CAZyme Information: KFA53960.1

Basic Information

• Species: Stachybotrys chartarum
• Lineage: Ascomycota; Sordariomycetes; ; Stachybotryaceae; Stachybotrys; Stachybotrys chartarum
• CAZyme ID: KFA53960.1
• CAZy Family: GH5
• CAZyme Description: unspecified product

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
2252		243506.93	5.3772

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_SchartarumIBT40293	11453	1280524	0	11453

Full Sequence      

MTGLGFSTAAAYPGFGALNGYWGQFGSESLRQYCDTGIEYVTLSFVNQAPEHSASNYPGT
NFAGHCWANTYTAPNGASSKLLSECRTIKNDIPYCREKGVKVLLSIGGEYSEEYSNYRVT
STANGEYFANFLYKAFGPYDPSWTGPRPFDLDANTHTQVDGFDFDIEADFDNEPYIRMAE
KFRELDSSMFLTAAPQCPTLDPYFHLKDLIQRAPLDALFVQFYNNAVCDAIRDPGLAGDG
FNYNAWANLLAQSDKSKNAKLFIGLLASPAASLTGSGFISAQAMKDLVCQYKDSPSFGGI
SLWDLTRGAAEISNGKNYYQHALDALKYGCAPVPTSTSRAITSTTSTRTSTSTSTRQPTT
TTTTIRSSSSSSVLTSTSTTSSSIRPTTTSTTVRSSSTTSPSSTLISTTSARTSTVTSSS
SSSSSSSSSSSSSISSSSTSSSSSSSSIMSSSSSSSSTSSSSSSSSSSTTTTSSGIIIET
PSVSDTSLISDVFTSVTSAASTSTLSASSSMTTTSSGIIIETPSVSDTSLISDVFTSVTS
AASTTSAETVSASVSSAVSVPTTTTVVTSLPVSFTSTRTWSNSTMTTSSAPGTSDVSVSA
PTTTTVMTSLPGSLTSTRSWSNTTFTTSDAGSLTTRVASLTTSAVSLTTSTVYTTKVQTV
TKCPPYVVDCPEGGYVTTVTVPWYTTVCPVTETPKPTGALTTSTVYATKVYTVTKCPPGV
ANCPTGHATTETVPVYTTVCPVGETVTVPLTTSTAYTTATYTITACPEGVVDCPTGHMTT
VTEPAYTTIGPIEETSVVPEPTGDAETQTYTLTYPHGGAETSTVVVPGGGDAESSTRPGV
AVPTDQWVNPIPSGTPGLPDVPNVPASAPSLAVGLGGLLALVAVQVFALFSDCVFDFHIS
GLLDAKNPDSLHKIACFEMRLFSGVVKLQLSKALVQRIAVHEEIRNFREESHCQASLFQD
LEQPEDQTKALMQKWTTCQDLGNAAPEPIKKLALGKHWTPPLFDIEMSRTLANHLAICPV
SNTSQHKRSKSAAALALLRRKDTREDDSGSEDARSAQPPSSASKPGNSSMAHKSSARSSN
SKLTTGSALSRAPSHQPSPAAKPTPAPDRGVTLEQSVKKFRIVEALRNGDTAYISRAIRD
TAENGPRTSISSIATTSASAALEDTTLLHLAIQCAEFPVIEYVLSDGLGSIDFNARDKDG
NTPLHVAATQGRAPVVKLLLEQKDINDAISNSQGKLPIDLARNPEIFQLLQLSRSLFTEA
KIDQVQGLIASRKYDTLAEVLEESRVKTVLDINSPEFASEPVTVQTGGTLLHEAVRKRDT
KLIEVLLLHGADPFCRDRKGKLPQSITSDDNIKSILKKSPAAVAAQRGIQEKAVLGHAAS
QGAATTDPLAGREAREMKGYLKKWTNYRKGYQLRWFVLEDGVLSYYKHQDDSGSACRGAI
NMRIAQLHMTADEKTKFEIIGKSSVKYTLKANHEVEAKRWFWALNNSIQWTKDQIKEEQR
QAARSAEMLKTAKAEQSGSLSLQESHSESASLSDLRRNSSHYGSRSIGGKGPTQKPEFGT
STVGSIDEDDEFADAATDAGASRAGHGHLIPGDPDDDDDDYGDGSLMEQPSATKDALNIT
AQSAKLQLETMSHVHNALMGELTQSPSTPLSDTKVTQALSTYDAAIRSLTGLVGDLLRIS
KDRDAYWQYRLDRESNMRRMWEESMAKVAREHEVLEARVGQAELKRKQTKRALREVMESG
FTATDVPDSQPGVAEDEDGQSRSPTVARRATIGQIVDLSESESEDEEEFFDAVDAGEVEV
SVMPPEDGAKQEADIVVTGGIDLSSSFKGYENGIRHRLKMDADDRPKISLWGILKSMIGK
DMTRMTLPVSFNEPTSLLYRCGEDMEYVDLLDLAAERTDSIERLIYVAAFAASEYASTID
RVAKPFNPLLGETFEYVRPDKNYRFFIEQVSHHPPIGAAWAESPHWTYWGESHVKSKFYG
KSFDINPLGTWFLKLRPKAGGKEDLYTWKKVTSSVVGIITGNPTVDNYGLMEIKNWTTGE
VAQLDFKPRGWKASSAYQISGKVMDETGRVRVSMGGRWNSKLYARLTPGYEAALDEPAKD
SGPVHRGNITDPTRAYLVWQANPRPAGIPFNLTPFVLTFNHIDEKLRPWIAPTDSRLRPD
QRAMEDGEYDFAATEKNRLEQNQRARRQDRDARGEAFVPAWFYKTRCEITGEEYWQFNGK
YWEQREKAGPNGDADAWAGLEPIYEDYEAKNE

