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Database: UniProt
Entry: A0A2H3IG88_9EURO
LinkDB: A0A2H3IG88_9EURO
Original site: A0A2H3IG88_9EURO 
ID   A0A2H3IG88_9EURO        Unreviewed;      1760 AA.
AC   A0A2H3IG88;
DT   31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT   31-JAN-2018, sequence version 1.
DT   31-JUL-2019, entry version 9.
DE   SubName: Full=Fungal chitin synthase {ECO:0000313|EMBL:PCH02373.1};
GN   ORFNames=PENO1_037830 {ECO:0000313|EMBL:PCH02373.1};
OS   Penicillium sp. 'occitanis'.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX   NCBI_TaxID=290292 {ECO:0000313|EMBL:PCH02373.1, ECO:0000313|Proteomes:UP000218381};
RN   [1] {ECO:0000313|EMBL:PCH02373.1, ECO:0000313|Proteomes:UP000218381}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CL100 {ECO:0000313|EMBL:PCH02373.1,
RC   ECO:0000313|Proteomes:UP000218381};
RX   PubMed=28951729; DOI=10.3389/fmicb.2017.01627;
RA   Bravo-Ruiz G., Sassi A.H., Marcet-Houben M., Di Pietro A.,
RA   Gargouri A., Gabaldon T., Roncero M.I.G.;
RT   "Regulatory Mechanisms of a Highly Pectinolytic Mutant of Penicillium
RT   occitanis and Functional Analysis of a Candidate Gene in the Plant
RT   Pathogen Fusarium oxysporum.";
RL   Front. Microbiol. 8:1627-1627(2017).
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:PCH02373.1}.
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DR   EMBL; NPFK01000084; PCH02373.1; -; Genomic_DNA.
DR   Proteomes; UP000218381; Unassembled WGS sequence.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0016459; C:myosin complex; IEA:InterPro.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR   GO; GO:0003774; F:motor activity; IEA:InterPro.
DR   GO; GO:0016758; F:transferase activity, transferring hexosyl groups; IEA:InterPro.
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; 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; 2.
PE   4: Predicted;
KW   Complete proteome {ECO:0000313|Proteomes:UP000218381};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000218381};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    729    749       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    765    783       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM   1025   1044       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM   1422   1443       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM   1449   1470       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM   1477   1500       Helical. {ECO:0000256|SAM:Phobius}.
FT   DOMAIN      100    603       Myosin motor. {ECO:0000259|SMART:
FT                                SM00242}.
FT   DOMAIN      797    924       Cytochrome b5 heme-binding.
FT                                {ECO:0000259|SMART:SM01117}.
FT   DOMAIN      925   1013       Cytochrome b5 heme-binding.
FT                                {ECO:0000259|SMART:SM01117}.
FT   REGION        1     22       Disordered. {ECO:0000256|SAM:MobiDB-
FT                                lite}.
FT   REGION      338    357       Disordered. {ECO:0000256|SAM:MobiDB-
FT                                lite}.
SQ   SEQUENCE   1760 AA;  195381 MW;  480C3B3DDDB6FC8B CRC64;
     MSNRYSIFST TSNPGLPKSP SQISTTTLLN SLHNSYSTAQ PYPLEAGTSL VVNTWLTVSH
     LNPDGTPGGI VDPQLGQRAW EHARRRAEDG CIVLSTLHRS CPTLLPSFLS VLPLSTPEIL
     YTSLNAIRPF VTAVTPFNPS YSLYSSLAVS YTFTLAGNVT GLTLALSKSG LNLTRGLLDV
     PAEPGYRAFD VFYYLINAES SQAEKEYLDL KEPSTYSILN KSGTYDPPSF LPTADDAAAA
     EDFRSALKAI GIKGAAQRGL LSILAGILKL GNTLGFLVDE EDLEQVCEEA AELLGVDPEA
     LLRGCSTDDR TVLVTGIYEA LVDWVISKAN EAIATQIKAD QENESSDGSG APWHSEDASD
     TVTITVVDIP SPPLGKAAAL QGVFNDEQGI NAEMKEDGVE IVSPGQSVIN EMHNAVAEVE
     ADLGITESVA FREREHFNDK RQGVLERIGV EVEIGGFLRD ILFPDPNEGI TLGKRGRFDL
     AATLGSSRVW YHLAVHPTDD TPETFAASPS TSPWSAGAVS RQLREWRLPE WANRRHKHLD
     FTADFDVEEF VTRYAPLGCK EGKDGVESWI LERGWSNGDV VVGKERIWMR EGAWWEAESM
     LDLKPPGDMP INPFESGYSA TPPNHNGSGF FPAIPIADSS SFIASRDNLL NVNRQSTMSP
     GIARSIAPTN NQTLRSMGGG DYGLGSKGDD YKGDDAYYEA ELNRLAGDDP EFGQRKHIEK
     KKITLGRRLW TALVWTLTFW IPSFALRYIG RMKRPDIRMA WREKVVLVAL ILLFNGVMVF
     WIIEFGTLLC PNKNKVWNEK ELSYNQGDND FYVGVRGTVY DISKFWRTQH SDTTTTTSAT
     NMQWAAGQIL DPYFPVPLTQ GCAAFVSDTS ISLSHNNTDA TPEVNAVHTS GPLQAVTTSA
     LHNITWYADR FLPFMAQYYK GEIVWTRDTI TNQANNDARY WVIINDGVYD LTDYFYTASL
     MNNLDTYDFL PSAVTTLIKQ NMGSDISDKW QNSVQFQNAL TCMKNVFYVG KVDFRQSARC
     TVNNWILLAF TIVVCSVILV KFLAALQFGS KPRPAPQDKF VICQVPAYTE GEDALRKGLD
     SLTALQYDNK RKLICVVCDG MIVGGGNDRP TPKIVLDILG VDPKVDPPAL PFRSVGQGSD
     QLNYGKVYSG LYEFEGNVVP YIVIVKVGKE SEQSKSKPGN RGKRDSQVLL LNFLNRVHHR
     APMSPLELEI FHQINNVIGV DPELYEFLFM VDADTSVKED SLNRLVAACA NDARIAGICG
     ETSLQNEERS WWTMIQVYEY YISHHLSKAF ESLFGSVTCL PGCFCMYRLR TADKGRPLII
     SDKVIKEYSD GDLDTLHKKN LLALGEDRFL TTLMAKHFPT MSYKFIADAF ASTAAPETWS
     VLLSQRRRWI NSTIHNLVEL AALKDLCGFC CFSMRFIVLI DLLGTIILPA TCAYLIYLIY
     LVASHKGDFG IISIVLLAAV YGLQAVLFIL KRQWQHIGWM IIYLCAFPIY SVVLPLYSFW
     KQDDFTWGNT RVVIGEKGDQ RVVAVEDEPF DPRSIPLQRW DDYALANNLP GRRGNAEYGE
     EKQPMHYTDE AAMEMDDFRS TYSSVKPAST ILTGFPGGRG PYMPPQSPAP FGGNNNRNSR
     MSSFTRYTDA PQLGGHAQRH MSMGNISSYQ DTPMNASRLS MPMQSSDNLL GVSGRQRSPL
     GGGYGSRPVS TAMDFRTGPG HGPDDHTIVE AIRQVLSEVD LDNVTKKQVR ALVEQRLQTE
     LTGDRRTFVD SQIDQELANM
//
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