ID A0A1J9R8C1_9EURO Unreviewed; 1865 AA.
AC A0A1J9R8C1;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE RecName: Full=chitin synthase {ECO:0000256|ARBA:ARBA00012543};
DE EC=2.4.1.16 {ECO:0000256|ARBA:ARBA00012543};
GN ORFNames=ACJ73_04761 {ECO:0000313|EMBL:OJD23885.1};
OS Blastomyces percursus.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Ajellomycetaceae; Blastomyces.
OX NCBI_TaxID=1658174 {ECO:0000313|EMBL:OJD23885.1, ECO:0000313|Proteomes:UP000242791};
RN [1] {ECO:0000313|EMBL:OJD23885.1, ECO:0000313|Proteomes:UP000242791}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=EI222 {ECO:0000313|EMBL:OJD23885.1,
RC ECO:0000313|Proteomes:UP000242791};
RA Cuomo C.A., Schwartz I.S., Kenyon C., De Hoog G.S., Govender N.P.,
RA Botha A., Moreno L., De Vries M., Munoz J.F., Stielow J.B.;
RT "Emmonsia species relationships and genome sequence.";
RL Submitted (AUG-2015) 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 -!- 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:OJD23885.1}.
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DR EMBL; LGTZ01000684; OJD23885.1; -; Genomic_DNA.
DR STRING; 1658174.A0A1J9R8C1; -.
DR VEuPathDB; FungiDB:ACJ73_04761; -.
DR OrthoDB; 1331060at2759; -.
DR Proteomes; UP000242791; 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:UP000242791};
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 907..926
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 946..966
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1212..1234
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1610..1630
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1636..1658
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1665..1688
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 1..794
FT /note="Myosin motor"
FT /evidence="ECO:0000259|PROSITE:PS51456"
FT DOMAIN 970..1033
FT /note="Cytochrome b5 heme-binding"
FT /evidence="ECO:0000259|PROSITE:PS50255"
FT DOMAIN 1807..1862
FT /note="DEK-C"
FT /evidence="ECO:0000259|PROSITE:PS51998"
FT REGION 1..27
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 594..661
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 614..636
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 637..651
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 104..111
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00782"
SQ SEQUENCE 1865 AA; 207117 MW; 27E693FF0C5FB520 CRC64;
MALHSLTGTG SIPAHAQSSL PSLPGHLQSD THLTAHLASR FHVSLPTARL SSQGLICLNT
YTSSTQGPDG QREGSAMGEA DDLARRAWAR LGGRGENQAV IFLGETGSGK TTVRSHLLSS
FLSLSSTPLS TKLSLAAFVF DTLTTTKSVT TPTASKAGLF FELQYDGSST VNPTLIGGKL
LDHRLERSRI ASVPTGERSF HVLYYLLAGT SPAEKTHLGL DSAIDIRTGG GSGNRSSGTV
SHKRWRYLGH PTQLKVGIND TEGFQQFKNA LRKLEFPRSE IAEICQVLAC ILQIGQLEFT
TGQSTTTGPE ESGGYSHEGG ETVTIVKNKD VLAIIAAFLG LSVDDLEASL GYKTKTIHRE
RVTVMLDPKG ARNNADDLAR TLYSLLVAYV IENINQRICA AEDAVANTIS IIDFPGFSQA
SSTGSTLDQL LNNAATESLY NYCLRSFFEY RADMLETEEV SVPPTSYFDN SDAVKGLLKQ
GNGLLAILDD QTRRGRSDMQ LLESLRKRFA NKNPAISVGS ATATLPGSNF ASKNQAANFT
VRHFAGEVDY PVQGLVEENS DLVSGDLMNL ITSSRSTFVR DLFGQEALQT IRHPKEKSAI
MQAQVSSKPL RMPSMARRKM DRPVRPTARA AQTDNDDDDI AGSTSSASGS KKRKPGALAN
GPSQGAAAQF LVSLDNINKS LATGSVNPYF VFCLKPNDRR IANQFDSKCV RAQVQTLGIA
EISQRLRNAD FPLFLPFSEF LGLSDAESII VGSEQEKCQL VVDERRWPKN EARVGSTGVF
LSERCWAEIA RVGERVVPSY SGGGTDDGGD GLLGAGTKDP YGDSKVRLLN SPDISSSPGA
YIYGDETKQA FYGGQDIDGR SDAGASAFNS GDMFKNLETR EQMAEKGNEK KMEEVDDVVV
SGSRKRWLAL VYMLTFYIPD VAIKFIGRMK RKDVRIAWRE KFAINLLIWF SCAFAVFFII
GFPQLICPKQ YVFSPDELSS HDGKKNDAYI AIRGEVFDLT AYIPSHYPKI VPRRALENYA
GLDATKLFPV QVHVLCDGVD GSIDPSVPLD FTSANRSGSV RVSRDDDPNA KYHDFRAFTN
DSRPDWYWNQ MRMLRANYRK GYVGYSPEYL KTLVDKDQSI AILDGFVYDL TNYVIGGRSP
RAPPGQEPPK DVNVNFMDPL VVNLFQQRPG QDISKLFRRL PLGERERAMR TCLTNLFQVG
KLDTRSSVQC QFAQYFILAI SLLLVTIIAF KFFAALQFGK KTLPENLDKF IICQVPAYTE
DEESLRRAID SMARMKYDDK RKLLVVICDG MIIGQGNDRP TPRIVLDILG VPETVDPEPL
SFESLGEGMK QHNMGKVYSG LYEVQGHIVP FLVVVKVGKP SEVSRPGNRG KRDSQLLLMR
FLNRVHYNLP MSPLELEIHH QIRNIIGVNP TFYEFIFQVD ADTMVAPDAA TRMVASFLQD
TRIIGLCGET GLNNAKSSMI TMIQVYEYYI SHNLTKAFES LFGSVTCLPG CFTMYRIRAA
DTGKPLFVSR EVVDAYSEIR VDTLHMKNLL HLGEDRYLTT LLLKHHPKYK TKFLFNAHAW
TIAPDSWAVF MSQRRRWINS TVHNLIELIP LQQLCGFCCF SMRFVVFVDL LSTIIQPVTV
AYVIYLIVLI AVNPTLIPIT AFILLGAIYG LQAIIFILRR KWEMVGWMII YILAMPVFSL
GLPLYSFWHM DDFTWGNTRI VTGEKGRKIV ISDEGKFDPS SIPKKKWEEY QSELWEAQTY
QDDRSEVSGF SYGTRSYHPP ASEYGFAPSR PLSQMELNRF AGSRMSVAPS EMLGHGPEME
MVDLAGLPSD DSLLAEIRDI LRTADLMTVT KKSVKLELEQ RFNVNLDAKR QYINSATEAV
LSGQL
//
