ID A0A150V760_9PEZI Unreviewed; 1849 AA.
AC A0A150V760;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE RecName: Full=chitin synthase {ECO:0000256|ARBA:ARBA00012543};
DE EC=2.4.1.16 {ECO:0000256|ARBA:ARBA00012543};
GN ORFNames=M433DRAFT_3833 {ECO:0000313|EMBL:KYG46310.1};
OS Acidomyces richmondensis BFW.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Dothideomycetidae; Mycosphaerellales; Teratosphaeriaceae; Acidomyces.
OX NCBI_TaxID=766039 {ECO:0000313|EMBL:KYG46310.1, ECO:0000313|Proteomes:UP000075602};
RN [1] {ECO:0000313|EMBL:KYG46310.1, ECO:0000313|Proteomes:UP000075602}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BFW {ECO:0000313|EMBL:KYG46310.1,
RC ECO:0000313|Proteomes:UP000075602};
RX PubMed=26973616; DOI=10.3389/fmicb.2016.00238;
RA Mosier A.C., Miller C.S., Frischkorn K.R., Ohm R.A., Li Z., LaButti K.,
RA Lapidus A., Lipzen A., Chen C., Johnson J., Lindquist E.A., Pan C.,
RA Hettich R.L., Grigoriev I.V., Singer S.W., Banfield J.F.;
RT "Fungi Contribute Critical but Spatially Varying Roles in Nitrogen and
RT Carbon Cycling in Acid Mine Drainage.";
RL Front. Microbiol. 7:238-238(2016).
CC -!- FUNCTION: Polymerizes chitin, a structural polymer of the cell wall and
CC septum, by transferring the sugar moiety of UDP-GlcNAc to the non-
CC reducing end of the growing chitin polymer.
CC {ECO:0000256|ARBA:ARBA00024009}.
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:KYG46310.1}.
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DR EMBL; JPDO01000121; KYG46310.1; -; Genomic_DNA.
DR STRING; 766039.A0A150V760; -.
DR Proteomes; UP000075602; Unassembled WGS sequence.
DR GO; GO:0016459; C:myosin complex; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
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 GO; GO:0048315; P:conidium formation; IEA:UniProt.
DR CDD; cd14879; MYSc_Myo17; 1.
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; IPR001199; Cyt_B5-like_heme/steroid-bd.
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; IPR036037; MYSc_Myo17.
DR InterPro; IPR029044; Nucleotide-diphossugar_trans.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR22914; CHITIN SYNTHASE; 1.
DR PANTHER; PTHR22914:SF45; CHITIN SYNTHASE; 1.
DR Pfam; PF03142; Chitin_synth_2; 1.
DR Pfam; PF00173; Cyt-b5; 1.
DR Pfam; PF08766; DEK_C; 1.
DR Pfam; PF00063; Myosin_head; 1.
DR SMART; SM01117; Cyt-b5; 2.
