CAZyme Information: FOC1_g10009133-t38_1-p1

Basic Information

• Species: Fusarium oxysporum
• Lineage: Ascomycota; Sordariomycetes; ; Nectriaceae; Fusarium; Fusarium oxysporum
• CAZyme ID: FOC1_g10009133-t38_1-p1
• CAZy Family: GH47
• CAZyme Description: Killer toxin subunits alpha/beta

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
1713		188074.00	6.3590

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_Foxysporumrace1	15626	1229664	188	15438

• Gene Location: location=KB731255:270746-280612(+)

Full Sequence      

MRISTFIAAVLSTVFTIYPAFASGTAAPQLNSCPPLIDEACVDSSNWTLFTNLDEALACN
HKPRLLDFTIHYPLRPSGPGNVLRACTSYQGETLNLTSVVSTSSLARNNQTKSKLELVWD
DTDEKVIMPQAITALKELQSFLLTEGSKDRQSIFSQYGDTSVGLYIGDKVVPSSVANVVI
EALVKRLRESGMPRRLGVQLCGDGRNSDYTSGIIIDTKPGPASLINAQVAVSGWSNATCI
DGFQHSSNFGSFLIETIKEDTAVSRPSNSTAPKLAKRAECKTIQVKSGDGCGDLAQRCGI
KAADFTKYNSQTKNLCSTLIDGQHVCCSSGDLPDFRPKPKPDGSCATYTVESGDFCNKIA
AANSLKVEDIESFNKNTWGWSGCKLLFDKAVICLSKGDPPMPNPIANAECGPQKPGTKKP
ENGKDLADLNPCPLNACCNIWGQCGVTADFCKNTTLGAPGTAKPGTNGCISNCGTDIVNN
KSPPSSFIIDISHVSYQFNKFKKLKGSKRILAFGGWVDSTHPTKYHILRNAVKMENRLQV
AKNIAAFVKKHDLDGVDIDWEYPGAPDIPDIPKADEEDGKNYLGLLTLLKGQLGGLSLSI
AAPASFWYLKPYPINNIAKVVDYIIDMTYDLHGQWDYDNKWASPGCPKGNCLRSHVNLTE
TMGALAMITKAGVPSTKVIVGVTSYGRSFKMAKKGCVGPIDSDILVYNDTEWVAYMSDST
KKRRISKYQGLNFGGVTDWAVDLQKFGKLEDSNLIEIIDKDGKCKWKTKDGFSCLDKAVI
ESDMNPQDRWNGVRAPCAWRDMASSWVDKRSSQNINVTGKENANKFSRHVSDLADGYEKF
DCASFSVGVNGCEQEDKCEDTRDSGPAGYFILNSFTSIHTTFKSLWQTVDKVENGMQSKL
DQLVETFAPDVDESSEFNLIADFLGIAVGMFAAPFFNKIMKTKDSPTADIKDLIANTASW
GATLAKDIQNSKRETPKSKVAGKLSEISDLWTESIEAFTEKAFRGDDESVDYIGDLIADG
KFNNDEVTFDMSDLRKQLRKVFFAVLIPEAWKVGAGYAPAFVMDSGYDCNAVGPLDYEYI
APSTGEEMGYCYQGRRYYLLAPNGRERNCDPQVPGGTGGNPTDCKPNYFTAPQGIENLDP
KNQDTYDWGGITAQDLVAGAVEGWKANKEKNGGGFLDLTKTSNYDFLLDGNSDEVNIRLP
GFIQIPYGGHNGNWNSTAHGGSKPSPNGGSNSGSKCGSSGGSQTSSNGGSSSGSSFGSNR
GPNGSNGSGSKNTQPSIVPVISGAAEQIWQNTLTPFQSTHQFQTLESTFRFRQADGQELD
CGRAKITPDLGDSISAVLTFVPLAILVVVTLSSWRVNQSSLTYAHGLNASSLWSVVLDVT
SYLRYLQFAFIAALMSIEYPGFFVPAVSKLSWASLLYWSGPFSNGYMYEGPTGAGHFLIQ
VLDDQAAYAVWDDREASKGRFIGYLYMDLLSRDNKYKGNQNVNLQCGYLKNDGSRVYPAT
LLMCSFPPPAPSACTFLKHSQIISLFHEELTRSELGHGIHDLLARTNYVAFHGHRSPPDF
AETLSVMLEKWCWMKPELKRLGLHYTSTDLHLKEKWLREHPGEDLPPERIPDDTIERLIK
GRQVTRSLWYLRQLVYAHFDMKVHHPRSHTELRNMDSTKIFNDLLEKLWLVRAPQPEDQG
YPHADLGHLVSGYDAGYYSYLRRVDLNLTIKND

Enzyme Prediction     

EC	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	490	742	8.4e-38	0.8243243243243243

