTLDLCLKYGKSLVMLCREQRNLESDLDEISLTFEGLWIKTEIQLQSVK
ALWTTLPPALQAHYGDVLSHLQIKITGAFKTYERVTAFVNAAYRIQRRVRAVYLKRHLQQ
IVLDLEEWQKRFDPSWYLITRIANPLVDQQLGSSVSSRDPSMRRLKMMRKAIQACHSGHD
IEQGSVFKNAGVIADILLDRICYKAGAVGIDGRKNVRDLARLLLHVEPDTFSLLKCSGVV
ELGEEGNTQFQYIFEIPEGLSTPKTLRSLLREMIRCSLSQRFQLAKHLARSVMFLHATGF
VHKNIRPETMIVFANTTGSMRQSFLIGFESIRKEGGSTERIGDLEWERNLYRHPMRQGLF
PEDVFTMEHDIYSLGVCLLEVGMWSSFVLNEGDAVTPCGELEISNALADNDPRRRGFAVK
DRLVQLSKERLPSLVGDSRSALKNLVSRRRPTLYAPNKRNGPESDHDYKYAEYAMAKGPS
GTEFGRLSSKQKMDSAQPTKLDFLAVPATPFSIGVLASVLVLVAVLIGPKVVIDTILNGY
LSLVHRIPAANGKKYMSGPAYTFPNGQMVDKFLAARKRSWEWEEKYGKTYRIWAASIPEV
VITDPKDVEALYQQSTDHNKAPQANAGWLLTQLLGSGLGLINGTRWTTLRKTLDPMFSHR
TALRYFRDSLDAGAQDYVAGIHRFAKADGQMQNADGKGMVINATQALQRYPFFEVASMFY
GKMSEGEQERLWDLGRLYSEVFAAVVSGGIHRSKLTRYLNTKAWNNARDYQKAWLDFNRE
IYAARKITAPDTPIVVLTEAAERGELTPNEVTDTIAESTFANLDIVTHVISSCIILLADS
PEVQNDLVQEMEKNKADREDYITRKDTLLHYCLLESLRLRPVLTFTFPENPPREKILGNF
VIPKDTTVIVDAFAINIRNPFWGPDNRAYRPSRFAGIKQSQLRYNLATFGYGPRKCLGQH
IADKIIKAVVYHMFSKYRVSLQPMQAVEGDFKVDKTSWVSLKWSDEEWRFIRNTAPDVCW
GRRRVNSVSTSTAPKPNFVGVTMASNLKSDLLNCLSGSNVIVDGDEAWSDAIKRWTGYLA
KFPAAVVQVTSEEDVIATVSYAVQNQRPFVVRGGGHSNGFSTIDSPGIIIDLSRMRKVAV
DVERQVVVAQGGATMGDGVKAASSVGMAVATGTCNEVGLIGAALGGGIGRFLGHFGYAAD
TVLSMRVVVVDQSGVARAVEASPEVNSDLFWGLRGGGHLFGVVVEATFRAYPWTHDTWHS
CLVFAPNDAGLVAEAVNKVHYQGGMQGRLVFCAPNKQPIVLLQMWYMGSHEEAASKFQPL
LDLPSMTDHPLNFVGRRIPYPNLNDSSDRICGYGGRKNLAAFGLKNLSAGSCMAALNVYM
DFITQHPEAAQTHILTEFYSMDAARELDQDGQETSIPGEFRREVKYWVMPLAWYDDPALD
NACVGLNKAIREAFLTQPDGTRATGVGYVNMPFEDDTATSVFGEGERLERLRKLKLTWDP
LGVVQGIVKL

Enzyme Prediction     

EC	1.1.3.-:1

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
AA7	1073	1305	8.7e-58	0.5065502183406113

