CAZyme Information: PTTG_02136-t43_1-p1

Basic Information

• Species: Puccinia triticina
• Lineage: Basidiomycota; Pucciniomycetes; ; Pucciniaceae; Puccinia; Puccinia triticina
• CAZyme ID: PTTG_02136-t43_1-p1
• CAZy Family: GH105
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
2370	ADAS02000022.1|CGC1	259868.03	6.0590

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_Ptriticina1-1BBBDRace1	15692	630390	814	14878

• Gene Location: location=ADAS02000022.1:780541-788568(+)

Full Sequence      

MAEEKMMDDQTAQKKTSIGDDDDDDGDGPLDVELSNSALLLVDIQHDFVSDEGALAVGSA
GEILATVYGLLDDEELGWKAVDFHPPGHISFASTHQAQPFTQLTTDLAGRSDGEPGGSSL
EVQTRTIDLWPDHCVQGTKGSELDGGIQERLERLKSEGRTVKVIHKGIHPDVENYSAFLD
DGADRLDEFLGSLGVRNVFVAGLAGDFCVKACCESALQAGLRVFWIRDGIRSVGGGSVQM
GVECALAGAAAVQGGSFRVVRGGAGAMEPTRLSQLTTPDSQEILSILHARHRAELHDILI
GHSILLHINPLRPTQDTSDHSAHAYLNNTSNALPPHLYQLAADVSYALKRTAKTQAIVYS
GFSGSGKTTSMKLITNQLIRLSQLNSLGPSSQSSQALKLTDQIPHLFTLLSAFSNAKTFQ
NPSASRLSSLLELHFDNLFHLAGAKLLVFGLERNRLRIPLKSSHDRTFDVFYQLLAGIPA
DQRTQLALHPDPSHYDLLASSSCYRTPDRPDADRIGFDELQAALKSLAFKPKHIHSLFKL
LSAILLLGNIQFELSQSRDFQDQSASVSNPETLELVAELLGLPSPDLARVLTNRIQYIRK
ETVTVLLRPEAAVQQRDDFTNALYGVLVAYVVETANHKLFPGDGFINELQAQGGSSILQF
DSPGPQGRSEELADMLGSGNNLPTRRQSIKKLERSNTLLGRAKSFGASAYEEFCINYQTE
LIHTWFSHQHLDQQSSRAAADGIQIPKIDSQDFSSSRLEMLRGGLLGGKADSKPGGIIGG
LAKTSNSQRKGKYNTMEEADNDVLDGMRSHFASHPSFISRPSHSTSQSVFGIQHWSGPVS
YDATGIIQADLGLVDVEFVSLLRNSTDSFVSRLLSGPSLALDRHPLDPSVLVAAQVSSSP
LRRPSPILPTHPHISLEPGSPRGAPLDSTVALIDTSVVQPTLSQLNATLSQFISHFSQCQ
VWHVLNLKPNDELYANDWDPVRVEHQLEAFRIPDLITCKQVDYPFDFDLTMFSIRFRLEG
TEASDLRRQLTTALGLEENKDFAIGRSRVWLTLPAFQSLEERLLADHPAGSQPRPIAGHL
AGVDIPGGSPRELDSWGDLGGGGSGSYQHLVTGGSGSGDDRPHSGYEAERNIPQSPGFGG
ETELPHGGSYQDGPAQSRVWGSEWESKQPEEQVMLNKEARYMDVGLIKHNQIDGNTNRDG
ATDDVLLKTDQNQTLEEVESSRGRMWWVVIVWSLTFYIPNFFLSTMGRMKRPDIQMAWRE
KVALCLIIFLMCGAVLFVILGLGKIMCPNLAKAWTPTELGYHATESDFYVGVRGQVFDLG
KFWKGQHSDITAQPVTNSDMLSLAGQDLTNYFPVPLRLACPNVQVDTVNIQFENWTATVP
NAVHVSGSAQVVKSSALGNDKWYTEKFLPFMTNFYKGPIVYGHKLISGLANNRSIGIYDG
GVYDLSDYFYTYNTQNRNPQFQYIDKSISDLFQQQPGQDITKEVNALPLGDAEKSASLAC
LRNMFYLGDTDFREGPRCTVANYILLAFTILIAAAVFAKFIAALQLGTKRMPELRDKFVI
CQVPCYTEGEESLRKTIDSLATLKYDDKRKLIFVICDGMIIGSGNDQPTPRIVLDLLGVD
PAIDPDPLLFQSVSEGSKQLNYGKVYSGLYEVDGHVVPYVVVVKVGKPSERSKPGNRGKR
DSQILLMRFLNRIHFDAPMCPLELEICHQIKNVIGVEPQLYEFLFTIDADTEVYPDALNR
LVSAASDDGRIIGICGETKLSNEKVSWWTMIQVYEYYISHHLSKAFESLFGSVTCLPGCF
TLYRIRSADKGRPLVVSNLIIDEYAEIHVDTLHKKNLFSLGEDRFFTTLLMKHFPHYKTK
FIPDATAMTAAPETWAVLLSQRRRWINSTIHNLGELMFLEDMCGFCCFSMRFFVMLDLVG
TVILPSTTVYIIYLIVIVSTKQAAIPIVSLVIIAAVYGLQVVIFLLKREWGLIFWLLIYL
LAYPIWSFFLPIYSFWHFDDFSWGNTRMVVGEGKNKKVLADTDDVGFDPSVIPLRKFSDY
QAAMWDEDGKSSRAGGGYGRRPESVGGFSMASRPMGAMGMMGAGGSVMGGGGMEGGGDYY
RDGHPRSTMYRSSGMNLAAPGSYNRSDSRSPSQRGSMMAGPNRLAPLNDFGGFQPGLNQH
QSMISLAGIRAAQQQQAAAMSVFNGAGPHGPGSVRGSMMDFANSGAATPGMFMSPGYPSM
MPMGGSGTGDMQHAHNMSMFGMPGAAGGIMPGNPSMMMGGTPSMMMMNPMGGGPGGGAMM
GYNPLGNPGAVAGAPQQQVASQPLVQNFSADPSDDQVVETLRIYLSQQDLMKITKRSVRD
ALNHWFPNANLNEKKAFINAQIDKILAGNN

