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Database: UniProt
Entry: A0A151JWD4_9HYME
LinkDB: A0A151JWD4_9HYME
Original site: A0A151JWD4_9HYME 
ID   A0A151JWD4_9HYME        Unreviewed;      1731 AA.
AC   A0A151JWD4;
DT   08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT   08-JUN-2016, sequence version 1.
DT   22-FEB-2023, entry version 24.
DE   RecName: Full=chitin synthase {ECO:0000256|ARBA:ARBA00012543};
DE            EC=2.4.1.16 {ECO:0000256|ARBA:ARBA00012543};
GN   ORFNames=ALC56_07121 {ECO:0000313|EMBL:KYN38507.1};
OS   Trachymyrmex septentrionalis.
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Formicoidea;
OC   Formicidae; Myrmicinae; Trachymyrmex.
OX   NCBI_TaxID=34720 {ECO:0000313|EMBL:KYN38507.1, ECO:0000313|Proteomes:UP000078541};
RN   [1] {ECO:0000313|EMBL:KYN38507.1, ECO:0000313|Proteomes:UP000078541}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Tsep2-gDNA-1 {ECO:0000313|EMBL:KYN38507.1};
RC   TISSUE=Whole body {ECO:0000313|EMBL:KYN38507.1};
RA   Nygaard S., Hu H., Boomsma J., Zhang G.;
RT   "Trachymyrmex septentrionalis WGS genome.";
RL   Submitted (MAR-2016) to the EMBL/GenBank/DDBJ databases.
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   EMBL; KQ981663; KYN38507.1; -; Genomic_DNA.
DR   STRING; 34720.A0A151JWD4; -.
DR   Proteomes; UP000078541; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0004100; F:chitin synthase activity; IEA:UniProtKB-EC.
DR   CDD; cd04190; Chitin_synth_C; 1.
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   Coiled coil {ECO:0000256|SAM:Coils};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000078541};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        81..104
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        137..155
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        175..196
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        202..222
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        234..257
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        263..283
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        304..331
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        386..404
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        416..436
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        473..492
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        926..953
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        959..976
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        983..1006
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1012..1033
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1045..1064
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1084..1107
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1119..1135
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1147..1166
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1386..1405
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1445..1464
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1502..1523
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   REGION          1..35
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1274..1327
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          1179..1209
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        1309..1323
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1731 AA;  195860 MW;  80A9D4214C268FF7 CRC64;
     MAKNQHQNGI IPGAGMVSGP DDFSDGESTP LTQDYGGSQR TIVETKGWDV FRNPPMKTDS
     NSGSMANQKC LERMVQVIKV IVYLFVFVIV LGSGVIAKGT ILFMTSQLRQ DRKMLYCNRQ
     LDRENQYIVT LPEEERIAWI WCIIIAFTVP EFGTLVRSIR MCIFKSWKKP QSMHFLVVSI
     METFHVVGLA LMFLAVLPEL DVVKGAMLTN CVCFVPGLLG LLSRNKSKDD SKRFVLVLVD
     IAALAAQATS FVLWPFLDSS RRSLWLIPLT LILVSCGWWE NYVSMQSRIG LIRSLGRVKK
     EMRLTRYFTY MLVSVWKIMA FFISSILILH IKGDNVGHLF SMLSSAFGDH KITVTSIKSI
     NSGSLPDLSE ILTGDITEVV NADFNTPIYV LLLQIAGAYF AYVFGKFACK ILIQGFSYAF
     PVNLTIPVSI SLLIAACGLR NNDPCFFHGT VPDYLFYESP LPNFLNDFVS KQYAWVWLLW
     LLSQTWITLH IWTPKCERLA ATEKLFVVPM YDSLLIDQSM GLNRRRDDQP EVKVEDLAEI
     EKEKGDGDYE TIYEQTDGST TPPSAVKNSD HVTRIYACAT MWHENKEEMM EFLKSILRLD
     EDQCARRVAQ KYLKVVDPDY YEFETHIFFD DAFELSDHDE NESQVNRFVK LLVGTLDEAA
     SDVHKTRMHV RAPKKYPTPY GGRLVWTLPG KTKMIAHLKD KSKIRHRKRW SQVMYMYYLL
     GHRLMELPIS VDRKEVIAEN TFLLTLDGDI DFQPAAVKLL VDLMKKNKNL GAACGRIHPV
     GSGPMVWYQM FEYAIGHWLQ KATEHMIGCV LCSPGCFSLF RGKALMDDNV MKKYTTKSDE
     ARHYVQYDQG EDRWLCTLLL QRGYRVEYSA ASDAYTHAPE GFNEFYNQRR RWVPSTIANI
     MDLLMDAKRT IKINDNISLP YISYQILLMG GTILGPGTIF LMLVGAFVAA FKIDNWTSFY
     YNIIPILLFM IVCFTCKSNI QLLCAQILST AYAMIMMAVI VGTALQLGED GIGSPSAIFL
     ISLSSSFFIA ACLHPQEFWC IVPGIIYLLS IPSMYLLLIL YSIINLNVVS WGTREVQTKK
     TKKVMIAAVI STIYAIVMIA VIVAFAINIT QDSVMSPNAW FLFLILGEFM IAGLLHPYEI
     NCLLHGLIYY LAVPSMYVLL ITYSLCNLNN ISWGTRETVT KKSNANVELE QEKREAEEAK
     RKAKQKSLLG FLQNGAGNND DDQGSIEISL AGLFKCLLCT HGKPSAEKQQ LVAIAESLEQ
     LGKRLETIER AVDPHSHGRR RASSVGSRTA DHLGAIGEDP EDEEGSETET VTSQNTEGNR
     DGSNFLSRPY WLTDEGVKKG EVDVLSMQEE QFWKDLLEKY LYPIDDDKAE KARIAKDLKD
     LRDQSVFAFF MMNALFVLIV FLLQLNKDLL HIKWPFGIKT NVTYDHTTME TRIAADLIEL
     RNKSVFAFLM FNALFVLIVF LLQLNKDQLH VVWPLGVKTN ITYVEETSEV HISKEYLQLE
     PIGLVFVFFF ALILVIQFTA MLFHRFGTLA HILASTSLDC YKKTKDLSEE ALLSKHAVDI
     VRDLQRLDGI EGDYEEGSGS GPGRRKTIRN LEKSRRKTQA INTLDVAFRQ RFFSMNEGAG
     LSRNMSTRRE AFKAFEGRRN SIMAMRRKSQ MQTLGANNIY GVAGNPLGIQ GRPSRSSQIS
     VKDVFEGHPG ATSGTGHVNA GYEGDDSPVN SLRLQNLGGN QVTWREANSN V
//
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