ID A0A060SSS7_PYCCI Unreviewed; 1913 AA.
AC A0A060SSS7;
DT 03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT 03-SEP-2014, sequence version 1.
DT 27-MAR-2024, entry version 43.
DE RecName: Full=chitin synthase {ECO:0000256|ARBA:ARBA00012543};
DE EC=2.4.1.16 {ECO:0000256|ARBA:ARBA00012543};
GN ORFNames=BN946_scf184857.g27 {ECO:0000313|EMBL:CDO77420.1};
OS Pycnoporus cinnabarinus (Cinnabar-red polypore) (Trametes cinnabarina).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Polyporales; Polyporaceae; Trametes.
OX NCBI_TaxID=5643 {ECO:0000313|EMBL:CDO77420.1, ECO:0000313|Proteomes:UP000029665};
RN [1] {ECO:0000313|EMBL:CDO77420.1, ECO:0000313|Proteomes:UP000029665}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BRFM137 {ECO:0000313|EMBL:CDO77420.1,
RC ECO:0000313|Proteomes:UP000029665};
RA Levasseur A., Lomascolo A., Ruiz-Duenas F.J., Uzan E., Piumi F., Kues U.,
RA Ram A.F.J., Murat C., Haon M., Benoit I., Arfi Y., Chevret D., Drula E.,
RA Kwon M.J., Gouret P., Lesage-Meessen L., Lombard V., Mariette J.,
RA Noirot C., Park J., Patyshakuliyeva A., Wieneger R.A.B., Wosten H.A.B.,
RA Martin F., Coutinho P.M., de Vries R., Martinez A.T., Klopp C.,
RA Pontarotti P., Henrissat B., Record E.;
RT "The genome of the white-rot fungus Pycnoporus cinnabarinus: a
RT basidiomycete model with a versatile arsenal for lignocellulosic biomass
RT breakdown.";
RL Submitted (JAN-2014) 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: 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:CDO77420.1}.
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DR EMBL; CCBP010000453; CDO77420.1; -; Genomic_DNA.
DR SMR; A0A060SSS7; -.
DR STRING; 5643.A0A060SSS7; -.
DR HOGENOM; CLU_000192_0_2_1; -.
DR OMA; LEMHHQI; -.
DR OrthoDB; 1331060at2759; -.
DR Proteomes; UP000029665; 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 CDD; cd14879; MYSc_Myo17; 1.
DR Gene3D; 1.10.10.820; -; 1.
DR Gene3D; 1.20.58.530; -; 1.
DR Gene3D; 6.20.240.20; -; 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 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.
DR PROSITE; PS50890; PUA; 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:UP000029665};
KW Transferase {ECO:0000313|EMBL:CDO77420.1};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 924..943
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 964..983
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1224..1246
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1622..1643
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1649..1670
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1677..1700
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 13..772
FT /note="Myosin motor"
FT /evidence="ECO:0000259|PROSITE:PS51456"
FT DOMAIN 1854..1909
FT /note="DEK-C"
