ID A0A1Y1VE10_9FUNG Unreviewed; 1800 AA.
AC A0A1Y1VE10;
DT 30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT 30-AUG-2017, sequence version 1.
DT 28-JUN-2023, entry version 30.
DE RecName: Full=chitin synthase {ECO:0000256|ARBA:ARBA00012543};
DE EC=2.4.1.16 {ECO:0000256|ARBA:ARBA00012543};
GN ORFNames=BCR36DRAFT_324082 {ECO:0000313|EMBL:ORX52983.1};
OS Piromyces finnis.
OC Eukaryota; Fungi; Fungi incertae sedis; Chytridiomycota;
OC Chytridiomycota incertae sedis; Neocallimastigomycetes; Neocallimastigales;
OC Neocallimastigaceae; Piromyces.
OX NCBI_TaxID=1754191 {ECO:0000313|EMBL:ORX52983.1, ECO:0000313|Proteomes:UP000193719};
RN [1] {ECO:0000313|EMBL:ORX52983.1, ECO:0000313|Proteomes:UP000193719}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=finn {ECO:0000313|Proteomes:UP000193719};
RG DOE Joint Genome Institute;
RA Haitjema C.H., Gilmore S.P., Henske J.K., Solomon K.V., De Groot R.,
RA Kuo A., Mondo S.J., Salamov A.A., Labutti K., Zhao Z., Chiniquy J.,
RA Barry K., Brewer H.M., Purvine S.O., Wright A.T., Boxma B., Van Alen T.,
RA Hackstein J.H., Baker S.E., Grigoriev I.V., O'Malley M.A.;
RT "Genomes of anaerobic fungi encode conserved fungal cellulosomes for
RT biomass hydrolysis.";
RL Submitted (AUG-2016) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:ORX52983.1, ECO:0000313|Proteomes:UP000193719}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=finn {ECO:0000313|Proteomes:UP000193719};
RG DOE Joint Genome Institute;
RA Mondo S.J., Dannebaum R.O., Kuo R.C., Labutti K., Haridas S., Kuo A.,
RA Salamov A., Ahrendt S.R., Lipzen A., Sullivan W., Andreopoulos W.B.,
RA Clum A., Lindquist E., Daum C., Ramamoorthy G.K., Gryganskyi A., Culley D.,
RA Magnuson J.K., James T.Y., O'Malley M.A., Stajich J.E., Spatafora J.W.,
RA Visel A., Grigoriev I.V.;
RT "Pervasive Adenine N6-methylation of Active Genes in Fungi.";
RL Submitted (AUG-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=[(1->4)-N-acetyl-beta-D-glucosaminyl](n) + UDP-N-acetyl-alpha-
CC D-glucosamine = [(1->4)-N-acetyl-beta-D-glucosaminyl](n+1) + H(+) +
CC UDP; Xref=Rhea:RHEA:16637, Rhea:RHEA-COMP:9593, Rhea:RHEA-COMP:9595,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:17029, ChEBI:CHEBI:57705,
CC ChEBI:CHEBI:58223; EC=2.4.1.16;
CC Evidence={ECO:0000256|ARBA:ARBA00000319};
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: Belongs to the TRAFAC class myosin-kinesin ATPase
CC superfamily. Myosin family. {ECO:0000256|PROSITE-ProRule:PRU00782}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00782}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:ORX52983.1}.
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DR EMBL; MCFH01000014; ORX52983.1; -; Genomic_DNA.
DR STRING; 1754191.A0A1Y1VE10; -.
DR EnsemblFungi; ORX52983; ORX52983; BCR36DRAFT_324082.
DR OrthoDB; 1331060at2759; -.
DR Proteomes; UP000193719; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016459; C:myosin complex; IEA:UniProtKB-KW.
DR GO; GO:0003779; F:actin binding; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004100; F:chitin synthase activity; IEA:UniProtKB-EC.
DR GO; GO:0003774; F:cytoskeletal motor activity; IEA:UniProtKB-UniRule.
DR Gene3D; 1.10.10.820; -; 1.
DR Gene3D; 1.20.58.530; -; 1.
DR Gene3D; 1.10.10.60; Homeodomain-like; 1.
DR Gene3D; 3.40.850.10; Kinesin motor domain; 1.
DR Gene3D; 1.20.120.720; Myosin VI head, motor domain, U50 subdomain; 1.
DR InterPro; IPR004835; Chitin_synth.
DR InterPro; IPR036400; Cyt_B5-like_heme/steroid_sf.
DR InterPro; IPR014876; DEK_C.
DR InterPro; IPR036961; Kinesin_motor_dom_sf.
DR InterPro; IPR001609; Myosin_head_motor_dom.
DR InterPro; IPR029044; Nucleotide-diphossugar_trans.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR22914; CHITIN SYNTHASE; 1.
DR PANTHER; PTHR22914:SF13; CHITIN SYNTHASE; 1.
DR Pfam; PF03142; Chitin_synth_2; 1.
DR Pfam; PF08766; DEK_C; 1.
DR Pfam; PF00063; Myosin_head; 1.
DR PRINTS; PR00193; MYOSINHEAVY.
DR SMART; SM00242; MYSc; 1.
DR SUPFAM; SSF55856; Cytochrome b5-like heme/steroid binding domain; 1.
DR SUPFAM; SSF109715; DEK C-terminal domain; 1.
DR SUPFAM; SSF53448; Nucleotide-diphospho-sugar transferases; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR PROSITE; PS51998; DEK_C; 1.
DR PROSITE; PS51456; MYOSIN_MOTOR; 1.
