ID A0A136J5A0_9PEZI Unreviewed; 1870 AA.
AC A0A136J5A0;
DT 11-MAY-2016, integrated into UniProtKB/TrEMBL.
DT 11-MAY-2016, sequence version 1.
DT 27-MAR-2024, entry version 34.
DE RecName: Full=chitin synthase {ECO:0000256|ARBA:ARBA00012543};
DE EC=2.4.1.16 {ECO:0000256|ARBA:ARBA00012543};
GN ORFNames=Micbo1qcDRAFT_134425 {ECO:0000313|EMBL:KXJ92355.1};
OS Microdochium bolleyi.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Xylariomycetidae; Xylariales; Microdochiaceae; Microdochium.
OX NCBI_TaxID=196109 {ECO:0000313|EMBL:KXJ92355.1, ECO:0000313|Proteomes:UP000070501};
RN [1] {ECO:0000313|Proteomes:UP000070501}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=J235TASD1 {ECO:0000313|Proteomes:UP000070501};
RG DOE Joint Genome Institute;
RA David A.S., May G., Haridas S., Lim J., Wang M., Labutti K., Lipzen A.,
RA Barry K., Grigoriev I.V.;
RT "Draft genome sequence of Microdochium bolleyi, a fungal endophyte of
RT beachgrass.";
RL Submitted (FEB-2016) to the EMBL/GenBank/DDBJ databases.
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}.
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DR EMBL; KQ964249; KXJ92355.1; -; Genomic_DNA.
DR SMR; A0A136J5A0; -.
DR STRING; 196109.A0A136J5A0; -.
DR InParanoid; A0A136J5A0; -.
DR OrthoDB; 1331060at2759; -.
DR Proteomes; UP000070501; 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; 3.10.120.10; Cytochrome b5-like heme/steroid binding domain; 2.
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 InterPro; IPR025662; Sigma_54_int_dom_ATP-bd_1.
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.
DR PROSITE; PS00675; SIGMA54_INTERACT_1; 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:UP000070501};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 887..906
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 926..946
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1194..1216
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1592..1612
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1618..1640
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1647..1670
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 1..783
FT /note="Myosin motor"
FT /evidence="ECO:0000259|PROSITE:PS51456"
FT DOMAIN 1812..1867
FT /note="DEK-C"
FT /evidence="ECO:0000259|PROSITE:PS51998"
FT REGION 1..25
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 587..650
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 587..608
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 103..110
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00782"
SQ SEQUENCE 1870 AA; 207204 MW; 241B451089F82853 CRC64;
MALNLPTGAG GGAHTQPSLP SLPAHLQSDT HLTAHLASRY HVSIPTARLS SHALISINTY
TNSAKGLDGG KEGSAMAGAE DMADRAFLRL GHRSENQAIL FLGESGSGKT TIRSHMLSSL
LNKSSTPLST KVSLAAYVFD SLTTTKTATT PTASKAGLFY ELQYDTASNT NPLLIGGKLL
DHRLERSRIA EVPTGERNFH VLYYLLAGTS EAEKTHLGID SPRDAAGQKR WKYLGHPTQL
KVGINDAEGF QLFKNALRKL EFPRSDIAEI CQILACILHI GQLEFETSAD TTPNGDDSGG
FSHEGAQNVT AARNKDVLGI IAAFLGVSSA DLQNTMGYKT KMIHRERVTV MLDPAGARSN
ADELARTLYS LLVAYVIENI NQRICAAEDT VSNTISIIDF PGFSQQSSTG SSLDQLLNNA
AVESLYNLTL QTFFDRKADM LETEEITVTA TSYFDNSDAV KGLCKPGNGM LSILDDQTRR
GRTDMQLLES LRKRFEGKNP AIAVGSATAK LPGSNFMSEN TSATFTVKHF AGEVDYPIKG
LVEENGEVIS GDLMSLVKSS KSEFVAKLFG QEVLQTIMHP HERSTVMQAS VSSKPMRAPS
VMSRKTTRTM RSRIARRQDS MEDIASEAGD FDPVSQGRDD AKRTGTGMRA SEQGASGQFL
AALQNVKAAI TAPNTNNYFV FCLKPNDRRI ANQFDSKCVR TQLQTFGIAE ISQRLRAADF
SVFLPFGEFL GLTEADSLIV GSERDKAQSV VQDKQWLSNE VLVGSTGVFL SERCWMEITQ
LSENVSASGR WQSEAGDGLT PSPGDPFGMS KERLLSVGNT PQYTDKSRAG YFASGDADTR
SEAGVSAFGA GDMFQSMETR EQMAERGNEK ALVEVEEYTD TASRKRWVFI VYMMTWFIPD
FLIRWAGRMP RKDVRMAWRE KLAINIFIWV SCLTAVFFMI VFPMLICPKQ NVFSAEELTA
FNGQNGASAY TAIRGQVFDL GKFAPTHIPA YLERKALLQY AGLDITGMFP VQVSALCQGT
TGTVDQAVLL DYKSDNTTGA ATINSQDVNA QYHDFRWFTG DYRKDWFAEQ MMILRSQWKK
GNIGYSAEYV ATLATKSNSI AILGGRVYDF TKYLKGGRTI KAPPGEPEPT DPNVTDFMSN
LVVDLFKLKA GQDVTEAWDS LGLDRTVKAY QKRCLDNLFY VGDVDTRNSV RCQFANYLIL
VISIILCSII GFKFLAALQF GSKNVPENLD KFVMCQIPAY TEDEESLRRA IDSAARMQYD
DKRKLLVIVC DGMIIGQGND RPTPRIVLDI LGVSETVDPE PLSFESLGEG LKQHNMGKVY
SGLYEVQGHI VPFLVIVKVG KPSEVSRPGN RGKRDSQMII MRFLNRVHYN LAMSPLELEI
YHQVRNVIGV NPTFYEFMLQ IDADTVVAAD SATRMVSTFI HDTRIIAVCG ETALTNSKSS
FITMIQVYEY WISHNLTKAF ESLFGSVTCL PGCFTMYRIR AADSGKPLFV SREVVENYST
IRVDTLHLKN LLHLGEDRYL TTLLLKFHNK YKTKYITSAQ AWTIAPDSWA VFMSQRRRWI
NSTVHNLMEL IPMNQLCGFC CFSMRFIVFV DLLSTVVQPI TMVYITYLLV LVGTQSTIIP
ITAFVMLAAI YGLQAIIFIL RRKWEMIGWM ILYILAIPVF SFALPLYSFW HMDDFNWGNT
RVIAGESGKK VVITDEGKFD PASIPRKKWE EYQAELWEAQ TVRDDARSEI SGYSYATKAG
MNVGVSEYGY YAHSRPGSTA GIIPPYGHGT HGMSRMSLAP SEMPGNRQSQ FGGSQFFSND
PSSVELSNLS GLPSDDALLA EIREILKTAD LMTVTKKGIK QELERRFGVP LDSKRTYINS
ATEALLSGQL
//