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
410708	CYP_GliC-like	0.0	587	999	1	409	cytochrome P450 monooxygenases similar to gliotoxin biosynthesis protein C. This subfamily is composed of cytochrome P450 monooxygenases that are part of gene clusters involved in the biosynthesis of various compounds such as mycotoxins and alkaloids, including Aspergillus fumigatus gliotoxin biosynthesis protein (GliC), Penicillium rubens roquefortine/meleagrin synthesis protein R (RoqR), Aspergillus oryzae aspirochlorine biosynthesis protein C (AclC), Aspergillus terreus bimodular acetylaranotin synthesis protein ataTC, Kluyveromyces lactis pulcherrimin biosynthesis cluster protein 2 (PUL2), and Aspergillus nidulans aspyridones biosynthesis protein B (ApdB). The GliC-like subfamily belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.
410651	cytochrome_P450	1.47e-46	587	988	1	377	cytochrome P450 (CYP) superfamily. Cytochrome P450 (P450, CYP) is a large superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs with > 40% sequence identity are members of the same family. There are approximately 2250 CYP families: mammals, insects, plants, fungi, bacteria, and archaea have around 18, 208, 277, 805, 591, and 14 families, respectively. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop. Their monooxygenase activity relies on the reductive scission of molecular oxygen bound to the P450 heme iron, and the delivery of two electrons to the heme iron during the catalytic cycle. CYPs use a variety of redox partners, such as the eukaryotic diflavin enzyme NADPH-cytochrome P450 oxidoreductase and the bacterial/mitochondrial NAD(P)H-ferredoxin reductase and ferredoxin partners. Some CYPs are naturally linked to their redox partners and others have evolved to bypass requirements for redox partners, and instead react directly with hydrogen peroxide or NAD(P)H to facilitate oxidative or reductive catalysis.
395020	p450	2.97e-36	584	988	31	442	Cytochrome P450. Cytochrome P450s are haem-thiolate proteins involved in the oxidative degradation of various compounds. They are particularly well known for their role in the degradation of environmental toxins and mutagens. They can be divided into 4 classes, according to the method by which electrons from NAD(P)H are delivered to the catalytic site. Sequence conservation is relatively low within the family - there are only 3 absolutely conserved residues - but their general topography and structural fold are highly conserved. The conserved core is composed of a coil termed the 'meander', a four-helix bundle, helices J and K, and two sets of beta-sheets. These constitute the haem-binding loop (with an absolutely conserved cysteine that serves as the 5th ligand for the haem iron), the proton-transfer groove and the absolutely conserved EXXR motif in helix K. While prokaryotic P450s are soluble proteins, most eukaryotic P450s are associated with microsomal membranes. their general enzymatic function is to catalyze regiospecific and stereospecific oxidation of non-activated hydrocarbons at physiological temperatures.
410677	CYP24A1-like	9.95e-30	584	980	2	405	cytochrome P450 family 24 subfamily A, polypeptide 1 and similar cytochrome P450s. This family is composed of vertebrate cytochrome P450 24A1 (CYP24A1) and similar proteins including several Drosophila proteins such as CYP315A1 (also called protein shadow) and CYP314A1 (also called ecdysone 20-monooxygenase), and vertebrate CYP11 and CYP27 subfamilies. Both CYP314A1 and CYP315A1, which has ecdysteroid C2-hydroxylase activity, are involved in the metabolism of insect hormones. CYP24A1 and CYP27B1 have roles in calcium homeostasis and metabolism, and the regulation of vitamin D. CYP24A1 catabolizes calcitriol (1,25(OH)2D), the physiologically active vitamin D hormone, by catalyzing its hydroxylation, while CYP27B1 is a calcidiol 1-monooxygenase that coverts 25-hydroxyvitamin D3 to calcitriol. The CYP24A1-like family belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.
223354	GlcD	3.06e-26	1083	1338	32	290	FAD/FMN-containing dehydrogenase [Energy production and conversion].