PE 3: Inferred from homology;
KW Actin-binding {ECO:0000256|PROSITE-ProRule:PRU00782};
KW ATP-binding {ECO:0000256|PROSITE-ProRule:PRU00782};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Motor protein {ECO:0000256|ARBA:ARBA00023175, ECO:0000256|PROSITE-
KW ProRule:PRU00782};
KW Myosin {ECO:0000256|ARBA:ARBA00023123, ECO:0000256|PROSITE-
KW ProRule:PRU00782};
KW Nucleotide-binding {ECO:0000256|PROSITE-ProRule:PRU00782};
KW Reference proteome {ECO:0000313|Proteomes:UP000193719};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 859..878
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1135..1153
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1530..1551
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1557..1578
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1585..1608
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 11..730
FT /note="Myosin motor"
FT /evidence="ECO:0000259|PROSITE:PS51456"
FT DOMAIN 1742..1797
FT /note="DEK-C"
FT /evidence="ECO:0000259|PROSITE:PS51998"
FT REGION 570..598
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 798..817
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 799..817
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 112..119
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00782"
SQ SEQUENCE 1800 AA; 207564 MW; 6D7ECFD724D86B5B CRC64;
MVRGRKPMLS MIIDNVVNCE GKSKDEIVNN LRDLYMNEVF YMKIGSNALL SVNPMREVES
SNDETLEKYT EIALDTSNEG KRKLSPHIFE MVCNAYFHMH RNKEDQSIIL NGLSGSGKTF
CRQLIINQLC EISKGKKKSK TKNGLKYVNT ILNAFGNSQT MDNVDASHYG LYTEVQYNSH
GKIIGAKFLD YILDKHHLYS SYDYERNFHV FYYLLAGASQ AEKSYWRLDD STTYEYLSGE
RAINQTDEKN YENLAIALKS LGIGRRTQRQ IFQLLAAILH IGNIHFIDAQ NPQQDSCQIK
NLDELEIVSE YLGIHPRNLE TILTYKTMLI KRELCTVFLT AEHAEIQKNE FASLLYSLLF
RWIVEYINTK LCKTEEETAN FIGIMDFRGT SICEDGDLYQ LLSNFANEKL FQFTNQQLFN
IPSEDYKYQR LDIDIPLPIE NIDTPFGRNK SVIELFTDGK SLLSVMDSEC NRSKPDTQRL
LTKFDPLQQK SNSIVLNNEG FSVKHYFGDC DYNVNDFIKS NSDNMNTDFV ALLKGSGEMP
ASSNDFIKGL FSEKSVTTKS LPGASNICEA QQSQKPLRAP STKRKNGRKK PTSEIIPTIG
NQLNDSLNEV IDTMANTNPW FVYCIKPNKS QKMSSYKFDT DFAKKQIDFY GIIDVAKARE
YDFTSYYNFD EFIEIFNPII QPMELNQSDP KEKCIQFAKI FNWSEKEFAI GNSKVYVAEE
QWKILDNEVR AVENALKSEK HKDMEDGDND DEGDERAIAM GEDVEGSTME ESESQLGSEI
YQSDEDFDPE ALGGETILGN KEVKKDEESS EEEEQHTTTA RKQWVCCTYL LTFYICNCCL
AKCGKMVRKD IQMAWREKFA LNLIILILNL GILFYIVGLG QIICPKKNWL THEELDIRST
NKNMLVGLHG RYLDVTKFFQ NNNHRIFEQV EDYAGRDVTY MFWSPLDLWG VSYCLGVGEK
PTNDWDYIYK NYESMRKSHV KSGQYIHRQD EPPTNPKGEK SGYKKDYVHY LLKNYFKGWI
VENKNIINVP PNLSRGQSYP QYVVIHENIY DVTNYFNSPV AFLGEFGSVV LANQNKDVTK
EFEEYRTKYI MNGNNVLNPA YENYHPDQCL RCMGDLFFYG KVDHRNDFKC QLTNYILLIG
SLIIVMVIGV KFLSALQLSS RKDPEDHDKF VICQVPCYTE DEESLLRTIK SLSILKYDDK
RKLLFIIADG MIIGSGNDRP TPRIVLDLLG VDPSVDPESF AFQSIGEGMK QYNMAKIYSG
LYECQGRSIP FIVVVKVGAP SERSRPGNRG KRDSQMILMR FLSKVHNNSP MTPMELELYH
QIKNIIGVNP SFYEYVLMVD ADTQVEPDSL NRMVSCMIHD SKIMGICGET QLLNEKDSWV
TMIQVYEYFI SHHLAKAFES LFGSVTCLPG CFSMYRIRTP TKRIPLLISN AIIEDYSECK
VDTLHKKNLL SLGEDRYLTT LLMKHFPQMK LKFTPDALCQ TNVPDRWSVL LSQRRRWINS
TVHNLIELLF LPQLCGFCCF SLRFVVMIDL FATLIQPVTL MYMAYLIYYI IFSGEKLPTI
SLLLILSMYG FQIIIFLLKK QWQHVGWMII YLMAMPLYGL FIPLYSFWHF DDFSWGNTRV
VVGDGKKKEF LPENEKFKLS MIPTKTWDEY EQELYEQSTK DSRLDDFSDH TGAKSDIYAP
SIPAMPQQSM QMQQLYAESA YAGSSYNAPA YQCMNTNTLN PNMSMISSIP PSQRNSMEFT
RFPSDEEIVA QIQNIIYNSD LMKITKKQVR EELSEHFGID MSGKKDFINC TIEEILSGQM
//
