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Database: UniProt
Entry: Q4X0H6_ASPFU
LinkDB: Q4X0H6_ASPFU
Original site: Q4X0H6_ASPFU 
ID   Q4X0H6_ASPFU            Unreviewed;      1848 AA.
AC   Q4X0H6;
DT   05-JUL-2005, integrated into UniProtKB/TrEMBL.
DT   05-JUL-2005, sequence version 1.
DT   31-JUL-2019, entry version 93.
DE   SubName: Full=Chitin synthase ChsE {ECO:0000313|EMBL:EAL93639.1};
DE            EC=2.4.1.16 {ECO:0000313|EMBL:EAL93639.1};
GN   ORFNames=AFUA_2G13440 {ECO:0000313|EMBL:EAL93639.1};
OS   Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC
OS   A1100) (Aspergillus fumigatus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX   NCBI_TaxID=330879 {ECO:0000313|EMBL:EAL93639.1, ECO:0000313|Proteomes:UP000002530};
RN   [1] {ECO:0000313|EMBL:EAL93639.1, ECO:0000313|Proteomes:UP000002530}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100
RC   {ECO:0000313|Proteomes:UP000002530};
RX   PubMed=16372009; DOI=10.1038/nature04332;
RA   Nierman W.C., Pain A., Anderson M.J., Wortman J.R., Kim H.S.,
RA   Arroyo J., Berriman M., Abe K., Archer D.B., Bermejo C., Bennett J.,
RA   Bowyer P., Chen D., Collins M., Coulsen R., Davies R., Dyer P.S.,
RA   Farman M., Fedorova N., Fedorova N., Feldblyum T.V., Fischer R.,
RA   Fosker N., Fraser A., Garcia J.L., Garcia M.J., Goble A.,
RA   Goldman G.H., Gomi K., Griffith-Jones S., Gwilliam R., Haas B.,
RA   Haas H., Harris D., Horiuchi H., Huang J., Humphray S., Jimenez J.,
RA   Keller N., Khouri H., Kitamoto K., Kobayashi T., Konzack S.,
RA   Kulkarni R., Kumagai T., Lafon A., Latge J.P., Li W., Lord A., Lu C.,
RA   Majoros W.H., May G.S., Miller B.L., Mohamoud Y., Molina M., Monod M.,
RA   Mouyna I., Mulligan S., Murphy L., O'Neil S., Paulsen I.,
RA   Penalva M.A., Pertea M., Price C., Pritchard B.L., Quail M.A.,
RA   Rabbinowitsch E., Rawlins N., Rajandream M.A., Reichard U.,
RA   Renauld H., Robson G.D., Rodriguez de Cordoba S., Rodriguez-Pena J.M.,
RA   Ronning C.M., Rutter S., Salzberg S.L., Sanchez M.,
RA   Sanchez-Ferrero J.C., Saunders D., Seeger K., Squares R., Squares S.,
RA   Takeuchi M., Tekaia F., Turner G., Vazquez de Aldana C.R., Weidman J.,
RA   White O., Woodward J., Yu J.H., Fraser C., Galagan J.E., Asai K.,
RA   Machida M., Hall N., Barrell B., Denning D.W.;
RT   "Genomic sequence of the pathogenic and allergenic filamentous fungus
RT   Aspergillus fumigatus.";
RL   Nature 438:1151-1156(2005).
CC   -!- SIMILARITY: Belongs to the TRAFAC class myosin-kinesin ATPase
CC       superfamily. Myosin family. {ECO:0000256|PROSITE-
CC       ProRule:PRU00782}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation
CC       of feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00782}.
CC   -!- CAUTION: The sequence shown here is derived from an
CC       EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is
CC       preliminary data. {ECO:0000313|EMBL:EAL93639.1}.
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DR   EMBL; AAHF01000001; EAL93639.1; -; Genomic_DNA.
DR   RefSeq; XP_755677.1; XM_750584.1.
