ID A1DHQ0_NEOFI Unreviewed; 1846 AA.
AC A1DHQ0;
DT 23-JAN-2007, integrated into UniProtKB/TrEMBL.
DT 23-JAN-2007, sequence version 1.
DT 27-MAR-2024, entry version 98.
DE RecName: Full=chitin synthase {ECO:0000256|ARBA:ARBA00012543};
DE EC=2.4.1.16 {ECO:0000256|ARBA:ARBA00012543};
GN ORFNames=NFIA_088630 {ECO:0000313|EMBL:EAW18907.1};
OS Neosartorya fischeri (strain ATCC 1020 / DSM 3700 / CBS 544.65 / FGSC A1164
OS / JCM 1740 / NRRL 181 / WB 181) (Aspergillus fischerianus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Fumigati.
OX NCBI_TaxID=331117 {ECO:0000313|EMBL:EAW18907.1, ECO:0000313|Proteomes:UP000006702};
RN [1] {ECO:0000313|Proteomes:UP000006702}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 1020 / DSM 3700 / CBS 544.65 / FGSC A1164 / JCM 1740 /
RC NRRL 181 / WB 181 {ECO:0000313|Proteomes:UP000006702};
RX PubMed=18404212; DOI=10.1371/journal.pgen.1000046;
RA Fedorova N.D., Khaldi N., Joardar V.S., Maiti R., Amedeo P., Anderson M.J.,
RA Crabtree J., Silva J.C., Badger J.H., Albarraq A., Angiuoli S., Bussey H.,
RA Bowyer P., Cotty P.J., Dyer P.S., Egan A., Galens K., Fraser-Liggett C.M.,
RA Haas B.J., Inman J.M., Kent R., Lemieux S., Malavazi I., Orvis J.,
RA Roemer T., Ronning C.M., Sundaram J.P., Sutton G., Turner G., Venter J.C.,
RA White O.R., Whitty B.R., Youngman P., Wolfe K.H., Goldman G.H.,
RA Wortman J.R., Jiang B., Denning D.W., Nierman W.C.;
RT "Genomic islands in the pathogenic filamentous fungus Aspergillus
RT fumigatus.";
RL PLoS Genet. 4:E1000046-E1000046(2008).
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}.
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DR EMBL; DS027696; EAW18907.1; -; Genomic_DNA.
DR RefSeq; XP_001260804.1; XM_001260803.1.
DR STRING; 331117.A1DHQ0; -.
DR EnsemblFungi; EAW18907; EAW18907; NFIA_088630.
DR GeneID; 4587362; -.
DR KEGG; nfi:NFIA_088630; -.
DR VEuPathDB; FungiDB:NFIA_088630; -.
DR eggNOG; KOG2571; Eukaryota.
DR eggNOG; KOG4229; Eukaryota.
DR HOGENOM; CLU_000192_0_2_1; -.
DR OMA; LEMHHQI; -.
DR OrthoDB; 1331060at2759; -.
