ID W9YHQ6_9EURO Unreviewed; 1764 AA.
AC W9YHQ6;
DT 14-MAY-2014, integrated into UniProtKB/TrEMBL.
DT 14-MAY-2014, sequence version 1.
DT 27-MAR-2024, entry version 41.
DE RecName: Full=chitin synthase {ECO:0000256|ARBA:ARBA00012543};
DE EC=2.4.1.16 {ECO:0000256|ARBA:ARBA00012543};
GN ORFNames=A1O1_07879 {ECO:0000313|EMBL:EXJ81814.1};
OS Capronia coronata CBS 617.96.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae; Capronia.
OX NCBI_TaxID=1182541 {ECO:0000313|EMBL:EXJ81814.1, ECO:0000313|Proteomes:UP000019484};
RN [1] {ECO:0000313|EMBL:EXJ81814.1, ECO:0000313|Proteomes:UP000019484}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 617.96 {ECO:0000313|EMBL:EXJ81814.1,
RC ECO:0000313|Proteomes:UP000019484};
RG The Broad Institute Genomics Platform;
RA Cuomo C., de Hoog S., Gorbushina A., Walker B., Young S.K., Zeng Q.,
RA Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Allen A.W., Alvarado L.,
RA Arachchi H.M., Berlin A.M., Chapman S.B., Gainer-Dewar J., Goldberg J.,
RA Griggs A., Gujja S., Hansen M., Howarth C., Imamovic A., Ireland A.,
RA Larimer J., McCowan C., Murphy C., Pearson M., Poon T.W., Priest M.,
RA Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Capronia coronata CBS 617.96.";
RL Submitted (MAR-2013) 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: Cell membrane {ECO:0000256|ARBA:ARBA00004651};
CC Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651}. Membrane
CC {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004141}.
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:EXJ81814.1}.
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DR EMBL; AMWN01000007; EXJ81814.1; -; Genomic_DNA.
DR RefSeq; XP_007726935.1; XM_007728745.1.
DR STRING; 1182541.W9YHQ6; -.
DR GeneID; 19162734; -.
DR eggNOG; KOG2571; Eukaryota.
DR HOGENOM; CLU_000192_0_0_1; -.
DR OrthoDB; 1331060at2759; -.
DR Proteomes; UP000019484; Unassembled WGS sequence.
DR GO; GO:0016459; C:myosin complex; IEA:InterPro.
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; 2.
DR Gene3D; 1.10.10.60; Homeodomain-like; 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; 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; SM01117; Cyt-b5; 2.
DR SMART; SM00242; MYSc; 1.
DR SUPFAM; SSF55856; Cytochrome b5-like heme/steroid binding domain; 2.
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 Reference proteome {ECO:0000313|Proteomes:UP000019484};
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 727..747
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 763..781
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1024..1042
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1415..1438
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1450..1469
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1476..1499
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 1705..1762
FT /note="DEK-C"
FT /evidence="ECO:0000259|PROSITE:PS51998"
SQ SEQUENCE 1764 AA; 196492 MW; D4923E49C52AB7CB CRC64;
MAHRYSTYST NSSQLGAVRS AAQQPTQVST TTLLNALHTV YASGQTYQLD ASTSIATNTW
LTAVNPDAQG RVGGTVDADI ASRAWEHARR RAEDACVILA SLHPSTPSVF QAFLQVIPLP
TPPIVYTALS ALRPFLSCVT PINPTTFLHS SFSAKYTVTL SGTVTGLSLA LSESGIDVEK
GLSKIPSEHG YRAFDVFYYL LTSASTPAER EFLSLQPPSK YALLNRSGTY EPPSYLPAAD
DVAAAEDFRS ALKSIGIKGA TFRGLLSSLA GLLKLGETVG FLVDSDVLED VCEDVGALIG
LEPEVLLNKC TTDDREVLIA GMYEALVDWV ISKANEAIAT ELRTGALTPD SSTQSGDEVS
LTIIEIPGET LGKAVTLRNV FDDTFGINAE MKDDGIEVVP AGHSVIKEMQ AAVAEADADL
NIKGGPLSRE REHEHERREA ILEKIGLEAE PGGFLHTLLY PVDGEGLNFG KKGRFDLSAT
LVSSRAWYQL SIHPTDDTPS ALATLASPTS AWSAGTVSRQ LRAWRLPEWA NYRNRHLDFT
ADFDVEEFVT RYSRLGCKDG KDGVESFLLE RGWTNGEVVV GHERVWMRES AWWEAESMLD
MLPAASGFSD DATFGQPLNP FASSYSANAP NNASSFFPPL GENMSLHDSR ENLLAQAGPE
RARSVAPTMA KTVQSIGGDY GLGPKGDSHK DNVYYDSDLG RYTGELDPEF GDPRNVESKP
TSRARQVWVS VVWALTWFIP SVLLRYIGRM KRPDVRMAWR EKVVLVFLIF LLNAIILFYI
IEFGRLLCPN FDKAWNAKEV GYHTGTNDVY VSIHGKVYDI TKFYRLQHSD TSIETTAENM
LPFAGQNLDA YFPPPLSRAC PGLNVDESVF LQHNDTDAIQ YPNAVHTSGP RLQTNQKSAL
YSWNWYNDRF QPKIEEYYKG DLVVTKSKIK RQAEDDQRMW VIIHHKIYDL TDYFYTLKLM
NNYDTYKFFP DEVTDLITNN PGLDITDKWG TSAAFGNSLN CMTNAFYVGK VDFRDSAKCQ
VNNYILLAFT CLLCAVILTK FLSALQLGSK RRPAPQDKFV ICQVPAYTEG EDHLRKSLDS
LTALQYDNKR KLICVICDGM IVGGGNDRPT PKIVLDVLGV DPKIDPPALP FRSVGNGSEQ
LNYGKVYSGL YEYEGNVVPY IVIVKVGKES EQSKSKPGNR GKRDSQILLM QFLNRVHHRS
PMSPLELEMF HQINNIIGVD PELYEYLFMV DADTNVKEDS LNRLVAACAN DAKIAGICGE
TSLENEERSW WTMIQVYEYY ISHHLAKAFE SLFGSVTCLP GCFCMYRLRT ADKGRPLIIS
DKVIREYADC DVDTLHKKNL LSLGEDRYLT TLMTKHFPAM SYKFIPDACA LTAAPETWSV
LLSQRRRWIN STIHNLAELV LLKDLCGFCC FSMRFVVFID LFGTIILPAT CCYLVYLIYR
VASHTGQFPL ISIVMIAAVY GLQAIIFIIK RQWQHVGWMI IYIIAYPIYS FVLPIYSFWN
QDNFSWGNTR IVIGEKGDKK VVAIQDEGFD PRSIPLQRWD DYAAANNLPG LRGDTGSYHE
KGFEVNYTDD PAMMEMDDMH STYSSIKPSS TILTGFARQQ HPYMAPPRSP APFGMNNRAS
TLTGLTQFRD HPVSMHGRNM SMMSLGSQGR LISPSPGPYQ DHIRSPYQSG FSGMQHSASR
PSLLGMATSR PASTIMDFRT VPSAGPSDHE IVDAIRAVLS EIDLDTVTKK QVRALVEQRL
QCEIPAGERR QFLDKAIDGE LANM
//
