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Database: UniProt
Entry: C0NSP8_AJECG
LinkDB: C0NSP8_AJECG
Original site: C0NSP8_AJECG 
ID   C0NSP8_AJECG            Unreviewed;      1866 AA.
AC   C0NSP8;
DT   05-MAY-2009, integrated into UniProtKB/TrEMBL.
DT   05-MAY-2009, sequence version 1.
DT   31-JUL-2019, entry version 57.
DE   SubName: Full=Chitin synthase {ECO:0000313|EMBL:EEH05914.1};
GN   ORFNames=HCBG_06178 {ECO:0000313|EMBL:EEH05914.1};
OS   Ajellomyces capsulatus (strain G186AR / H82 / ATCC MYA-2454 / RMSCC
OS   2432) (Darling's disease fungus) (Histoplasma capsulatum).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Onygenales; Ajellomycetaceae; Histoplasma.
OX   NCBI_TaxID=447093 {ECO:0000313|EMBL:EEH05914.1, ECO:0000313|Proteomes:UP000001631};
RN   [1] {ECO:0000313|Proteomes:UP000001631}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=G186AR / H82 / ATCC MYA-2454 / RMSCC 2432
RC   {ECO:0000313|Proteomes:UP000001631};
RA   Champion M., Cuomo C.A., Ma L.-J., Henn M.R., Sil A., Goldman B.,
RA   Young S.K., Kodira C.D., Zeng Q., Koehrsen M., Alvarado L., Berlin A.,
RA   Borenstein D., Chen Z., Engels R., Freedman E., Gellesch M.,
RA   Goldberg J., Griggs A., Gujja S., Heiman D., Hepburn T., Howarth C.,
RA   Jen D., Larson L., Lewis B., Mehta T., Park D., Pearson M.,
RA   Roberts A., Saif S., Shea T., Shenoy N., Sisk P., Stolte C., Sykes S.,
RA   Walk T., White J., Yandava C., Klein B., McEwen J.G., Puccia R.,
RA   Goldman G.H., Felipe M.S., Nino-Vega G., San-Blas G., Taylor J.,
RA   Mendoza L., Galagan J.E., Nusbaum C., Birren B.W.;
RT   "The genome sequence of Ajellomyces capsulatus strain G186AR.";
RL   Submitted (FEB-2009) to the EMBL/GenBank/DDBJ databases.
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}.
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DR   EMBL; GG663370; EEH05914.1; -; Genomic_DNA.
DR   EnsemblFungi; EEH05914; EEH05914; HCBG_06178.
DR   InParanoid; C0NSP8; -.
DR   OrthoDB; 20724at2759; -.
DR   Proteomes; UP000001631; Unassembled WGS sequence.
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:0003774; F:motor activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0016758; F:transferase activity, transferring hexosyl groups; IEA:InterPro.
DR   CDD; cd14879; MYSc_Myo17; 1.
DR   Gene3D; 3.10.120.10; -; 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:UP000001631};
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:UP000001631};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    908    927       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    947    967       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM   1213   1235       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM   1611   1633       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM   1639   1659       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM   1666   1689       Helical. {ECO:0000256|SAM:Phobius}.
FT   DOMAIN        1    798       Myosin motor. {ECO:0000259|PROSITE:
FT                                PS51456}.
FT   DOMAIN      971   1029       Cytochrome b5 heme-binding.
FT                                {ECO:0000259|PROSITE:PS50255}.
FT   NP_BIND     104    111       ATP. {ECO:0000256|PROSITE-ProRule:
FT                                PRU00782}.
FT   REGION        1     22       Disordered. {ECO:0000256|SAM:MobiDB-
FT                                lite}.
FT   REGION      594    664       Disordered. {ECO:0000256|SAM:MobiDB-
FT                                lite}.
FT   COMPBIAS    614    641       Polyampholyte. {ECO:0000256|SAM:MobiDB-
FT                                lite}.
FT   COMPBIAS    644    664       Polar. {ECO:0000256|SAM:MobiDB-lite}.
