CAZyme Information: PSURA_73616T0-p1

Basic Information

• Species: Phytophthora ramorum
• Lineage: Oomycota; NA; ; Peronosporaceae; Phytophthora; Phytophthora ramorum
• CAZyme ID: PSURA_73616T0-p1
• CAZy Family: GH1
• CAZyme Description: unspecified product

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
1707	PramPr-102_SC0004|CGC2	186957.96	5.4901

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_PramorumPr-102	15743	N/A	251	15492

• Gene Location: location=PramPr-102_SC0004:351392-356764(-)

Full Sequence      

MRFLRGLLLSLALVRRRCSASLQDAQGLEFTDAAAFCAFHCSPALLSQTSQCSPTLCGAR
RALEATDQQIDVLSCNDVEQNASTLAFSLTLSTEDSSRVFRGFHDAFFQAYDAMLGGDSV
TADACQLAFLQDKLLPSVRDDDSEQEERAERKPRLVKLLTGQEEDQDRTCIVAIQKLWGQ
SEQNDTPLLTRRGDSLGENTVLLVHANESVAEQIRALECVDVVLDLPEILKLMPFARSAA
QLSDKMEQSAKGNTSVAAAPAMEIRLVSGADLNSTMSSFEQRASELFGLTNVFETSEYQP
KSIFTKPLQDLRTWTNILALAVVESSVEWLDERHELTQNVLRGEEQERWTQMQSHRRLDT
YVPSLVGVDSAREAGIRGNDVVVGITDTGLYLYHDQFDQTDRDIFSGMILSARKVVMYNG
WANKEDEAETITCGHGTHVAGLLAGSSFSGKHANLGIADKSRIAFMDIGTQDKSCAGKLN
CAVTLATPADASALLESQIDAGAKIFSFSWGTPGSDYSSQARDLDAFIYENPDVLVVVAA
GNSGESSNTGQQTISSPSGAKNVISVGASLNSAASFTDFGCPDIFNEHTVASFSSAGPTT
DGRLKPDVVAPGMSLTSSQSEAPGSTKDSSATCSLQGTSQATPVVTGVAVLLYEWLRDGW
WKDGTKNASYGMSSVPASLLKALIIHSGDTLQQRMASLPASGVVSCASLAADATEVTYPD
VYQGYGKPNLTNIVDFTGSGNSSVNGSTDSLPTLYFLPNSTENSEPSVEHGGEVVILFTV
ARDVDLRATLVWTDPPGSTQASSQLQHDLDLAVRVRNSTKTFGPLTADSSTGRDSKNNVE
MVHVSYTDLFAAAGGSNSSSSGSSNSNGTDSSALGDDGEIVVEAVIYGRSVLLADRQTFA
FVASSSAIGSTSGTSATTSDGGSFWSAWAVAIIVGCVIILLIIIASCTRWFHRRSKRAPR
SRSGREQYPAQAGIASASYHPTYAAAITSTNADRCPYCPFATPDAVAMVAHVEGAHANAT
NENNNEDVAIAVLGGSRIFGLEPTVPVVTTTPSPMQEAQGPAHDEKQQCPHCRFVAPDAV
ILLPSHPPLRRWKRLLLLSCLLYTSLLVFWFISTGRRRDDGGAGGVVGNFISTANLDEAK
LEYLQAHEDRELLVEIPFAELEMKFLHQNNASMERDEQAIAEAEAHTKTLKTFPVLEAKP
RRLRCIGWRATDDCSPNGPRMPNLDEPCNKVIPFGASGYCEVQDKDTGESFRVMNRYCSS
VRDTARFRCSESWDFAVFPQKAREAARKAQNRNFVLPNIAAKPSDQQEPRDGIVMVVYPK
LLASAYATIRTLRELLDCHLPIELWFRPQEMKFFPEAFAQLQQWSSEGSGSITFRKIDAP
SVTGFATKVFAIYHSFFERVLFLDADNVPVRNPNFLFESPEFEETGAVFWPDFWHPGKTI
FNIQPHSLVWELLDLPFVSMFEQESGQLLVDRRRHAAPLELVKFYTFHRPNHFDKMKLAH
GDKDLFRFAWLKLGASFHMIQSPPAVAGKVVNDSFCGMTMVQYDAQGAVLFLHRNSHKLM
GVPRRKATNMKAAAIRRARNKRLRMQMGEADRVTTDGNDTERAGLEITPSPTLDAPERDG
YPDMAIWTHLISLRNTSRRSEYRVGTYNADPDFEKGQNCYGRRYLNRSQHFITQEFANLS
YARLETELRRFAMEGAHFYGQAGITGR

Enzyme Prediction     

No EC number prediction in PSURA_73616T0-p1.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GT71	1311	1544	1.1e-48	0.9924242424242424