DR   STRING; 746128.CADAFUBP00002848; -.
DR   EnsemblFungi; EAL93639; EAL93639; AFUA_2G13440.
DR   GeneID; 3513767; -.
DR   KEGG; afm:AFUA_2G13440; -.
DR   EuPathDB; FungiDB:Afu2g13440; -.
DR   HOGENOM; HOG000165497; -.
DR   InParanoid; Q4X0H6; -.
DR   KO; K00698; -.
DR   OMA; YNFCLQS; -.
DR   OrthoDB; 20724at2759; -.
DR   Proteomes; UP000002530; Chromosome 2.
DR   GO; GO:0030428; C:cell septum; IBA:GO_Central.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0016459; C:myosin complex; IEA:UniProtKB-KW.
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; IBA:GO_Central.
DR   GO; GO:0003774; F:motor activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0043936; P:asexual sporulation resulting in formation of a cellular spore; IMP:AspGD.
DR   GO; GO:0006038; P:cell wall chitin biosynthetic process; IMP:AspGD.
DR   GO; GO:0031505; P:fungal-type cell wall organization; IMP:AspGD.
DR   GO; GO:0030448; P:hyphal growth; IMP:AspGD.
DR   CDD; cd14879; MYSc_Myo17; 1.
DR   Gene3D; 3.10.120.10; -; 1.
DR   Gene3D; 3.90.550.10; -; 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; IPR036037; MYSc_Myo17.
DR   InterPro; IPR029044; Nucleotide-diphossugar_trans.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   PANTHER; PTHR22914; PTHR22914; 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; SSF52540; SSF52540; 1.
DR   SUPFAM; SSF53448; SSF53448; 1.
DR   SUPFAM; SSF55856; SSF55856; 1.
DR   PROSITE; PS50255; CYTOCHROME_B5_2; 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   Complete proteome {ECO:0000313|Proteomes:UP000002530};
KW   Glycosyltransferase {ECO:0000313|EMBL:EAL93639.1};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Motor protein {ECO:0000256|PROSITE-ProRule:PRU00782};
KW   Myosin {ECO:0000256|PROSITE-ProRule:PRU00782};
KW   Nucleotide-binding {ECO:0000256|PROSITE-ProRule:PRU00782};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002530};
KW   Transferase {ECO:0000313|EMBL:EAL93639.1};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    889    908       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    928    948       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM   1196   1218       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM   1594   1615       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM   1621   1642       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM   1649   1672       Helical. {ECO:0000256|SAM:Phobius}.
FT   DOMAIN        1    779       Myosin motor. {ECO:0000259|PROSITE:
FT                                PS51456}.
FT   DOMAIN      952   1040       Cytochrome b5 heme-binding.
FT                                {ECO:0000259|PROSITE:PS50255}.
FT   NP_BIND     102    109       ATP. {ECO:0000256|PROSITE-ProRule:
FT                                PRU00782}.
FT   REGION        1     22       Disordered. {ECO:0000256|SAM:MobiDB-
FT                                lite}.
FT   REGION      593    621       Disordered. {ECO:0000256|SAM:MobiDB-
FT                                lite}.