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QRC92907.1|AA7	2.98e-17	1037	1264	11	239
UQC87672.1|AA7	7.14e-17	1031	1251	16	235
CAE7214923.1|AA7	2.72e-15	1053	1251	31	230
QPH04356.1|AA7	1.42e-14	1048	1251	84	287
CCA69005.1|AA7	2.38e-14	1048	1257	23	223

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
6FYG_A	1.49e-23	1060	1248	22	206	The crystal structure of EncM V135T mutant [Streptomyces maritimus],6FYG_B The crystal structure of EncM V135T mutant [Streptomyces maritimus],6FYG_C The crystal structure of EncM V135T mutant [Streptomyces maritimus],6FYG_D The crystal structure of EncM V135T mutant [Streptomyces maritimus]
6FYD_A	2.00e-23	1060	1248	22	206	The crystal structure of EncM T139V mutant [Streptomyces maritimus],6FYD_B The crystal structure of EncM T139V mutant [Streptomyces maritimus],6FYD_C The crystal structure of EncM T139V mutant [Streptomyces maritimus],6FYD_D The crystal structure of EncM T139V mutant [Streptomyces maritimus]
2BVF_A	3.39e-23	1047	1308	2	265	Crystal structure of 6-hydoxy-D-nicotine oxidase from Arthrobacter nicotinovorans. Crystal Form 3 (P1) [Paenarthrobacter nicotinovorans],2BVF_B Crystal structure of 6-hydoxy-D-nicotine oxidase from Arthrobacter nicotinovorans. Crystal Form 3 (P1) [Paenarthrobacter nicotinovorans],2BVG_A Crystal structure of 6-hydoxy-D-nicotine oxidase from Arthrobacter nicotinovorans. Crystal Form 1 (P21) [Paenarthrobacter nicotinovorans],2BVG_B Crystal structure of 6-hydoxy-D-nicotine oxidase from Arthrobacter nicotinovorans. Crystal Form 1 (P21) [Paenarthrobacter nicotinovorans],2BVG_C Crystal structure of 6-hydoxy-D-nicotine oxidase from Arthrobacter nicotinovorans. Crystal Form 1 (P21) [Paenarthrobacter nicotinovorans],2BVG_D Crystal structure of 6-hydoxy-D-nicotine oxidase from Arthrobacter nicotinovorans. Crystal Form 1 (P21) [Paenarthrobacter nicotinovorans],2BVH_A Crystal structure of 6-hydoxy-D-nicotine oxidase from Arthrobacter nicotinovorans. Crystal Form 2 (P21) [Paenarthrobacter nicotinovorans],2BVH_B Crystal structure of 6-hydoxy-D-nicotine oxidase from Arthrobacter nicotinovorans. Crystal Form 2 (P21) [Paenarthrobacter nicotinovorans],2BVH_C Crystal structure of 6-hydoxy-D-nicotine oxidase from Arthrobacter nicotinovorans. Crystal Form 2 (P21) [Paenarthrobacter nicotinovorans],2BVH_D Crystal structure of 6-hydoxy-D-nicotine oxidase from Arthrobacter nicotinovorans. Crystal Form 2 (P21) [Paenarthrobacter nicotinovorans]
4XLO_A	6.36e-23	1060	1248	22	206	Crystal Structure of EncM (crystallized with 4 mM NADPH) [Streptomyces maritimus],4XLO_B Crystal Structure of EncM (crystallized with 4 mM NADPH) [Streptomyces maritimus],4XLO_C Crystal Structure of EncM (crystallized with 4 mM NADPH) [Streptomyces maritimus],4XLO_D Crystal Structure of EncM (crystallized with 4 mM NADPH) [Streptomyces maritimus],6FOQ_A The crystal structure of EncM complexed with dioxygen under 15 bar of oxygen pressure. [Streptomyces maritimus],6FOQ_B The crystal structure of EncM complexed with dioxygen under 15 bar of oxygen pressure. [Streptomyces maritimus],6FOQ_C The crystal structure of EncM complexed with