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 Glycosyltransferase {ECO:0000256|ARBA:ARBA00022676};
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:UP000075602};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:KYG46310.1};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 878..897
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 909..929
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1187..1206
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1576..1599
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1611..1630
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1637..1660
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 1..771
FT /note="Myosin motor"
FT /evidence="ECO:0000259|PROSITE:PS51456"
FT DOMAIN 1791..1846
FT /note="DEK-C"
FT /evidence="ECO:0000259|PROSITE:PS51998"
FT REGION 577..626
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 781..801
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 578..594
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 93..100
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00782"
SQ SEQUENCE 1849 AA; 206257 MW; D82EE47ECAF06A58 CRC64;
MASPQTANLV ALPMHSQSDT GLTSHIASRF HNQEPICTLS TQAYISVNTY KSASKGPNGD
KEGSALGAAE ELAQRMWIRL GSRQENQAAV FLGETGAGKT TIRSFLLSHL LQFSSTPLSK
KLSFASFVFD SLTSTKSVTT PTASKAGLFF ELQYNTASST HPTLIGGKIL DHRLERSRVT
TVPPGERNFH VLYYLLAGTS PSERQHLGLD LGEGNSVGNR ASLGSKRWRY LGHPSQLKVG
INDSEGFQHF KTALRKLEFP REEIAHICEI LAAILHIGQL EFQSIQATTP APDESGGYGH
EGGEEVTVVK NKEVLRAIAA FLGVAEKDLE QSLGYRTKTL HRERVTIMLD PKGARENADE
LARTLYSLLV AYIMEKINEK TCADEEAVAN TISIVDFPGF SHTSSTGSTL DQLLNNAATE
SLYNFCLQSF FERRADLLES EEVQVPATSY FDNTDAVKGL LKPGNGLLSI LDDQMRRGKT
DLQFLESIRK RFENRNPAIE VAPATVIAPG SNFATPNEKP QFTVKHFAGP VDYPVNGLLE
ANGEIISGDL MNLINTSNSD FIAKLFGQEA LNKVTHPRDR SAVTQASVSS KPSRMPSMAR
RRGGQKPTTL GAFRDYDDGG SDEGGRNFSR STRAATTEFQ QGAAAQFLSS LDNINKSLTA
PNTNAYFVFA LKPNDRRIAN QFESKTVRMQ VQALGIAEIS QRLKNADFSI FMPFREFLGA
AEGEVTVVGS EREKAEAIIE EKSWPANEAR AGSTGVFLSE RCWRQIAHVP DMSGGAPLLY
SDEPDNEAGV PPTPKGGFGD SRVQLLQPSP GSHYLDDKAA GYFGSRDLDA RSEAGASAFR
DGDMFRNLDT RSVMAEKGND AKMAEVDVHP MTGSRKRWLF IVYALTFWLP DFAIRIRRKD
VRLAWREKLA INMIIWLSCA SIVFFMIGMP RLICPHQYVY SPSELATKNG KKGEPSYIAI
RGIVFDLGKF QYAHYPSIVP VSALEKYAGT VATNLFPVQV SAMCQGVNGH IDPAVQLNYQ
NYNYSGESNV LSATDPNAQY HDFRWASPLN SSRPDWFTQQ MLQLESQYYK GTVGYSPQYL
RTLADKQNSI AYINNRVYDF TQYIAGGRNA QYPPGYPKPS TPPDTNFMDE GIVSLFQTRS
GQDLTKYWEA LDMTPEYRQN MLTCMNNLFY VGDLDTRDSV QCQFAKYILL AVSMLLVSVI
GFKFFAALQF SRKNVPENLD KFLICTVPAY TEDEDSLRRA IDSAARMRYD DKRKLLFIIC
DGMIIGQGND RPTPRIVLDI LGVPENVDPE PLSFESLGEG QRQHNMGKVY SGLYEVQGHI
VPFIVVVKVG KPSEVSRPGN RGKRDSQMIL MRFLNRVHYN LPMTPLELEL HHQIRNVIGV
NPTFYEFLMQ IDADTIVAPD SATRFISAFL SDTKLIAVCG ETALSNAKAS MITMMQVYEY
YISHNLTKAF ESLFGSVTCL PGCFSMFRIR AAETGKPLFV SREIVNDYAE IRVDTLHTKN
LLHLGEDRYL TTLLLKYHSK YKTKYIMRAH AWTIAPEHFT VFMSQRRRWI NSTVHNLIEL
IPIQEMCGFC CFSMRFVVFV DLLSTIVQPV IVGYIAYLIV EVVQNPSTVP ITAFILLGAI
YGLQAIIFIL RRKWEMIGWM IIYMLATPLF SCALPLYAFW HMDDFSWGST RIITGDNGKQ
VVVSDEGKFD PSSIPRKKWE DYQAELWDAA TQRDDTRSEV SGISYGTRSW HPAASEYGYA
PSRPMSQLGV PPMPHGGSRM SLLSDQGGIG MHAARNYSGS DLDIPGSQQR QPSDDELLAE
IREILKTADL MHVTKKSIKM QLEQRFACNL DSRRQYIGSA TEAILSGQL
//