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
119357	GH18_zymocin_alpha	2.49e-150	485	744	40	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.
341050	M3A_TOP	4.20e-97	1443	1701	356	581	Peptidase M3 thimet oligopeptidase (TOP), also includes neurolysin. Peptidase M3 Thimet oligopeptidase (TOP; PZ-peptidase; endo-oligopeptidase A; endopeptidase 24.15; soluble metallo-endopeptidase; EC 3.4.24.15) family also includes neurolysin (endopeptidase 24.16, microsomal endopeptidase, mitochondrial oligopeptidase M, neurotensin endopeptidase, soluble angiotensin II-binding protein, thimet oligopeptidase II) which hydrolyzes oligopeptides such as neurotensin, bradykinin and dynorphin A. TOP and neurolysin are neuropeptidases expressed abundantly in the testis, but are also found in the liver, lung and kidney. They are involved in the metabolism of neuropeptides under 20 amino acid residues long and cleave most bioactive peptides at the same sites, but recognize different positions on some naturally occurring and synthetic peptides; they cleave at distinct sites on the 13-residue bioactive peptide neurotensin, which modulates central dopaminergic and cholinergic circuits. TOP has been shown to degrade peptides released by the proteasome, limiting the extent of antigen presentation by major histocompatibility complex class I molecules, and has been associated with amyloid protein precursor processing.
341068	M3A	1.07e-41	1450	1701	308	526	Peptidase M3A family includes thimet oligopeptidase, dipeptidyl carboxypeptidase and mitochondrial intermediate peptidase. The M3-like family also called neurolysin-like family, is part of the "zincins" metallopeptidases, and includes M3, M2 and M32 families of metallopeptidases. The M3 family is subdivided into two subfamilies: the widespread M3A, represented by this CD, which comprises a number of high-molecular mass endo- and exopeptidases from bacteria, archaea, protozoa, fungi, plants and animals, and the small M3B, whose members are enzymes primarily from bacteria. Well-known mammalian/eukaryotic M3A endopeptidases are the thimet oligopeptidase (TOP; endopeptidase 3.4.24.15), neurolysin (alias endopeptidase 3.4.24.16), and the mitochondrial intermediate peptidase. The first two are intracellular oligopeptidases, which act only on relatively short substrates of less than 20 amino acid residues, while the latter cleaves N-terminal octapeptides from proteins during their import into the mitochondria. The M3A subfamily also contains several bacterial endopeptidases, called oligopeptidases A, as well as a large number of bacterial carboxypeptidases, called dipeptidyl peptidases (Dcp; Dcp II; peptidyl dipeptidase; EC 3.4.15.5). The peptidases in the M3 family contain the HEXXH motif that forms part of the active site in conjunction with a C-terminally-located Glutamic acid (Glu) residue. A single zinc ion is ligated by the side-chains of the two Histidine (His) residues, and the more C-terminal Glu. Most of the peptidases are synthesized without signal peptides or propeptides, and function intracellularly.
396149	Peptidase_M3	4.98e-41	1444	1701	168	387	Peptidase family M3. This is the Thimet oligopeptidase family, large family of mammalian and bacterial oligopeptidases that cleave medium sized peptides. The group also contains mitochondrial intermediate peptidase which is encoded by nuclear DNA but functions within the mitochondria to remove the leader sequence.
223416	Dcp	1.76e-40	1448	1701	398	618	Zn-dependent oligopeptidase [Posttranslational modification, protein turnover, chaperones].

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QKD52296.1|CBM18|GH18	0.0	147	1713	256	2367
AEO59465.1|CBM18|CBM50|GH18	4.00e-257	32	1206	43	1322
EGX53225.1|CBM18|CBM50|GH18	2.25e-255	24	1226	28	1343
QMW48046.1|CBM18|CBM50|GH18	2.29e-255	33	1206	35	1312
QRD93063.1|CBM18|CBM50|GH18	2.29e-255	33	1206	35	1312

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
2O36_A	3.63e-26	1454	1701	385	598	Chain A, Thimet oligopeptidase [Homo sapiens]
1S4B_P	4.79e-26	1454	1701	385	598	Chain P, Thimet oligopeptidase [Homo sapiens]
1HKK_A	8.13e-20	497	746	58	344	High resoultion crystal structure of human chitinase in complex with allosamidin [Homo sapiens]
1HKI_A	8.24e-20	497	746	58	344	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	1.11e-19	497	746	58	344	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]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|P09805|KTXA_KLULA	1.59e-87	120	696	50	623	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|P25375|PRTD_YEAST	1.22e-35	1443	1701	417	647	Saccharolysin OS=Saccharomyces cerevisiae (strain ATCC 204508 / S288c) OX=559292 GN=PRD1 PE=1 SV=1
sp|Q1JPJ8|THOP1_BOVIN	7.79e-29	1443	1701	392	613	Thimet oligopeptidase OS=Bos taurus OX=9913 GN=THOP1 PE=2 SV=3
sp|Q54DD2|THOPL_DICDI	2.94e-28	1456	1701	394	610	Thimet-like oligopeptidase OS=Dictyostelium discoideum OX=44689 GN=DDB_G0292362 PE=3 SV=1
sp|Q8C1A5|THOP1_MOUSE	7.36e-28	1443	1701	392	613	Thimet oligopeptidase OS=Mus musculus OX=10090 GN=Thop1 PE=1 SV=1

SignalP and Lipop Annotations

This protein is predicted as SP

Other	SP_Sec_SPI	CS Position
0.001263	0.998697	CS pos: 22-23. Pr: 0.9782

TMHMM  Annotations     

Start	End
5	27