ID   A0A1I8BD69_MELHA        Unreviewed;      1351 AA.
AC   A0A1I8BD69;
DT   18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT   18-JAN-2017, sequence version 1.
DT   03-MAY-2023, entry version 26.
DE   RecName: Full=chitin synthase {ECO:0000256|ARBA:ARBA00012543};
DE            EC=2.4.1.16 {ECO:0000256|ARBA:ARBA00012543};
OS   Meloidogyne hapla (Root-knot nematode worm).
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Tylenchina; Tylenchomorpha; Tylenchoidea; Meloidogynidae; Meloidogyninae;
OC   Meloidogyne.
OX   NCBI_TaxID=6305 {ECO:0000313|Proteomes:UP000095281, ECO:0000313|WBParaSite:MhA1_Contig1895.frz3.fgene1};
RN   [1] {ECO:0000313|WBParaSite:MhA1_Contig1895.frz3.fgene1}
RP   IDENTIFICATION.
RG   WormBaseParasite;
RL   Submitted (NOV-2016) to UniProtKB.
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: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC       pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
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DR   WBParaSite; MhA1_Contig1895.frz3.fgene1; MhA1_Contig1895.frz3.fgene1; MhA1_Contig1895.frz3.fgene1.
DR   OMA; LNTVHIT; -.
DR   Proteomes; UP000095281; Unplaced.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0004100; F:chitin synthase activity; IEA:UniProtKB-EC.
DR   InterPro; IPR004835; Chitin_synth.
DR   InterPro; IPR029044; Nucleotide-diphossugar_trans.
DR   PANTHER; PTHR22914; CHITIN SYNTHASE; 1.
DR   PANTHER; PTHR22914:SF42; CHITIN SYNTHASE; 1.
DR   Pfam; PF03142; Chitin_synth_2; 1.
DR   SUPFAM; SSF53448; Nucleotide-diphospho-sugar transferases; 1.
PE   4: Predicted;
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        6..31
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        52..73
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        79..97
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        835..861
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        873..893
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        899..921
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        933..950
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        962..980
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1132..1154
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   REGION          437..492
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        453..492
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1351 AA;  156136 MW;  FD9F7BC56D4089AB CRC64;
     MFTVESAHAF GLGALVFGIM PHISAITIVQ LGNSLCLIPS LLLPLSRSTN RWLPLLLLID
     SSAIFVQLIS IIWKKYFPIE NFGFIFLCTT LISITWWQNF MHPKSFFPLT RFFAYYAAKL
     RECRSKAYLI ISPWKCLIFT FCMFQFVPPN IPINYLLQKD PFGEQLITIN AYNLNQTQLN
     LFQERMEELQ KMNEGYQIKP KLKLNRKIVE QINNIEKELI NGTIKNNKKI NKINEKKIKE
     KINRERRKVE KKEEVENNNG EDEEEEMDVA AYNIYDDRVE LNQFTTAYDA LWLAFIQIGS
     SLICQLSAKF ACKVVMQRMG LALPVFLSVP ISVIFLSHFC RQKTKDSCYL NDWISKELFW
     QCPSRPLNWH RFWREMPNLL WIGWWLSQSW VTIHLWMPKQ ERLAKSEDLF FLGYFDGPFP
     EQSIALDRRR DDKIRIRSDE IETDDEDDGN GSTHTCESAA SGNSPKPTNG LINANSISSS
     LSNTSQRSDG GLIRESASSA DKICKIYVCA TMWHESELEM GCMLKSIFRL DEIIDPDYYE
     FEAHIYLDDA FELDEYNNPI PNKFVHQLIG SMNEAASSVH QTKLQLRTPK ICITPYGGRI
     SYVLPGRNRL SIHLKNRFLI RQRKRWSQVM YLYFLLGFRL TLRVNDNKRR ELLAENTFIL
     TLDGDVDFQP ECVHLLVDLM RKNRRLGAAC GRIHPRGSGI MIWYQRFEYA VGHWLQKATE
     HMIGCVLCSP GCFSLFRSAA LIDDNVARKY ATKSEKPFHY VQYDQGEDRW LCTLLLQRGY
     RVEYCAASDA LTFAPEGFKE FFNQRRRWIP STMANIIDLL QDYKNVIKVN DSVSIWYIAY
     QLVMLFSSVL GPGTIFLMIV GAISISFNID TRLALLIVTT PVVCFCICCL TCSTDTQLLL
     AQIIGALFAM LMTAVIVGTS LQIQKDGILS PHSIFLFTVL GSWTFSALLH PLEFLCLLPC
     GLYFLAIPCM YMLLPIYSLC NLNTVNWGTR ENNTAFENNK NKIIKEDNGE ISIGCGNFCR
     IVCCVKNSEN SQEPLEKSLK IIEKKLDSLD RRTISRNEIN ENKKEENKKE EEKVKEMDIK
     KWIELKPFNC FEQILLDPDE ESFWHEMIDK YLKPIHSDSQ EQERIQQGLN ELRNTCCSAF
     FMVNSVFIIV VLVLQLQKDC LHIEWPLGPL VNQTRVQCGG GALDPEGEEW VKFLAMLFHR
     FGTITHIIAS TELCCSQQPL DKISEDELVA HNAVEIAREL QAFRGLDINI PQQNNQQYLI
     QTNNLQQNSN NQIFNINQQP TISSNNNLNI FQINKNQNKM DTLDAAFKKR FFALSTNNQQ
     NNQQIFGNKN IGKNFTLRKR TLRAIEQRGN V
//