Enzyme Prediction     

EC	2.4.1.16:11

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GT2	1535	2041	2.6e-236	0.9905123339658444

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
367353	Chitin_synth_2	0.0	1536	2041	4	525	Chitin synthase. Members of this family are fungal chitin synthase EC:2.4.1.16 enzymes. They catalyze chitin synthesis as follows: UDP-N-acetyl-D-glucosamine + {(1,4)-(N-acetyl-beta-D-glucosaminyl)}(N) <=> UDP + {(1,4)-(N-acetyl-beta-D-glucosaminyl)}(N+1).
276845	MYSc_Myo17	1.05e-179	283	1060	6	646	class XVII myosin, motor domain. This fungal myosin which is also known as chitin synthase uses its motor domain to tether its vesicular cargo to peripheral actin. It works in opposition to dynein, contributing to the retention of Mcs1 vesicles at the site of cell growth and increasing vesicle fusion necessary for polarized growth. Class 17 myosins consist of a N-terminal myosin motor domain with Cyt-b5, chitin synthase 2, and a DEK_C domains at it C-terminus. The chitin synthase region contains several transmembrane domains by which myosin 17 is thought to bind secretory vesicles. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
276950	MYSc	2.22e-92	283	1051	3	632	Myosin motor domain superfamily. Myosin motor domain. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
214580	MYSc	6.99e-80	272	1062	11	675	Myosin. Large ATPases. ATPase; molecular motor. Muscle contraction consists of a cyclical interaction between myosin and actin. The core of the myosin structure is similar in fold to that of kinesin.
133033	Chitin_synth_C	4.48e-76	1560	1892	1	244	C-terminal domain of Chitin Synthase catalyzes the incorporation of GlcNAc from substrate UDP-GlcNAc into chitin. Chitin synthase, also called UDP-N-acetyl-D-glucosamine:chitin 4-beta-N-acetylglucosaminyltransferase, catalyzes the incorporation of GlcNAc from substrate UDP-GlcNAc into chitin, which is a linear homopolymer of GlcNAc residues formed by covalent beta-1,4 linkages. Chitin is an important component of the cell wall of fungi and bacteria and it is synthesized on the cytoplasmic surface of the cell membrane by membrane bound chitin synthases. Studies with fungi have revealed that most of them contain more than one chitin synthase gene. At least five subclasses of chitin synthases have been identified.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
CDR37062.1|GT2	0.0	269	2367	18	2059
UOP56890.1|GT2	0.0	277	2368	27	2026
CDZ98697.1|GT2	0.0	278	2368	29	1990
QDK64620.1|GT2	0.0	278	2367	21	1970
AZQ26804.1|GT2	0.0	278	2367	21	1970