Enzyme Prediction     

No EC number prediction in KFA53960.1.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH18	19	276	2.5e-18	0.6722972972972973

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
395990	Oxysterol_BP	0.0	1849	2223	1	362	Oxysterol-binding protein.
119356	GH18_hevamine_XipI_class_III	4.29e-92	16	324	1	280	This conserved domain family includes xylanase inhibitor Xip-I, and the class III plant chitinases such as hevamine, concanavalin B, and PPL2, all of which have a glycosyl hydrolase family 18 (GH18) domain. Hevamine is a class III endochitinase that hydrolyzes the linear polysaccharide chains of chitin and peptidoglycan and is important for defense against pathogenic bacteria and fungi. PPL2 (Parkia platycephala lectin 2) is a class III chitinase from Parkia platycephala seeds that hydrolyzes beta(1-4) glycosidic bonds linking 2-acetoamido-2-deoxy-beta-D-glucopyranose units in chitin.
241446	PH_Osh1p_Osh2p_yeast	1.34e-58	1394	1494	1	103	Yeast oxysterol binding protein homologs 1 and 2 Pleckstrin homology (PH) domain. Yeast Osh1p is proposed to function in postsynthetic sterol regulation, piecemeal microautophagy of the nucleus, and cell polarity establishment. Yeast Osh2p is proposed to function in sterol metabolism and cell polarity establishment. Both Osh1p and Osh2p contain 3 N-terminal ankyrin repeats, a PH domain, a FFAT motif (two phenylalanines in an acidic tract), and a C-terminal OSBP-related domain. OSBP andOsh1p PH domains specifically localize to the Golgi apparatus in a PtdIns4P-dependent manner. Oxysterol binding proteins are a multigene family that is conserved in yeast, flies, worms, mammals and plants. In general OSBPs and ORPs have been found to be involved in the transport and metabolism of cholesterol and related lipids in eukaryotes. They all contain a C-terminal oxysterol binding domain, and most contain an N-terminal PH domain. OSBP PH domains bind to membrane phosphoinositides and thus likely play an important role in intracellular targeting. They are members of the oxysterol binding protein (OSBP) family which includes OSBP, OSBP-related proteins (ORP), Goodpasture antigen binding protein (GPBP), and Four phosphate adaptor protein 1 (FAPP1). They have a wide range of purported functions including sterol transport, cell cycle control, pollen development and vessicle transport from Golgi recognize both PI lipids and ARF proteins. PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes.
270101	PH_OSBP_ORP4	5.97e-28	1397	1489	1	91	Human Oxysterol binding protein and OSBP-related protein 4 Pleckstrin homology (PH) domain. Human OSBP is proposed to function is sterol-dependent regulation of ERK dephosphorylation and sphingomyelin synthesis as well as modulation of insulin signaling and hepatic lipogenesis. It contains a N-terminal PH domain, a FFAT motif (two phenylalanines in an acidic tract), and a C-terminal OSBP-related domain. OSBPs and Osh1p PH domains specifically localize to the Golgi apparatus in a PtdIns4P-dependent manner. ORP4 is proposed to function in Vimentin-dependent sterol transport and/or signaling. Human ORP4 has 2 forms, a long (ORP4L) and a short (ORP4S). ORP4L contains a N-terminal PH domain, a FFAT motif (two phenylalanines in an acidic tract), and a C-terminal OSBP-related domain. ORP4S is truncated and contains only an OSBP-related domain. Oxysterol binding proteins are a multigene family that is conserved in yeast, flies, worms, mammals and plants. They all contain a C-terminal oxysterol binding domain, and most contain an N-terminal PH domain. OSBP PH domains bind to membrane phosphoinositides and thus likely play an important role in intracellular targeting. They are members of the oxysterol binding protein (OSBP) family which includes OSBP, OSBP-related proteins (ORP), Goodpasture antigen binding protein (GPBP), and Four phosphate adaptor protein 1 (FAPP1). They have a wide range of purported functions including sterol transport, cell cycle control, pollen development and vessicle transport from Golgi recognize both PI lipids and ARF proteins. PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes.
269951	PH_FAPP1_FAPP2	2.43e-23	1397	1487	1	91	Four phosphate adaptor protein 1 and 2 Pleckstrin homology (PH) domain. Human FAPP1 (also called PLEKHA3/Pleckstrin homology domain-containing, family A member 3) regulates secretory transport from the trans-Golgi network to the plasma membrane. It is recruited through binding of PH domain to phosphatidylinositol 4-phosphate (PtdIns(4)P) and a small GTPase ADP-ribosylation factor 1 (ARF1). These two binding sites have little overlap the FAPP1 PH domain to associate with both ligands simultaneously and independently. FAPP1 has a N-terminal PH domain followed by a short proline-rich region. FAPP1 is a member of the oxysterol binding protein (OSBP) family which includes OSBP, OSBP-related proteins (ORP), and Goodpasture antigen binding protein (GPBP). They have a wide range of purported functions including sterol transport, cell cycle control, pollen development and vessicle transport from Golgi recognize both PI lipids and ARF proteins. FAPP2 (also called PLEKHA8/Pleckstrin homology domain-containing, family A member 8), a member of the Glycolipid lipid transfer protein(GLTP) family has an N-terminal PH domain that targets the TGN and C-terminal GLTP domain. FAPP2 functions to traffic glucosylceramide (GlcCer) which is made in the Golgi. It's interaction with vesicle-associated membrane protein-associated protein (VAP) could be a means of regulation. Some FAPP2s share the FFAT-like motifs found in GLTP. PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QKD55908.1|GH18	QKD55908.1|GH18	0.0	18	2246	16	2188
CCT69979.1|GH18	CCT69979.1|GH18	4.43e-122	18	336	16	334
QGI96702.1|GH18	QGI96702.1|GH18	4.43e-122	18	336	16	334
QGI65821.1|GH18	QGI65821.1|GH18	4.43e-122	18	336	16	334
QGI83062.1|GH18	QGI83062.1|GH18	2.04e-121	18	336	16	334