FT /evidence="ECO:0000259|PROSITE:PS51998"
FT REGION 597..644
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 651..673
FT /note="Actin-binding"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00782"
FT REGION 773..800
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 858..880
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 613..635
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 773..793
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 865..880
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 113..120
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00782"
SQ SEQUENCE 1913 AA; 215413 MW; 114AC83F4FEF2841 CRC64;
MNRQSTMPPQ QLESVTDLAT LSPVSEDIVV SCIRERFMND NIYTAVGTSA LVAVNPHKYV
PSNSDAVLHK YAAEYRDTSP DKTLLPPHIF QLANNAYYHM RRTAQDQSIL FTGETASGKS
ENRRLAIKTL LELSVSQPGK KGSKLGHQIP AAEFVLETFG NSRTLFNPNA SHFGKYTELQ
FTERGRICGV KTLDYYLEKG RVAGAPSGER NYHIFYYLVA GASPEERQHM HLSEKTQYRY
LGARAPPLGV RGPSSQNEDA TRFEQLKVAL KNVGFSKRHV AQTCQLIAAI LHLGNLEFTI
DRHRNEDAAV VRNLDVLNIV SEFLGVQSAA LEAALSYKTK LVKKELCTVF LDPDGASDNR
DELAKTLYSL LFAWLNEHIN QRLCRDDFAT FIGLFDLPGP QNLTSRPNSL DQFCINFANE
RLLNFIHKRL FEAHVQEYNN EGISRFVPHV PYFDNSECLR LLQHRPGGLI HIMDDQARRM
PRKTDHTMVE AFVKRWGNHS SFKSGGVDRQ GFPTFTINHY SGPVTYSASG FLEKNLDAIN
PDFVSLLRGT SAGTGDAPAA DGSGSMNPFV RGLFSAKAIA TQAHPRNEET IVAAQQPVKP
MRAPSTRRKN TIKRMPTLKE SGDIDEKDRD DDDTPSSNGP PCVAGEFRQA LDVLFETLED
TQSWYVFCIN PNDSQLPNQL EGRSVKAQVR SVGLAEIARR CVNVFEAMMT PDEFTQRYQG
LLQSVGVTEG DSRQKVEQAR TALGLQERDI VLGMSMVFLS QAAFHRLEDD LRSKDTEEQK
RNRLRDAEAE AGLDPRNLGD PYAPYHVPGT DSPYHADFGD PFSNSSQALP LVQHASPFQR
ADMYDEYDER KSFRSDDFDG RSAYTSQRDD GSVSNFGTES YAPSRNMFQN TDGKGLLDKE
ALAGEIQEGE VTEVIKESSA RRKWVALCWV LTWWCPNFLL KYVGRMKRED VRQAWREKLA
INMIIWFICA CAIFVIAIIS PLICPTEHVF NSQELAQHSQ QNNPNNVYTS IRGEVFDLTK
IAADHQRHVS VVPTKSILKY GGTSADNIFP VQVSALCNGI TGSVSPYVVL SSSNNTDVNA
QYHDFRSWTN DPRPDWYFES MTQMRWTARV GYLAYSSKQL KSMASTGKSV AVYRGFVYDF
TTYLTSPPAV ATLPNNAVAP GDIDTHFMHS AILDVFQHNA GSDVTKQIDQ LNIGDDVLER
QRVCMRNLFM IGKLDTRNSP QCLFATYILL ALSIMMVSVI GFKFIASLNF SAPRAPEEHD
KFVICQVPCY TEGHASLKKT IDSLAQMKYD DKRKLLFIIC DGMVVGSGND QPTPRIVLDV
LGANPNVDAE PLSFLSLGEG AKQHNMGKVF SGLYETAGHV VPYIVVVKCG KPGEKSRPGN
RGKRDSQMVL MHFLNKVHFN APMNPLELEI YHQIKNVIGV NPTFYEYVFM VDADTTVHPL
SLNRLVSAMI HDKKLLGVCG ETELANAKQS IITMMQVYEY FISHHMAKAF ESLFGSVTCL
PGCFTLYRLR TPDTHKPLFI SNQVIHDYSE NRVDTLHMKN LLHLGEDRYL TTLLLKHFSN
YKTQFVRDAH AYTVAPDDWK VLLSQRRRWI NSTVHNLAEL LFLDQLCGFC CFSMRFVVMI
DLLSTLIQPV TVGYIIYLIY LAAGAHSHIP TLSIILIAAV YGVQALVFIL RRKWDMVGWM
IFYILAIPAF SFFLPLYSFW RMDDFSWGQT RIVLGEAGKK IVVHDEGKFD PRSIPLKSWN
DYENELWDKE SNHSIGSWVP PTKMRNDGYA ESATASLYGR ETMYEPAMSR AYSPAPSHQM
YPPPGYQSGR NTPLSHVMMP GVLHQPTPSR PASNYLDVQI PITHSPEDQD FIGGPSDAEI
ERAVDEHLRN ADLTTVTKRE IRRRLEEQFG MDLSARKRVI NDAIDRVLLA RAG
//