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
5I0H_A	1.71e-42	266	1062	56	737	Crystal structure of myosin X motor domain in pre-powerstroke state [Homo sapiens],5I0H_B Crystal structure of myosin X motor domain in pre-powerstroke state [Homo sapiens]
5I0I_A	2.64e-42	266	1062	54	735	Crystal structure of myosin X motor domain with 2IQ motifs in pre-powerstroke state [Homo sapiens],5I0I_B Crystal structure of myosin X motor domain with 2IQ motifs in pre-powerstroke state [Homo sapiens]
5KG8_A	1.25e-41	266	1062	54	735	Rigor myosin X co-complexed with an actin filament [Homo sapiens]
1LVK_A	1.28e-36	272	913	91	651	X-Ray Crystal Structure Of The Mg (Dot) 2'(3')-O-(N- Methylanthraniloyl) Nucleotide Bound To Dictyostelium Discoideum Myosin Motor Domain [Dictyostelium discoideum]
1MMD_A	1.70e-36	272	913	91	651	Truncated Head Of Myosin From Dictyostelium Discoideum Complexed With Mgadp-Bef3 [Dictyostelium discoideum],1MND_A Truncated Head Of Myosin From Dictyostelium Discoideum Complexed With Mgadp-Alf4 [Dictyostelium discoideum],1MNE_A Truncated Head Of Myosin From Dictyostelium Discoideum Complexed With Mg-Pyrophosphate [Dictyostelium discoideum],1VOM_A Complex Between Dictyostelium Myosin And Mgadp And Vanadate At 1.9a Resolution [Dictyostelium discoideum]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|J9VF17|CHS4_CRYNH	0.0	1199	2367	138	1269	Chitin synthase 4 OS=Cryptococcus neoformans var. grubii serotype A (strain H99 / ATCC 208821 / CBS 10515 / FGSC 9487) OX=235443 GN=CHS4 PE=2 SV=2
sp|Q4P9K9|CHS8_USTMA	0.0	268	2367	6	2003	Chitin synthase 8 OS=Ustilago maydis (strain 521 / FGSC 9021) OX=237631 GN=CHS8 PE=3 SV=1
sp|O13395|CHS6_USTMA	0.0	1215	2368	61	1176	Chitin synthase 6 OS=Ustilago maydis (strain 521 / FGSC 9021) OX=237631 GN=CHS6 PE=3 SV=2
sp|J9VNT4|CHS5_CRYNH	0.0	335	2048	96	1742	Chitin synthase 5 OS=Cryptococcus neoformans var. grubii serotype A (strain H99 / ATCC 208821 / CBS 10515 / FGSC 9487) OX=235443 GN=CHS5 PE=2 SV=1
sp|O13356|CHS1_CRYNH	1.38e-139	1226	2041	74	954	Chitin synthase 1 OS=Cryptococcus neoformans var. grubii serotype A (strain H99 / ATCC 208821 / CBS 10515 / FGSC 9487) OX=235443 GN=CHS1 PE=2 SV=2

SignalP and Lipop Annotations

This protein is predicted as OTHER

Other	SP_Sec_SPI	CS Position
1.000043	0.000001

TMHMM  Annotations     

Start	End
1225	1244
1264	1283
1519	1541
1912	1934
1944	1966
1973	1995