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
5H2D_A	5H2D_A	1.83e-141	1826	2233	21	433	Crystal structure of Osh1 ORD domain in complex with ergosterol [Kluyveromyces lactis NRRL Y-1140],5WVR_A Crystal structure of Osh1 ORD domain in complex with cholesterol [Kluyveromyces lactis NRRL Y-1140]
7DEI_A	7DEI_A	2.85e-74	1824	2229	2	378	Chain A, Oxysterol-binding protein-related protein 3 [Homo sapiens],7DEI_B Chain B, Oxysterol-binding protein-related protein 3 [Homo sapiens],7DEJ_A Chain A, Oxysterol-binding protein-related protein 3 [Homo sapiens],7DEJ_B Chain B, Oxysterol-binding protein-related protein 3 [Homo sapiens]
7CYZ_A	7CYZ_A	9.55e-74	1848	2229	16	367	The structure of human ORP3 OSBP-related domain [Homo sapiens],7CYZ_B The structure of human ORP3 OSBP-related domain [Homo sapiens]
5ZM6_A	5ZM6_A	9.82e-73	1832	2224	6	419	Crystal structure of ORP1-ORD in complex with PI(4,5)P2 [Homo sapiens],5ZM6_B Crystal structure of ORP1-ORD in complex with PI(4,5)P2 [Homo sapiens],5ZM7_A Crystal structure of ORP1-ORD in complex with cholesterol at 3.4 A resolution [Homo sapiens]
5ZM5_A	5ZM5_A	1.37e-72	1845	2224	12	409	Crystal structure of human ORP1-ORD in complex with cholesterol at 2.6 A resolution [Homo sapiens]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|P35845|OSH1_YEAST	sp|P35845|OSH1_YEAST	8.82e-192	1167	2225	55	1176	Oxysterol-binding protein homolog 1 OS=Saccharomyces cerevisiae (strain ATCC 204508 / S288c) OX=559292 GN=SWH1 PE=1 SV=4
sp|Q12451|OSH2_YEAST	sp|Q12451|OSH2_YEAST	2.07e-179	1167	2225	59	1271	Oxysterol-binding protein homolog 2 OS=Saccharomyces cerevisiae (strain ATCC 204508 / S288c) OX=559292 GN=OSH2 PE=1 SV=1
sp|O14340|YB35_SCHPO	sp|O14340|YB35_SCHPO	1.15e-175	1113	2244	22	1310	Oxysterol-binding protein homolog C2F12.05c OS=Schizosaccharomyces pombe (strain 972 / ATCC 24843) OX=284812 GN=SPBC2F12.05c PE=1 SV=2
sp|Q3B7Z2|OSBP1_MOUSE	sp|Q3B7Z2|OSBP1_MOUSE	8.49e-87	1394	2227	88	795	Oxysterol-binding protein 1 OS=Mus musculus OX=10090 GN=Osbp PE=1 SV=3
sp|P22059|OSBP1_HUMAN	sp|P22059|OSBP1_HUMAN	2.39e-85	1394	2227	90	797	Oxysterol-binding protein 1 OS=Homo sapiens OX=9606 GN=OSBP PE=1 SV=1

SignalP and Lipop Annotations

This protein is predicted as OTHER

Other	SP_Sec_SPI	CS Position
0.859363	0.140655

TMHMM  Annotations     

There is no transmembrane helices in KFA53960.1.