ID A0A178DG50_9PLEO Unreviewed; 1766 AA.
AC A0A178DG50;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 27-MAR-2024, entry version 35.
DE RecName: Full=chitin synthase {ECO:0000256|ARBA:ARBA00012543};
DE EC=2.4.1.16 {ECO:0000256|ARBA:ARBA00012543};
GN ORFNames=IQ07DRAFT_580927 {ECO:0000313|EMBL:OAL43008.1};
OS Pyrenochaeta sp. DS3sAY3a.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Pleosporales; Pleosporineae; Cucurbitariaceae;
OC Pyrenochaeta.
OX NCBI_TaxID=765867 {ECO:0000313|EMBL:OAL43008.1, ECO:0000313|Proteomes:UP000077535};
RN [1] {ECO:0000313|EMBL:OAL43008.1, ECO:0000313|Proteomes:UP000077535}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DS3sAY3a {ECO:0000313|EMBL:OAL43008.1,
RC ECO:0000313|Proteomes:UP000077535};
RG DOE Joint Genome Institute;
RA Zeiner C.A., Purvine S.O., Zink E.M., Wu S., Pasa-Tolic L., Chaput D.L.,
RA Haridas S., Grigoriev I.V., Santelli C.M., Hansel C.M.;
RT "Comparative analysis of secretome profiles of manganese(II)-oxidizing
RT ascomycete fungi.";
RL Submitted (MAY-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}.
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DR EMBL; KV441671; OAL43008.1; -; Genomic_DNA.
DR STRING; 765867.A0A178DG50; -.
DR InParanoid; A0A178DG50; -.
DR OrthoDB; 1331060at2759; -.
DR Proteomes; UP000077535; 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:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0004100; F:chitin synthase activity; IEA:UniProtKB-EC.
DR GO; GO:0003774; F:cytoskeletal motor activity; IEA:InterPro.
DR GO; GO:0048315; P:conidium formation; IEA:UniProt.
DR Gene3D; 1.10.10.820; -; 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; 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; PF00173; Cyt-b5; 1.
DR Pfam; PF08766; DEK_C; 1.
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.
PE 4: Predicted;
KW Glycosyltransferase {ECO:0000256|ARBA:ARBA00022676};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Motor protein {ECO:0000256|ARBA:ARBA00023175};
KW Myosin {ECO:0000256|ARBA:ARBA00023123};
KW Reference proteome {ECO:0000313|Proteomes:UP000077535};
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 734..751
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 771..790
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1036..1055
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1433..1454
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1460..1481
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1488..1511
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 1707..1763
FT /note="DEK-C"
FT /evidence="ECO:0000259|PROSITE:PS51998"
FT REGION 1..30
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 346..370
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 347..361
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1766 AA; 196838 MW; FB9ACA92CFAF0A4A CRC64;
MSFVNNSRMS VYSTASTSVP RPGNPPSQTS TTTLLNTLNS AYKHGQAYNL EASTSLVVNT
WVNAKTITND RIGGTVDLEL GRKAWEHARR RAEDGCIVLA SLHDASPSLF SPFISGLPLS
LPGNFYIALE ALKAFTHCVT PQNPFTPRYS ALAAVFTLNI AGTVVGAEIK LSTSGLDVQQ
GLLQVPAHQG YRAFDVFYYL NSSSASKQEK QFLNIQPLDR YALLSRSGTY DPPAYLPDAD
DAAAAEDFRA NLKAIGIKGQ KLLDVISTLT GLLKLGNTLD YFVDEETLQT VCEDVSDLVD
IPVDVLRQKL GSNEREVAIG GIYEAIVDFV IAQANATIKA DMQRAKSGFS SGDSDGSQPG
MMTPVESDEE NGDIVNITVV DIPSRALGKA IALRTVFDDT DGINAEMRDD GVQVTPAGNS
VLESMKEAVH NCTADLNLSG PALSEREAAV EKREAVLDKI ALEISDESHF LRQVLYPVQN
NGIVLGKHGR FDLPTTVASS RVWFQLALHP TDIIPTSMNQ DFNSTWQAGV VSRQLREWRL
PEWANRRNRY LDFTADFEHH EFYDRYHPLG CTDGKEGIQT FALERGWSNG EIVVGTERVW
VREGTWWEAE SQLDQKTQDF ENSPNMLGHM IGAGGMESGY PAQGPPRAST FFPPLAPVTQ
VPSNPFQSSA SLAAPSGADA KSVAPTTLTA PAQAAGDYGL GMKGDENKGI TYYDAESGGN
AIVTESPITA TRRMWVAFVW AVTFWFPSPL LKFVGRMKRP DVRMAWREKV VLVLLIILLN
GAIVFYLVGF GKLLCPKKDK VWNRKEVSQH QGEDDFFVSH HGVVYDLSSF WKKQHSDSNT
ESTRERMMDL AGANMDGYIA PPLYLACPHL IVENDRNKVL ELSSNETLDF SFAVHKAGYA
PIPADSKAMK SANWYPDVFL PAIGEFRKGD LVWDSGVIKD EGEDLNHMWF TMQDRVYDLT
DYFKTLDMMN DLDEYKFLDP KLTDLVKSKA GQDISEDMKN QMNSTAYAYN LQCLDNAFFV
GKKDFRKSAK CRVNDYILLS VSILLCTVIV IKFLAALQLG SRKRPANQDK FVICQVPAYT
EGEDHLRKSL DSLTALAYDN KRKLICVVCD GMIVGGGNDR PTPKIVLDIL GVDPKVDPPA
LPFWSVGEGS EQLNYGKVYS GLYEFEGNVV PYIVVVKMGK ESEQHKSKPG NRGKRDSQIL
LMSFLNRVHH RSAMNPLELE MFHQINNIIG VDPELYEYLL MVDADTMVRP DALNRLVASC
ANDSKIAGIC GETSLENEDR SWWTMIQVYE YYISHHLSKA FESLFGSVTC LPGCFCMYRL
RTADKGKPLV ISDKVIKDYA DCVVDTLHKK NLLSLGEDRY LTTLMTKHFP NMSYKFIPDA
FALTAAPDTW SILLSQRRRW INSTIHNLAE LVFLKDLCGF CCFSMRFVVF IDLFGTLVLP
SICAYLVFLI YTVASGTGQF PLFSIIMLAA VYGLQALIFI IKRQWQHVGW MIIYLLAFPV
FSLILPMYSF WKQDDFSWGN TRVVIGEKGT KQVLTTDDEG FDPKSIPMMR WDEYAERNDL
PGRRGLPGQQ SEKGGFSAYE DEAYEMNDMQ SVYSSVKPAS TIMSNMHHIS HMPPQSPGPY
QGMQTRQSTY SNLSRYHDNP HESRLMSMGN MSEQYNNSPY GQRPSMGGFQ SSDNLMTSTP
PIRGRSPLGF NQSRPGSTVN FQSMMNGPSD GMIIETVQAC LKDADLDRVT KKQIVALAEQ
RLQVQLTGER KIFLSQTIDN ELANMG
//
