ID V5F8X2_BYSSN Unreviewed; 1782 AA.
AC V5F8X2;
DT 22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT 22-JAN-2014, sequence version 1.
DT 27-MAR-2024, entry version 49.
DE RecName: Full=chitin synthase {ECO:0000256|ARBA:ARBA00012543};
DE EC=2.4.1.16 {ECO:0000256|ARBA:ARBA00012543};
GN ORFNames=PVAR5_1010 {ECO:0000313|EMBL:GAD92419.1};
OS Byssochlamys spectabilis (strain No. 5 / NBRC 109023) (Paecilomyces
OS variotii).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Thermoascaceae; Paecilomyces.
OX NCBI_TaxID=1356009 {ECO:0000313|EMBL:GAD92419.1, ECO:0000313|Proteomes:UP000018001};
RN [1] {ECO:0000313|Proteomes:UP000018001}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=No. 5 / NBRC 109023 {ECO:0000313|Proteomes:UP000018001};
RX PubMed=24407650; DOI=10.1128/genomeA.01162-13;
RA Oka T., Ekino K., Fukuda K., Nomura Y.;
RT "Draft genome sequence of the formaldehyde-resistant fungus Byssochlamys
RT spectabilis No. 5 (anamorph Paecilomyces variotii No. 5) (NBRC109023).";
RL Genome Announc. 2:E0116213-E0116213(2014).
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:GAD92419.1}.
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DR EMBL; BAUL01000025; GAD92419.1; -; Genomic_DNA.
DR eggNOG; KOG2571; Eukaryota.
DR eggNOG; KOG4229; Eukaryota.
DR HOGENOM; CLU_000192_0_0_1; -.
DR InParanoid; V5F8X2; -.
DR OrthoDB; 1331060at2759; -.
DR Proteomes; UP000018001; 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 CDD; cd04190; Chitin_synth_C; 1.
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 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; 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 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; 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:UP000018001};
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 745..762
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 782..805
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1042..1061
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1439..1460
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1466..1487
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1494..1517
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 1724..1780
FT /note="DEK-C"
FT /evidence="ECO:0000259|PROSITE:PS51998"
FT REGION 354..374
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1703..1724
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 354..368
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1782 AA; 197642 MW; 34149E0C3A04364A CRC64;
MAGMSARYSV YSNSSAPAGP PAAAPALRSA AQQGTQVSTT TLLNALHTFY ASGRPYPLDS
GSSIVVNTWV TASQTNPDGS TGGVVDPDLA TRAWQHARRR AEDGCIVLCS MHHSTPSLLV
PFLSSLPLST PPIAFTALSA LRPFLSTVTP FNPSYGRHSS LAVSYTFTLR GAVTGLSLAL
STSGINTTDG LLNIPAESGF RAFDVFYYLI TSASTPAERE FLSLKDPSAY ALLNRSNTYD
APSYVPTADD AASAEDLRAS LKAIGIKGAA LRGLLSVLAG LLKLGNAVGF MVDQEELEET
CEDVGALLDI EPDVLLEKCS TDEREVLIAG IYEALVDWVI SKSNEAIANE LQSVQENGSS
QGGQGARSPF TDDDNADTVG ITIVDIPDPT LGKAVAMRGI FDDSLGINAE MKEDGLDITP
AGHSVLNEMR NAVAAVEFDL GITNNLTSRD RERANDKRQN VLEKVGVEAE TGGFLQQVLF
PVENEGITLG KRGRFDLATT LGSSRVWYHL ALHPTDDDPA SLASLPSITS AWSAGTVSRQ
LREWRLPEWA NRRHKNLDFT ADFDIDEFYN RYMPLGCMEG RDGVENWVVE RGWSNGEVVL
GHERIWMREA PWWEAETMLD VKADEPEGNP FMMADPFASG YSSNPPNPNA SGFFPPVEPV
GMQGSRDNLL QTQSIAGGAR SIAPTVPHSF HTQGGDYGLG TKGDQKTYDD VLYDGDVGRY
TGELDPEFGD PKHIEKKHIT PVRRIWSGFV WAMTFWIPSF LLRYVGRMKR PDVRMAWREK
VVLVFLILLF NGIVLFYIIA FGNILCPNKD KAWNNKQVSY HQGDNDFYVS IHGKVYDISK
FWRIQHSDTS IETTPTNMQP FAGENLDAYF PPPLSRACRP FVTDQSIKMQ NNNTNAVLYP
NALHDCGPLN QPDPDTALNK ITWYEDVFLP KIKEYYKGDL VYTTGTVQSQ ATSAERYWVI
INQKIYDLTN YFYTLKMMNN LDTYNFLPSG VTELFKNNPG QDITDKWQDS VQFENALNCL
DNAFYVGKTD FRDTPRCQVN NYILLAFTIL ICSVILIKFL AALQLGSKRR PAPQDKFVIC
QVPAYTEGED ALRKGLDSLT ALQYDNKRKL ICVICDGMIV GGGNDRPTPK IVLDILGVDP
KIDPPALPFK SVGQGSDQLN YGKVYSGLYE FEGNVVPYVV IVKVGKESEQ NKSKPGNRGK
RDSQILLLNF LNRVHHRAPM SPLELEIFHQ INNVIGVDPE LYEYLLMVDA DTSVKEDALN
RLVAACANDA KIAGICGETS LQNEERSWWT MIQVYEYYIS HHLTKAFESL FGSVTCLPGC
FCMYRLRTAD KGRPLIISDK VIQEYSDNDI DTLHKKNLLS LGEDRYLTTL MTKHFPSMSY
KFIPDAFAST AAPETWGVLL SQRRRWINST VHNLVELAAL KDLCGFCCFS MRFVVLVDLL
GTIILPATCA YLVYMIVLAA THQGQFPLIT IILLACVYGL QAIIFIIKRQ WQHIGWMIIY
LCAYPVYSVI LPLYSFWKQD DFSWGNTRVV IGEKGDKRVV AVEDEIFDPR NIPLQRWDDY
ALANGLPGRR GNPDMSQEKF INGAYADDAA MELDDMQSTY SSVKPASTIL TGFGGHGRQT
GPYMPPHSPA PFAGNTAGNR SSHFSSFTRY TDHPQMGSSH SRQQSMGNLS HYQDNPMNAS
RYSMGMMQSS ENLLRQGARS PLTGGFNSRP VSTVPDFRGG PSAGPDDTTI TEAIQSCLAE
VDLDSVTKKQ VRALVEQRLQ TELTGERKAF LDRQIDHELA NM
//
