CAZyme Information: HMPREF1544_02982-t46_1-p1

Basic Information

• Species: Mucor circinelloides
• Lineage: Mucoromycota; Mucoromycetes; ; Mucoraceae; Mucor; Mucor circinelloides
• CAZyme ID: HMPREF1544_02982-t46_1-p1
• CAZy Family: GH125
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
1907		216779.10	6.6078

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: location=KE123924:63438-69603(+)

Full Sequence      

MSSTVSNIVQLVEIQSNDTNVTGQEAIVRLLQSRFKVDQPYTQLGDHRLVVVNPFKPLDL
LNDATLQAYGQHGYKGISPDRFAPPEPHVYDMATRVYLLMRRRSENQAVILSGVTGSGKS
TTHHHLIKELLYLSTHTRKEEKMQSQILGVHTIFESFGSAASNTNETASCLGQFQTLQFN
ERGRIIGCNTSIFLLDKHRISRSHTQQYNIFYQLLAGTTPDEKQALHMTHTNFNYLKQLN
QRNTQRDQIGFSDIKAALKVCGFKTKTVAQMCQLLAAILHLGNVQFVDSNKHFVGGHESC
RIKNKEILTLVAAALGVATSKLETTLTHKLKLIGNEFCSAFLTTDTASQQRDALAHTLYS
VLVLWIMNALNQKLDVAANSSSTMMRTISILDTTGFQLSTSTTQRGCTFHDLCVNYTVEQ
LHKYTLDRTLFPDSPTNAACRQDGIWPNRIPMQIRSTPSPLALFHGTNKNSFALIPFMNK
ESKRFQTYALDATDSNLLSVLFQKKRSSQNNSNNDYTTLLNPSTPSYSFAIRHFDDAVSV
DYSIDGFLESNLDSISPDFIHLFKYNCTNAFVHDLFGANSLAGWITDIHPRDERTVIKAQ
LPVWPSLKTTDSSKKATAEETKPEAKSVAALPPPASKIQSVFDQVVQGVESLKQILNTMC
LSEIMHIRPNDQQKPDVFDPVFVQRQIQALRMTELAVHAVHVDVLYPYTQRKFMSRYKHL
MDSYLQEQEDGSSSTQRILHWVQVMQWTHQQIKFGKNDIWLTFDLWRNLENQVRSMEKEA
RLREKERLAAIEAEKEAMRQAAIAAALEAEEFEAAQRAAAEAEAAAQAAEIAAIAADRWS
SDKNPFDDDCRSDMTNEDDRTEIETHFDQSGKRSEWGDDEYGPNLDMSKMMEDYSVQPEE
QVEEVSISSIRRWWARFVYFSTWWVPSFTLKYIGKMSRQDVQMAWREKVTLCLLIFAFSG
SIIFFIVGLSQIICPGTKDLYSAEDVTNHQTISDYWVSVRGTVYDMTKFVATDHGTAAYM
AGKSNLDPLAGRDLSYTFPPPLSVACAGLVSDPIITVTPNETIVLGPFVHFSGPQQPERS
LDKLRDPYWLNKYFGPTMNIYKRGDLVIPMKQIKDDYSSWGRLIASIDDKVYDLTDYMAS
ARRYPSGSTGVPNYHYLHTSIETLFTKFGGKDATAEWNRYSAAMDEQTRIRNKACLDNVF
YIGRLDYRESLKCTFVNYLLLSFAVVMSVVILVKFLAALQFGSAPTPEDHDKFVICQVPC
YTEDEESLRKTIDSLTAMTYDDKHKLLFLIADGMIIGSGNDKPTPRILLDILGHDENDDP
EALMFKSIGEGSKQLNYGKVYSGVYQHEGHVVPYVVVVKVGKSSERAKPGNRGKRDSQII
CMNFLNKVHFDSEMSPLELEIFYHIKHIIGIEPRLYEYILMVDSDTEVYPDALNRLISCM
LHDSRIIGLCGETELGNEDRSWTTMIQVYEYYISHHLVKSFESLFGSVTCLPGCFCMYRI
RTASKHQPLIVSPNVIHAYSDNQVDTLHKKNLLHLGEDRYLTTLMMKNFPQYKMMFTPYA
KCRTVAPDQWRVLLSQRRRWINSTIHNLLELILLQELCGFCCLSMRFVVLTDLIGTITLP
SSVIYLIYLIYEVISGSGPIPTIALGMLAGAYGLQSLIFIFKRQWQHIGWMVIYMLAIPI
FSFFIPLYAFWHFDDFSWGNTRVVVGDKKKQIIVTDDEKFDEKMIPLKKWAVYEQEMWET
KTLRSEETNSKCSDYSYNDDEMPSIYNRSYNDVHSLQSHPSVMTSSKSNSNHTMNSRYQL
LPPLLSSFSDNDSLGLDLSSVFRSKSSTTTAAADDSNGMRGEDVKVAMLPEDNEIEKEII
RILASSNLMALTKKQVRDQLSKIFGVDLTIKKGFINATIERLLEQDF

