CAZyme Information: TPX38635.1

Basic Information

• Species: Synchytrium endobioticum
• Lineage: Chytridiomycota; Chytridiomycetes; ; Synchytriaceae; Synchytrium; Synchytrium endobioticum
• CAZyme ID: TPX38635.1
• CAZy Family: CE4
• CAZyme Description: unspecified product

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
1052		115456.48	6.6958

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_SendobioticumMB42	8031	N/A	0	8031

• Gene Location: location=QEAN01000386:13703-19303(+)

Full Sequence      

MQTQIAFASVHVIGRTPIGDPRVTENVEYLAELAVLCAALSLTHHTIFPMQPSKAIPQST
QMLFLPSFTNAQRTYLLSTSIALLYTPKNEHFGIVPLEAMISSCIVIASNSGGPKETVVN
NVTGYLVDDTIDGFGGAMLKVLNDLREEKRKDMGRLGRERVHEFFSLDRFKMQLEIVIQS
IMEGKWIHRYRAMSASLFLETLRRADLDNYYTNFAQSGINSLESLANLTMQDYSSVGIIS
MEDRKRLFQLIQTLKTDLPTPSTEPRLAQPLNITKPSVMTTQRIPVQSSASSTTPYSTAP
VPFSNSAPSRRTTFAFDPPPHDSSQMELNISPAQSSKSLSDGEDNGNNVNAILTMEAAAK
ARKASRRQSLGSSPPKKPAQPLLNAYGIPVASTVRNASNSSWSRTGAARSSVSDLDARIR
VCVRKRPLSRKEKANGQVDVAPVTGRRSIGIHEPKVKVDLTKYVEQHQFTFDEVFDADTT
NEEVYKRTAQPLVEYIFGGGKATCFAYGQTGSGKTHTMLDEEKGLYVLAARDIFALLKQQ
QYQNLSAYASFYEIYQGHLYDLLNERKKLFAREDGKQQVQITGLQEFEVDNVDKLMKVFE
FGNTARSTGATGANADSSRSHAIFQIVLKHKNKKRTMQGKFSFIDLAGSERGADRGDADK
QTRMEGSEINKSLLALKECIRALDQESKHTPFRQSKLTQVLKDSFIGDSKTCMIATISPN
IGNSEHSLNTLRYADRVKELKSDGREDFDEDDDQDLLEGEVYDDDEDGMKDDDDDFLLDS
EYPPDNLVLSDVEGNDHQEPPRVIPSNSNVNTSSAIISRDDEKPPRATNRLSTAVATPPA
VVKEQKSNILSQLNSLVGRVAGGGSNSSPRPNSQSYSQGNVSTPVNNARNNSMSNISGSV
GQSSSVSANTPSSSCSTTARSAPPIAKTPSSVSQDGIVADSMPSTVTTNNISGSVQKSDA
TSAPVDFEGLIRLHRQHIREFTELGKLESRLLVNATMKMGRPAEPLSYSSNTSSGSITMP
SESYMKELDSLLDRKLDAIVSLQNSIRALSSL