SQ   SEQUENCE   1866 AA;  207464 MW;  72089E3CF4C94C5B CRC64;
     MALHSLTGTG SVPAHAQSSL PSLPAHLQSD THLTAHLASR FHVSLPTARL SSQGLICLNT
     YTSSTRGPDG QREGSAMGEA DDLARRAWAR LGGRGENQAV IFLGETGSGK TTVRSHLLSS
     FLSLSSTPLS AKLSLAAFVF DTLTTTKSVT TPTASKAGLF FELQYDASST LNPTLIGGKL
     LDHRLERSRI ASVPTGERSF HVLYYLLAGT SAAEKAHLGL DSSVDIRTGG NTGNHSSGTI
     SHKRWRYLGH PTQLKVGIND TEGFQQFKNA LRKLEFPRSE IAEICQILAC ILHIGQLEFT
     TGQSTTTGPE ESGGYSHEGG ETVTIVKNKD ALAIIAAFLG LSVDDLETSL GYKTKTIHRE
     RVTVMLDPKG ARSNADDLAR TLYALLVAYV IENINQRVCA AEDAVANTIS IIDFPGFSQT
     SATGSTLDQL LNNAATESLY NYCLRNFFDH KAEILEAEEV SVPPTSYFDN SDAVKALLKQ
     GNGILTILDD QTKRGRSDMQ LLESLRKRFA NKNPAISVGS STATLPGSNF ASKNEAATFT
     VRHFAGEVDY PVQGLVEENS DLVSGDLMNL ITSSRSAFVR DLFGQEALQT IRHPKEKSAI
     MQAQVSSKPL RMPSMARRKM DRPPRLTARA TQADKDIDDD TGASLTSVPG SKKRKQGDST
     NGPGQSAAAQ FLVSLDNINK SLAADNVNSY FVFCLKPNDR RIANQFDSKC VRSQVQTFGI
     AEISQRLRNA DFSVFLPFSE FLGLSDAESI IVGSEQEKCQ LVVDEKRWPG NEARVGSTGV
     FLSERCWADI ARVGERVLPS YSGDGTDDDK DGLLGVGQKA PYGDSKVRLL NSPDVSPLPG
     SYIYGDETKQ PFYGVRDIDG RSDAGASAFN SGDMFKNLET REQMAEKGNE KKMEEVDDVV
     VSGSRKRWLA IVYLLTFYIP DFTIKLIGRM KRKDVRIAWR EKFAINLLIW FSCALAVFFI
     IGFPQLICPK QYVFSPDELS SRDGKKNDAY IAIRGEVFDL GAFIPSHYPK IVPRKSLEKY
     AGLDATKLFP VQVSALCDGV DGQVDPSVPL DFRSTNRTGS VKVSRDDDPN AQYHDFRAFT
     DDYRPDWYWN QMRMLRANYK KGYVGYSPQY LKTLVDKDQA IAVLDGYVYD LTNYVIGGRR
     PRPPPGQQAP KDVNVNFMDP LVVNLFQQRP GQDITEDFNR LPLGKREQAM RTCLANLFQV
     GKLDTRSSAQ CQFAQYFILA ISLLLVTIIG FKFFAALQFG KKNLPENLDK FIICQVPAYT
     EDEESLRRAI DSMARMRYDD KRKLLVVICD GMIIGQGNDR PTPRIVLDIL GVSDTVDPEP
     LSFESLGEGM KQHNMGKVYS GLYEVQGHIV PFLVVVKVGK PSEVSRPGNR GKRDSQMLLM
     RFLNRIHYNH PMSPLELEIH HQIRNIIGVN PTFYEFILQV DADTMVAPDS ATRMVASFLQ
     DTRIIGLCGE TGLNNAKSSI ITMIQVYEYY ISHNLTKAFE SLFGSVTCLP GCFTMYRIRA
     ADTGKPLFVS REVVEAYAEI RVDTLHMKNL LHLGEDRYLT TLLLKHHPKY KTKFLFNAHA
     WTIAPDSWAV FMSQRRRWIN STVHNLIELI PLQQLCGFCC FSMRFVVFVD LLSTVIQPVT
     VAYVIYLIVL IAINPSLIPI TAFILLGAIY GLQAIIFIVR RKWEMVGWMI IYILAMPVFS
     LGLPLYSFWH MDDFTWGNTR IVTGEKGRKV VISDEGKFDP ASIPKKKWEE YQIELWEAQT
     QQDDRSEVSG ISYGTRSYHP PASEYGFAAS RPVSQVELNR FAGSRMSLSP SEMLGTGPDM
     EMVDLTGLPS DDSLLAEIRD ILRTADLMTV TKKSVKLELE QRFNINLDAK RQYINSATEA
     VLSGQL
//
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