SQ   SEQUENCE   1848 AA;  205351 MW;  B190E7DF4C85B2E2 CRC64;
     MAAPSPAGGA PSHAQSSLPS LPAHLQSDTH LTAHLASRFH VGLPTARLSS QALISLNTYT
     TSTKGPDGGK EGSAMGEAED LAKRAFTRLG ARGENQAVVF LGESGSGKTT IRSHLLSAFL
     SFSSTPLSSK LSYAAFLFDT LTTTKSLTTQ TASKAGLFLE LQYDGSSSVN PTLIGGKIID
     HRLERSRITS VPTGERSFHV LYYLLAGTSP AEKAHLGFDK AVHVSTSSGA IGHKRWRYLG
     HPTQLKVGVN DVEGFQHFKT ALRKLEFPRS EIAEICQILA TILHIGQLEF ASGQATTTHA
     EESGGYSHEG GETVTIVKNK DVLSIIAAFL GLSVEDLENS FGYRTKTIHR ERVTVMLDPK
     GARQNADELA RTIYSLLVAY VIEAVNQRIC AAEDSVANTI SIVDFPGFAQ ACATGSTLDQ
     LFNNAATELL YNFCLQSFFD RKADELEREE VSVPATSYFD NTDAVRGLLK HGNGLLSILD
     DQTRRGRTDN QLLESLRRRF ENKNPTIIVE GSKRTSLISQ NARSAFTVKH FAGEIDYSVN
     GLIEENGEFI SGDLMRLMKS TKSDFVRELF GQAALQTVTH PKEKTAIMQA QVSSKPLRMP
     SMARRKTSPS SRLAFDAGDA DEVESQAESI AKDSSSGRRK SAMLTSGIQG AAGQFLSSLD
     IVNKCLSSTN LNPYFIFCLK PNDRRIANQF DSKCVRAQVQ MFGIAEISQR LRNADFSVFL
     PFAEFLGLAE IGNIVVGSDK EKAEVVLDEK RWPGNEARVG STGVFLSERC WADLAKVGER
     VVPVYAADMS DEGGDGLLHP RSTGYGDSKV RLLNPADQSP GAFIYGDEAK QGYFGSRDLD
     GRSDAGNSAF NSGDMFRNHE TREQMLEKGN EKKMEEVDDA PISGSRKRWI ALVYLLTFYI
     PDFAIKLFGR IKRKDVRMAW REKFAINLII WFSCGVAIFF IVAFPGLVCP TQHVYSAAEL
     SSHNGKDGHS SFIAIRGVVF DLDKFMPGHY PHIVPESALK KYAGVDATGL FPVQVSALCQ
     GKSGSVDPMV LLDYRPTNIS GSATTISGTD TNSVYHDFRH FTNDSRPDWF YEQMVMLKAN
     YLKGYVGYTP KYLNTLGKKS QSIGSINGKV YDLTSYIAGG RLTKAPPGET VPSDVDTDFM
     DNSVVSLFQS LPGQDLSKHW ENLKIDPALR RRMQLCLDNL FFVGHVDTRN SAQCEFARYF
     ILAISVLICS IIVFKFLAAL QFGRKNVPEN LDKFIICQVP AYTEDEESLR RAIDSMARMR
     YDDKRKLLVV ICDGMIIGQG NDRPTPRIVL DILGVPESVD PEPLSFESLG EGQKQHNMGK
     VYSGLYEVQG HIVPFLVIVK VGKPSEVSRP GNRGKRDSQM VLMRFLNRVH YNLPMSPMEL
     EMHHQIRNVI GVNPTFYEFI LQVDADTVVA PDSATRMVAA FLNDTRLIGV CGETALTNAK
     NSAVTMIQVY EYYISHNLTK AFESLFGSVT CLPGCFTMYR IRSAETAKPL FVSKEVVDAY
     AEIRVDTLHM KNLLHLGEDR YLTTLLLKHH SKYKTKYISS AKAWTIAPES WTVFLSQRRR
     WINSTVHNLI ELIPMQQLCG FCCFSMRFVV FVDLLSTVIQ PVTLAYIIYL IYWLVKDTST
     IPYTSLILLA AIYGLQALIF IIRRKWEMVG WMIVYLLALP VFSLALPLYS FWHMDDFTWG
     NTRIITGEKG RKVVISDEGK FDPASIPKKK WEEYQTELWE AQTSRDDRSE VSGISYGTKS
     YHPAQSEYGF PGSRPMSQLD LPRFGSRMSL APSEMMSRHA DMEMENLSHL PSDDAILAEI
     REILRTADLM SVTKKSIKLE LERRFGVNLD LKRPYINSAT EAVLAGAL
//
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