Enzyme Prediction     

EC	2.4.1.16:11

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GT2	1230	1736	2.2e-237	0.9943074003795066

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
367353	Chitin_synth_2	0.0	1231	1736	4	527	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	6.76e-177	25	771	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.
214580	MYSc	9.13e-99	25	770	20	673	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.
276950	MYSc	5.53e-94	25	756	1	627	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.
133033	Chitin_synth_C	7.07e-75	1255	1587	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
CDS05755.1|GT2	0.0	30	1903	26	1832
CDS05327.1|GT2	0.0	14	1755	13	1730
CDS03648.1|GT2	0.0	11	1748	9	1750
CDZ98697.1|GT2	0.0	10	1769	17	1778
UOP56890.1|GT2	0.0	11	1739	13	1749

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
5I0H_A	1.27e-45	19	772	72	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	2.07e-45	19	772	70	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]
1LVK_A	4.97e-45	17	582	92	618	X-Ray Crystal Structure Of The Mg (Dot) 2'(3')-O-(N- Methylanthraniloyl) Nucleotide Bound To Dictyostelium Discoideum Myosin Motor Domain [Dictyostelium discoideum]
3MYH_X	6.63e-45	17	582	92	618	Insights into the Importance of Hydrogen Bonding in the Gamma-Phosphate Binding Pocket of Myosin: Structural and Functional Studies of Ser236 [Dictyostelium discoideum],3MYK_X Insights into the Importance of Hydrogen Bonding in the Gamma-Phosphate Binding Pocket of Myosin: Structural and Functional Studies of Ser236 [Dictyostelium discoideum],3MYL_X Insights into the Importance of Hydrogen Bonding in the Gamma-Phosphate Binding Pocket of Myosin: Structural and Functional Studies of Ser236 [Dictyostelium discoideum]
1MMD_A	8.83e-45	17	582	92	618	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|Q4P9K9|CHS8_USTMA	0.0	19	1745	14	1758	Chitin synthase 8 OS=Ustilago maydis (strain 521 / FGSC 9021) OX=237631 GN=CHS8 PE=3 SV=1
sp|O13395|CHS6_USTMA	0.0	870	1739	26	896	Chitin synthase 6 OS=Ustilago maydis (strain 521 / FGSC 9021) OX=237631 GN=CHS6 PE=3 SV=2
sp|J9VNT4|CHS5_CRYNH	0.0	24	1905	23	1931	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|J9VF17|CHS4_CRYNH	5.12e-301	881	1746	135	1001	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|O13353|CHS4_MAGO7	4.35e-145	1255	1736	686	1184	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

This protein is predicted as OTHER

Other	SP_Sec_SPI	CS Position
1.000062	0.000000

TMHMM  Annotations     

Start	End
913	930
951	973
1214	1236
1607	1629
1639	1661
1668	1690