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CAZyme Information: HMPREF1544_00063-t46_1-p1

You are here: Home > Sequence: HMPREF1544_00063-t46_1-p1

Basic Information | Genomic context | Full Sequence | Enzyme annotations |  CAZy signature domains |  CDD domains | CAZyme hits | PDB hits | Swiss-Prot hits | SignalP and Lipop annotations | TMHMM annotations

Basic Information help

Species Mucor circinelloides
Lineage Mucoromycota; Mucoromycetes; ; Mucoraceae; Mucor; Mucor circinelloides
CAZyme ID HMPREF1544_00063-t46_1-p1
CAZy Family AA1
CAZyme Description hypothetical protein
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
1930 KE123896|CGC2 217328.34 6.5078
Genome Property
Genome Version/Assembly ID Genes Strain NCBI Taxon ID Non Protein Coding Genes Protein Coding Genes
FungiDB-61_Mcircinelloides1006PhL 12410 1220926 183 12227
Gene Location

Full Sequence      Download help

Enzyme Prediction      help

EC 2.4.1.16:11

CAZyme Signature Domains help

Family Start End Evalue family coverage
GT2 1209 1715 2.5e-226 0.9924098671726755

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
276845 MYSc_Myo17 0.0 29 755 4 647
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.
367353 Chitin_synth_2 0.0 1210 1715 4 526
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).
276950 MYSc 2.08e-122 29 551 1 516
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 1.93e-121 19 758 10 677
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.
395017 Myosin_head 4.56e-97 19 676 3 602
Myosin head (motor domain).

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
0.0 23 1927 17 1892
0.0 24 1929 21 1886
0.0 23 1718 17 1690
0.0 23 1930 21 1910
0.0 23 1930 21 1910

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
5.73e-62 23 582 93 627
Crystal structure of myosin-2 dictyostelium discoideum motor domain S456Y mutant in complex with adp-orthovanadate [Dictyostelium discoideum]
7.51e-62 23 582 94 628
CRYSTAL STRUCTURE OF THE APO MOTOR DOMAIN OF DICTYOSTELLIUM MYOSIN II [Dictyostelium discoideum],1FMW_A Crystal Structure Of The Mgatp Complex For The Motor Domain Of Dictyostelium Myosin Ii [Dictyostelium discoideum]
9.62e-62 23 582 93 627
Structural basis for the allosteric interference of myosin function by mutants G680A and G680V of Dictyostelium myosin-2 [Dictyostelium discoideum]
9.62e-62 23 582 93 627
Structural basis for the allosteric interference of myosin function by mutants G680A and G680V of Dictyostelium myosin-2 [Dictyostelium discoideum],2Y8I_X Structural basis for the allosteric interference of myosin function by mutants G680A and G680V of Dictyostelium myosin-2 [Dictyostelium discoideum]
1.01e-61 23 582 94 628
Chain A, MYOSIN S1DC MOTOR DOMAIN [Dictyostelium discoideum],1D0Y_A Chain A, MYOSIN S1DC MOTOR DOMAIN [Dictyostelium discoideum],1D0Z_A Chain A, MYOSIN [Dictyostelium discoideum],1D1A_A Chain A, MYOSIN [Dictyostelium discoideum],1D1B_A Chain A, MYOSIN [Dictyostelium discoideum],1D1C_A Chain A, MYOSIN [Dictyostelium discoideum]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
0.0 23 1926 13 2002
Chitin synthase 8 OS=Ustilago maydis (strain 521 / FGSC 9021) OX=237631 GN=CHS8 PE=3 SV=1
0.0 29 1926 24 1929
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
8.90e-287 860 1734 45 911
Chitin synthase 6 OS=Ustilago maydis (strain 521 / FGSC 9021) OX=237631 GN=CHS6 PE=3 SV=2
5.41e-267 882 1714 160 989
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
1.53e-136 1234 1715 686 1183
Chitin synthase 4 OS=Magnaporthe oryzae (strain 70-15 / ATCC MYA-4617 / FGSC 8958) OX=242507 GN=CHS4 PE=3 SV=2

SignalP and Lipop Annotations help

This protein is predicted as OTHER

Other SP_Sec_SPI CS Position
1.000057 0.000001

TMHMM  Annotations      download full data without filtering help

Start End
888 910
923 942
1194 1216
1586 1608
1618 1640
1647 1669