ID A0A2P5HKR7_9PEZI Unreviewed; 1881 AA.
AC A0A2P5HKR7;
DT 23-MAY-2018, integrated into UniProtKB/TrEMBL.
DT 23-MAY-2018, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE RecName: Full=chitin synthase {ECO:0000256|ARBA:ARBA00012543};
DE EC=2.4.1.16 {ECO:0000256|ARBA:ARBA00012543};
GN ORFNames=DHEL01_v210751 {ECO:0000313|EMBL:POS70855.1};
OS Diaporthe helianthi.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Diaporthales; Diaporthaceae; Diaporthe.
OX NCBI_TaxID=158607 {ECO:0000313|EMBL:POS70855.1, ECO:0000313|Proteomes:UP000094444};
RN [1] {ECO:0000313|EMBL:POS70855.1, ECO:0000313|Proteomes:UP000094444}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=7/96 {ECO:0000313|EMBL:POS70855.1,
RC ECO:0000313|Proteomes:UP000094444};
RA Baroncelli R.;
RT "Polyketide synthases of a Diaporthe helianthi virulent isolate.";
RL Submitted (SEP-2017) 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}.
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:POS70855.1}.
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DR EMBL; MAVT02001462; POS70855.1; -; Genomic_DNA.
DR SMR; A0A2P5HKR7; -.
DR STRING; 158607.A0A2P5HKR7; -.
DR InParanoid; A0A2P5HKR7; -.
DR OrthoDB; 1331060at2759; -.
DR Proteomes; UP000094444; 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; 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; PS50255; CYTOCHROME_B5_2; 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:UP000094444};
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 879..895
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 916..938
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1188..1210
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1586..1606
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1612..1634
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1641..1664
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 1..773
FT /note="Myosin motor"
FT /evidence="ECO:0000259|PROSITE:PS51456"
FT DOMAIN 942..1001
FT /note="Cytochrome b5 heme-binding"
FT /evidence="ECO:0000259|PROSITE:PS50255"
FT DOMAIN 1823..1878
FT /note="DEK-C"
FT /evidence="ECO:0000259|PROSITE:PS51998"
FT REGION 1..23
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 588..644
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 623..640
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 102..109
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00782"
SQ SEQUENCE 1881 AA; 208371 MW; B647F354D909858B CRC64;
MASNAHGGNG GAHTQPSLPS LPAHLQSDTQ ITAHLASRFH VNIPTAQLSS HALISLNTYT
SSTKGHDGGK EGSAMAGAED MAGRAFIRLG HRSENQAILF LGESGSGKTT VRSHILTALL
NKTSTPLSNK VSLAAYVFDT LTTTKTATTP TASKAGLFYE LQYDTSSSTH PELIGGKLLD
HRLERSRIAE VPTGERNFHV LYYLLAGTSG AEKQHLGLDQ PGGASQKRWR FLGHPTQLKV
GINDAEGFQL FKTALRKLEF ARGEIAEICQ ILATILHIGQ LEFETSNSTT ATGDDSGGFS
HEGGQTTTTV KNKDVLSIVA AFLGVGQQDL QTTLGYKTKI IHKERVTVML DPAGARSNAN
ELARTLYSLL VAYVIENINQ KICAPEESIA NTVSIVDFPG FIQQSPTHST IDQLLNNAAT
EALYNLTLKN FFDNKAEMLE SEEVSVAATS YFDNSDATKG LLKTGNGLLS ILDDQTRRHR
TDIQLLESLR KRFEGKNPAV SVSSATARLP GSNFLSENSA ASFTVRHFAG EVEYPVKGLV
EENGEVISGD LLNLINSTKS DFVARLFGQE ALQTVVHPQE RTAVMQATVS SKPTRAPSVM
SRKNRYRPGT VKRPGTAFTA TQESEKVEEE SSEPKRSIRH SEQGASGQFL SALDNVTKSV
TAPGTNAYFV FCLKPNDRRI ANQFDSKCVR TQVQTFGIAE ISQRLRSADF TVFLPFAEFL
GLADADTILV GSEREKVELV VEEKRWPSNE VQVGSTGVFL SERCWMEMNN FAEIDPNRYR
LPSDADDNQT PGGTLGDPFA ASKERLLSAG NTPGYNDKTK SGYFGSDDVD ARSDAGMTAI
GGGDMFKNLE TREEMAQKGN EKNMEEVEEF RDTGTRKRWV FFVYLLTWWV PDLLIRKMGK
MPRKDVRLAW REKLAINMII WFSCLIAIFF TIALPQIICP KQNVYSSAEL TDYNGKNGKG
MYVAIRGIVF DLEAFMPTHY PSYISDTIME KFAGQDVTDL FPVQVSALCQ GVDGKVDPAV
SLDYTSTNFT GSASTTSITS LYAKYHDFNY YQNDSRPDWF AEQMIRLKRG GYKKGNIGYT
PDYIKKQGQK GKSVGIIGSR IYDMSKYVAG GRRMRAPVGE QAPTDVDLTN FMDQLVVDLF
QQKAGADVTK LWDALALDAA KKQRMKLCLD NLFYIADVDT RNSVKCQFAN YLILAVSILL
CSIIGVKFLA ALQFGGNNVP ENLDKFIMCQ IPAYTEDEDS LRRAIDSAAR MRYDDKRKLL
VVICDGMIIG QGNDRPTPRI VLDILGVSET VDPEPLSFES LGEGMKQHNM GKVYTGLYEV
QGHIVPFMVV VKVGKPSEVS RPGNRGKRDS QMVIMRFLNR VHYNLPMSPL ELEMYHQVRN
IIGVNPTFYE FLLQMDADTV VAPDSATRFV SAFLDDTRLI AVCGETALTN AKSSFVTMIQ
VYEYYISHNL VKAFESLFGS VTCLPGCFTM YRIRAADSGK PLFVSREVVE QYSTIRVDTL
HMKNLLHLGE DRYLTTLLLR HHQQYKTKYM MKAHAWTIAP DSWTVFLSQR RRWINSTVHN
LMELMPMNQL CGFCCFSMRF IVFMDLMTTV VQPVTIAYIV YLIVLISIDA TVVPMTAFIM
LGAIYGLQGI IFIVRRKWEM IGWMLLYICA VPVYSFALPL YAFWHMDDFN WGNTRVIAGE
KGKKVVISDE GKFDPASIPR KKWEEYQAEL WDAQTARDDV RSEVSGYSYA TKAGPNVGVS
EHGWGGYTPS RPASVVNYGH GPYNTSSGDL KVPLAGSQSR LSFAASEMMG GGISPANRAS
QFGGSQFFGG SQNDLEMSNL AGLPGDDALL AEIREILRTA DLMTVTKKGV KKELERRFGV
PLDARRAYIN SATEACLSGQ L
//