DR Proteomes; UP000006702; 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:UP000006702};
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 887..906
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 926..946
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1194..1216
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1592..1613
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1619..1640
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1647..1670
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 1..777
FT /note="Myosin motor"
FT /evidence="ECO:0000259|PROSITE:PS51456"
FT DOMAIN 950..1009
FT /note="Cytochrome b5 heme-binding"
FT /evidence="ECO:0000259|PROSITE:PS50255"
FT DOMAIN 1788..1843
FT /note="DEK-C"
FT /evidence="ECO:0000259|PROSITE:PS51998"
FT REGION 1..22
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 102..109
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00782"
SQ SEQUENCE 1846 AA; 205080 MW; 2E344D57E11C607A CRC64;
MAAQSPAGGA PSHAQSSLPS LPAHLQSDTH LTAHLASRFH VGLPTARLSS QALISLNTYT
TSTKGPDGGK EGSAMGEAED LAKRAFTRLG ARGENQAVVF LGESGSGKTT IRSHLLSAFL
SFSSTPLSSK LSYAAFLFDT LTTTKSLTTQ TASKAGLFLE LQYDGSSSVN PTLIGGKIID
HRLERSRITS VPTGERSFHV LYYLLAGTSP AEKAHLGFDK AVYVSTSSGA IGHKRWRYLG
HPTQLKVGVN DVEGFQHFKT ALRKLEFPRS EIAEICQILA TILHIGQLEF ASGQATTTHA
EESGGYSHEG GETVTIVKNK DVLSIIAAFL GLSVEDLENS FGYRTKTIHR ERVTVMLDPK
GARQNADELA RTIYSLLVAY VIEAANQRIC AAEDSVANTI SIVDFPGFAQ ACATGSTLDQ
LLNNAATELL YNFCLQSFFD RKADELEREE VSVPATSYFD NTDAVRGLLK HGNGLLSILD
DQTRRGRTDN QLLESLRRRF ENKNPTIIVE GSKRTSLISQ NARSAFTVKH FAGEVDYSVN
GLIEENGEFI SGDLMRLMKS TKSDFVRELF GQAALQTVTH PKEKTAIMQA QVSSKPLRMP
SMARRKTSPS SRLAFDAGDA DEVESQAESI AKDSGRRKSA MLTSGIQGAA GQFLSSLDIV
NKCLSSTNLN PYFIFCLKPN DRRIANQFDS KCVRAQVQMF GIAEISQRLR NADFSVFLPF
AEFLGLAEIG NIVVGSDKEK AEVVLDEKRW PGNEARVGST GVFLSERCWA DLAKVGERVV
PVYAADMSDE GGDGLLHPRS TGYGDSKVRL LNPADQSPGA FIYGDEAKQG YFGSRDLDGR
SDAGNSAFNS GDMFRNHETR EQMLEKGNEK KMEEVDDAPV SGSRKRWIAL VYLLTFYVPD
FAIKLFGRIK RKDVRMAWRE KFAINLIIWF SCGVAIFFIV AFPGLVCPTQ HVYSAAELSS
HDGKDGHSSF IAIRGVVFDL DKFMPGHYPD IVPESALKKY AGVDATGLFP VQVSALCQGK
SGSVDPTVLL DYRPTNISGS ATTISGTDTN SVYHDFRHFT NDSRPDWFYE QMVMLKANYL
KGYVGYTPKY LNTLGKKSQS IGSINGKVYD LTNYIAGGRL TKAPPGETVP PDVDTDFMDS
SVVSLFQSLP GQDLSKHWEN LKIDPALRHR MQLCLDNLFF VGHVDTRNSA QCEFARYFIL
AISLLICSII VFKFLAALQF GRKNVPENLD KFIICQVPAY TEDEESLRRA IDSMARMRYD
DKRKLLVVIC DGMIIGQGND RPTPRIVLDI LGVPESVDPE PLSFESLGEG QKQHNMGKVY
SGLYEVQGHI VPFLVIVKVG KPSEVSRPGN RGKRDSQMVL MRFLNRVHYN HPMSPMELEM
HHQIRNVIGV NPTFYEFILQ VDADTVVAPD SATRMVATFL NDTRLIGVCG ETALTNAKTS
AVTMIQVYEY YISHNLTKAF ESLFGSVTCL PGCFTMYRIR SAETAKPLFV SKEVVDAYAE
IRVDTLHMKN LLHLGEDRYL TTLLLKHHSK YKTKYISSAK AWTIAPESWT VFLSQRRRWI
NSTVHNLIEL IPMQQLCGFC CFSMRFVVFV DLLSTVIQPV TLAYIIYLIY WLAKDTSTIP
FTSLILLAAI YGLQALIFII RRKWEMVGWM IVYLLAIPVF SLALPLYSFW HMDDFSWGNT
RIITGEKGRK VVISDEGKFD PASIPKKKWE EYQTELWEAQ TSRDDRSEVS GISYGTKSYH
PAQSEYGFPG SRPMSQLDLP RFGSRMSLAP SEMMSRHADM EMENLSHLPS DDAILAEIRE
ILRTADLMSV TKKSIKLELE RRFGVNLDLK RPYINSATEA ILAGAL
//