dioxygen under 15 bar of oxygen pressure. [Streptomyces maritimus],6FOQ_D The crystal structure of EncM complexed with dioxygen under 15 bar of oxygen pressure. [Streptomyces maritimus],6FOW_A The crystal structure of EncM complexed with dioxygen under 10 bar of oxygen pressure. [Streptomyces maritimus],6FOW_B The crystal structure of EncM complexed with dioxygen under 10 bar of oxygen pressure. [Streptomyces maritimus],6FOW_C The crystal structure of EncM complexed with dioxygen under 10 bar of oxygen pressure. [Streptomyces maritimus],6FOW_D The crystal structure of EncM complexed with dioxygen under 10 bar of oxygen pressure. [Streptomyces maritimus],6FP3_A The crystal structure of EncM complexed with dioxygen under 5 bar of oxygen pressure. [Streptomyces maritimus],6FP3_B The crystal structure of EncM complexed with dioxygen under 5 bar of oxygen pressure. [Streptomyces maritimus],6FP3_C The crystal structure of EncM complexed with dioxygen under 5 bar of oxygen pressure. [Streptomyces maritimus],6FP3_D The crystal structure of EncM complexed with dioxygen under 5 bar of oxygen pressure. [Streptomyces maritimus],6FY8_A The crystal structure of EncM bromide soak [Streptomyces maritimus],6FY9_A The crystal structure of EncM complex with xenon under 15 bars Xe pressure [Streptomyces maritimus],6FYA_A The crystal structure of EncM under anaerobic conditions [Streptomyces maritimus],6FYA_B The crystal structure of EncM under anaerobic conditions [Streptomyces maritimus]
6FYB_A	6.36e-23	1060	1248	22	206	The crystal structure of EncM L144M mutant [Streptomyces maritimus],6FYB_B The crystal structure of EncM L144M mutant [Streptomyces maritimus],6FYB_C The crystal structure of EncM L144M mutant [Streptomyces maritimus],6FYB_D The crystal structure of EncM L144M mutant [Streptomyces maritimus],6FYC_A The crystal structure of EncM L144M mutant complex with dioxygen under 15 bars O2 pressure [Streptomyces maritimus],6FYC_B The crystal structure of EncM L144M mutant complex with dioxygen under 15 bars O2 pressure [Streptomyces maritimus]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|Q6Q881|SIRC_LEPMC	4.97e-105	535	1001	32	455	Cytochrome P450 monooxygenase sirC OS=Leptosphaeria maculans OX=5022 GN=sirC PE=1 SV=1
sp|M1W080|TCPC_CLAP2	4.09e-101	533	1007	33	494	Cytochrome P450 monooxygenase tcpC OS=Claviceps purpurea (strain 20.1) OX=1111077 GN=tcpC PE=2 SV=1
sp|B8N0E9|ASAD_ASPFN	1.41e-91	510	1000	17	501	Cytochrome P450 monooxygenase asaD OS=Aspergillus flavus (strain ATCC 200026 / FGSC A1120 / IAM 13836 / NRRL 3357 / JCM 12722 / SRRC 167) OX=332952 GN=asaD PE=2 SV=1
sp|E9RCR4|GLIC_ASPFU	1.67e-90	511	1001	3	495	Cytochrome P450 monooxygenase gliC OS=Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100) OX=330879 GN=gliC PE=1 SV=1
sp|A0A1U9YHZ9|VERC_CLORO	2.86e-82	556	1001	56	488	Cytochrome P450 monooxygenase verC OS=Clonostachys rogersoniana OX=122658 GN=verC PE=2 SV=2

SignalP and Lipop Annotations

This protein is predicted as OTHER

Other	SP_Sec_SPI	CS Position
1.000022	0.000003

TMHMM  Annotations     

There is no transmembrane helices in GAQ04191.1.