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
173791	Peptidases_S8_Kp43_protease	3.52e-82	375	689	3	293	Peptidase S8 family domain in Kp43 proteases. Kp43 proteases are members of the peptidase S8 or Subtilase clan of proteases. They have an Asp/His/Ser catalytic triad similar to that found in trypsin-like proteases, but do not share their three-dimensional structure (an example of convergent evolution). Kp43 is topologically similar to kexin and furin both of which are proprotein convertases, but differ in amino acids sequence and the position of its C-terminal barrel. Kp43 has 3 Ca2+ binding sites that differ from the corresponding sites in the other known subtilisin-like proteases. KP-43 protease is known to be an oxidation-resistant protease when compared with the other subtilisin-like proteases
395035	Peptidase_S8	2.25e-42	378	697	1	281	Subtilase family. Subtilases are a family of serine proteases. They appear to have independently and convergently evolved an Asp/Ser/His catalytic triad, like that found in the trypsin serine proteases (see pfam00089). Structure is an alpha/beta fold containing a 7-stranded parallel beta sheet, order 2314567.
402574	Mannosyl_trans3	6.97e-38	1311	1544	2	273	Mannosyltransferase putative. This family is conserved in fungi. Several members are annotated as being alpha-1,3-mannosyltransferase but this could not be confirmed.
173812	Peptidases_S8_1	8.48e-36	378	654	1	245	Peptidase S8 family domain, uncharacterized subfamily 1. This family is a member of the Peptidases S8 or Subtilases serine endo- and exo-peptidase clan. They have an Asp/His/Ser catalytic triad similar to that found in trypsin-like proteases, but do not share their three-dimensional structure and are not homologous to trypsin. The stability of subtilases may be enhanced by calcium, some members have been shown to bind up to 4 ions via binding sites with different affinity. Some members of this clan contain disulfide bonds. These enzymes can be intra- and extracellular, some function at extreme temperatures and pH values.
173787	Peptidases_S8_S53	2.44e-31	381	654	1	224	Peptidase domain in the S8 and S53 families. Members of the peptidases S8 (subtilisin and kexin) and S53 (sedolisin) family include endopeptidases and exopeptidases. The S8 family has an Asp/His/Ser catalytic triad similar to that found in trypsin-like proteases, but do not share their three-dimensional structure and are not homologous to trypsin. Serine acts as a nucleophile, aspartate as an electrophile, and histidine as a base. The S53 family contains a catalytic triad Glu/Asp/Ser with an additional acidic residue Asp in the oxyanion hole, similar to that of subtilisin. The serine residue here is the nucleophilic equivalent of the serine residue in the S8 family, while glutamic acid has the same role here as the histidine base. However, the aspartic acid residue that acts as an electrophile is quite different. In S53, it follows glutamic acid, while in S8 it precedes histidine. The stability of these enzymes may be enhanced by calcium; some members have been shown to bind up to 4 ions via binding sites with different affinity. There is a great diversity in the characteristics of their members: some contain disulfide bonds, some are intracellular while others are extracellular, some function at extreme temperatures, and others at high or low pH values.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
UIZ28119.1|GT71	1.59e-114	1315	1705	1	364
UIZ24000.1|GT71	4.05e-91	1205	1703	106	575
CCA25989.1|GT71	2.10e-88	1205	1565	98	466
UIZ24059.1|GT71	2.14e-88	1205	1696	143	596
UIZ27901.1|GT71	7.21e-82	1205	1561	72	421

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
5FAX_A	1.01e-38	375	845	18	404	Chain A, Subtilase SubHal from Bacillus halmapalus [Sutcliffiella halmapala],5FAX_B Chain B, Subtilase SubHal from Bacillus halmapalus [Sutcliffiella halmapala],5FBZ_A Chain A, Enzyme subtilase SubHal from Bacillus halmapalus [Sutcliffiella halmapala],5FBZ_C Chain C, Enzyme subtilase SubHal from Bacillus halmapalus [Sutcliffiella halmapala]
1WMD_A	2.07e-37	365	845	7	405	Crystal Structure of alkaline serine protease KP-43 from Bacillus sp. KSM-KP43 (1.30 angstrom, 100 K) [Bacillus sp. KSM-KP43],1WME_A Crystal Structure of alkaline serine protease KP-43 from Bacillus sp. KSM-KP43 (1.50 angstrom, 293 K) [Bacillus sp. KSM-KP43]
1WMF_A	6.86e-37	365	845	7	405	Crystal Structure of alkaline serine protease KP-43 from Bacillus sp. KSM-KP43 (oxidized form, 1.73 angstrom) [Bacillus sp. KSM-KP43]
3AFG_A	6.18e-14	375	668	135	387	Chain A, Subtilisin-like serine protease [Thermococcus kodakarensis],3AFG_B Chain B, Subtilisin-like serine protease [Thermococcus kodakarensis]
1BH6_A	1.80e-10	365	652	10	233	Subtilisin Dy In Complex With The Synthetic Inhibitor N- Benzyloxycarbonyl-Ala-Pro-Phe-Chloromethyl Ketone [Bacillus licheniformis]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|Q8T9W1|TAGD_DICDI	1.20e-35	376	840	327	866	Serine protease/ABC transporter B family protein tagD OS=Dictyostelium discoideum OX=44689 GN=tagD PE=3 SV=1
sp|Q9GTN7|TAGA_DICDI	6.74e-34	375	813	300	764	Serine protease/ABC transporter B family protein tagA OS=Dictyostelium discoideum OX=44689 GN=tagA PE=1 SV=2
sp|P54683|TAGB_DICDI	1.57e-31	376	847	376	916	Serine protease/ABC transporter B family protein tagB OS=Dictyostelium discoideum OX=44689 GN=tagB PE=3 SV=2
sp|Q23868|TAGC_DICDI	4.43e-31	376	843	314	864	Serine protease/ABC transporter B family protein tagC OS=Dictyostelium discoideum OX=44689 GN=tagC PE=2 SV=2
sp|Q59KJ7|MNN21_CANAL	1.32e-18	1284	1546	219	528	Alpha-1,2-mannosyltransferase MNN21 OS=Candida albicans (strain SC5314 / ATCC MYA-2876) OX=237561 GN=MNN21 PE=3 SV=1

SignalP and Lipop Annotations

This protein is predicted as OTHER

Other	SP_Sec_SPI	CS Position
0.999633	0.000412

TMHMM  Annotations     

Start	End
925	947
1095	1114