Enzyme Prediction     

EC	2.4.1.257:6	2.4.1.132:6

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GT4	60	148	1e-18	0.55625

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
276818	KISc_KIF2_like	8.18e-174	418	738	1	328	Kinesin motor domain, KIF2-like group. Kinesin motor domain, KIF2-like group. KIF2 is a protein expressed in neurons, which has been associated with axonal transport and neuron development; alternative splice forms have been implicated in lysosomal translocation. This catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Kinesins are microtubule-dependent molecular motors that play important roles in intracellular transport and in cell division. In this subgroup the motor domain is found in the middle (M-type) of the protein chain. M-type kinesins are (+) end-directed motors, i.e. they transport cargo towards the (+) end of the microtubule. Kinesin motor domains hydrolyze ATP at a rate of about 80 per second, and move along the microtubule at a speed of about 6400 Angstroms per second (KIF2 may be slower). To achieve that, kinesin head groups work in pairs. Upon replacing ADP with ATP, a kinesin motor domain increases its affinity for microtubule binding and locks in place. Also, the neck linker binds to the motor domain, which repositions the other head domain through the coiled-coil domain close to a second tubulin dimer, about 80 Angstroms along the microtubule. Meanwhile, ATP hydrolysis takes place, and when the second head domain binds to the microtubule, the first domain again replaces ADP with ATP, triggering a conformational change that pulls the first domain forward.
395169	Kinesin	3.47e-129	424	739	1	325	Kinesin motor domain.
214526	KISc	4.21e-119	418	741	1	329	Kinesin motor, catalytic domain. ATPase. Microtubule-dependent molecular motors that play important roles in intracellular transport of organelles and in cell division.
276812	KISc	3.46e-115	418	738	1	326	Kinesin motor domain. Kinesin motor domain. This catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Kinesins are microtubule-dependent molecular motors that play important roles in intracellular transport and in cell division. In most kinesins, the motor domain is found at the N-terminus (N-type), in some its is found in the middle (M-type), or C-terminal (C-type). N-type and M-type kinesins are (+) end-directed motors, while C-type kinesins are (-) end-directed motors, i.e. they transport cargo towards the (-) end of the microtubule. Kinesin motor domains hydrolyze ATP at a rate of about 80 per second, and move along the microtubule at a speed of about 6400 Angstroms per second. To achieve that, kinesin head groups work in pairs. Upon replacing ADP with ATP, a kinesin motor domain increases its affinity for microtubule binding and locks in place. Also, the neck linker binds to the motor domain, which repositions the other head domain through the coiled-coil domain close to a second tubulin dimer, about 80 Angstroms along the microtubule. Meanwhile, ATP hydrolysis takes place, and when the second head domain binds to the microtubule, the first domain again replaces ADP with ATP, triggering a conformational change that pulls the first domain forward.
276821	KISc_KIP3_like	6.25e-89	418	740	1	345	Kinesin motor domain, KIP3-like subgroup. Kinesin motor domain, KIP3-like subgroup. The yeast kinesin KIP3 plays a role in positioning the mitotic spindle. This catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Kinesins are microtubule-dependent molecular motors that play important roles in intracellular transport and in cell division. In most kinesins, the motor domain is found at the N-terminus (N-type). N-type kinesins are (+) end-directed motors, i.e. they transport cargo towards the (+) end of the microtubule. Kinesin motor domains hydrolyze ATP at a rate of about 80 per second, and move along the microtubule at a speed of about 6400 Angstroms per second. To achieve that, kinesin head groups work in pairs. Upon replacing ADP with ATP, a kinesin motor domain increases its affinity for microtubule binding and locks in place. Also, the neck linker binds to the motor domain, which repositions the other head domain through the coiled-coil domain close to a second tubulin dimer, about 80 Angstroms along the microtubule. Meanwhile, ATP hydrolysis takes place, and when the second head domain binds to the microtubule, the first domain again replaces ADP with ATP, triggering a conformational change that pulls the first domain forward.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
CAG1855277.1|CBM57	1.03e-40	412	741	431	764
VDC88467.1|CBM0	7.02e-39	414	741	505	836
CAG7893381.1|CBM0	7.05e-39	414	741	508	839
QWT43334.1|CBM57	2.67e-38	414	741	448	779
CAA7387648.1|CBM0	4.39e-38	412	738	253	579

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
2HEH_A	4.37e-123	418	740	52	382	Crystal Structure of the KIF2C motor domain [Homo sapiens],4UBF_A HsMCAK motor domain complex,4UBF_B HsMCAK motor domain complex,4UBF_C HsMCAK motor domain complex,4UBF_D HsMCAK motor domain complex
2GRY_A	1.39e-121	418	740	90	420	Crystal structure of the human KIF2 motor domain in complex with ADP [Homo sapiens],6BBN_E Crystal structure of a curved tubulin complex induced by the kinesin-13 Kif2A [Homo sapiens]
3EDL_D	3.99e-121	419	740	1	330	Kinesin13-Microtubule Ring complex [Drosophila melanogaster]
3J2U_K	4.46e-121	419	740	38	369	Kinesin-13 KLP10A HD in complex with CS-tubulin and a microtubule [Drosophila melanogaster],6B0C_K KLP10A-AMPPNP in complex with curved tubulin and a microtubule [Drosophila melanogaster]
6B0I_K	5.18e-121	416	740	80	414	Apo KLP10A in complex with a microtubule [Drosophila melanogaster],6B0L_K KLP10A-AMPPNP in complex with a microtubule [Drosophila melanogaster]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|Q6NWW5|KIF24_MOUSE	9.26e-128	195	741	2	542	Kinesin-like protein KIF24 OS=Mus musculus OX=10090 GN=Kif24 PE=1 SV=2
sp|Q5T7B8|KIF24_HUMAN	2.54e-123	195	741	2	547	Kinesin-like protein KIF24 OS=Homo sapiens OX=9606 GN=KIF24 PE=1 SV=2
sp|Q5ZKV8|KIF2A_CHICK	2.67e-118	418	743	223	556	Kinesin-like protein KIF2A OS=Gallus gallus OX=9031 GN=KIF2A PE=2 SV=2
sp|Q95LP1|KIF2C_MACFA	2.78e-118	418	740	204	534	Kinesin-like protein KIF2C OS=Macaca fascicularis OX=9541 GN=KIF2C PE=2 SV=1
sp|Q99661|KIF2C_HUMAN	6.23e-118	418	740	258	588	Kinesin-like protein KIF2C OS=Homo sapiens OX=9606 GN=KIF2C PE=1 SV=2

SignalP and Lipop Annotations

This protein is predicted as OTHER

Other	SP_Sec_SPI	CS Position
0.999304	0.000705

TMHMM  Annotations     

There is no transmembrane helices in TPX38635.1.