ID A0A163MQN1_ABSGL Unreviewed; 1425 AA.
AC A0A163MQN1;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 27-MAR-2024, entry version 37.
DE RecName: Full=chitin synthase {ECO:0000256|ARBA:ARBA00012543};
DE EC=2.4.1.16 {ECO:0000256|ARBA:ARBA00012543};
GN Name=ABSGL_13264.1 scaffold 13659 {ECO:0000313|EMBL:SAM07621.1};
OS Absidia glauca (Pin mould).
OC Eukaryota; Fungi; Fungi incertae sedis; Mucoromycota; Mucoromycotina;
OC Mucoromycetes; Mucorales; Cunninghamellaceae; Absidia.
OX NCBI_TaxID=4829 {ECO:0000313|EMBL:SAM07621.1};
RN [1] {ECO:0000313|EMBL:SAM07621.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 101.48 {ECO:0000313|EMBL:SAM07621.1};
RA Evans L.H., Alamgir A., Owens N., Weber N.D., Virtaneva K., Barbian K.,
RA Babar A., Rosenke K.;
RL Submitted (APR-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; LT554760; SAM07621.1; -; Genomic_DNA.
DR STRING; 4829.A0A163MQN1; -.
DR InParanoid; A0A163MQN1; -.
DR OMA; YFVIRRQ; -.
DR OrthoDB; 1351804at2759; -.
DR Proteomes; UP000078561; Unassembled WGS sequence.
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:SF41; CHITIN SYNTHASE; 1.
DR Pfam; PF03142; Chitin_synth_2; 2.
DR SUPFAM; SSF53448; Nucleotide-diphospho-sugar transferases; 1.
PE 4: Predicted;
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000078561};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 14..34
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 46..65
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 829..857
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 869..887
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 894..918
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT REGION 654..718
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1053..1074
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1114..1204
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1255..1291
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1315..1359
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 654..677
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 700..718
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1115..1131
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1140..1168
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1255..1277
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1320..1336
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1425 AA; 161563 MW; 61280B864BABEC3B CRC64;
MHVPTTRRLL WVTLSRLITF VFPDFILHYV FNLHSHAVRR AWREKITLVV IFLSCAIFLC
FWLEYISALF CDRNKYYSAS SVFSNSSHLA GLRNNAIDWN GATSAMAKQV SQYSGYDVSP
MFPTFMGLQR NLSFDPDPPY SDSVYRRCIA NFGMASKADR WLDFKLENDR GYSFNNGELV
SCPYPNQINT TGAPCYYSFE DQVEEMSLGT KGSIIYDSGD ILKNYSSLPT TSTPGKGFVI
LDNKILDVTS YLVSATNVVL VANNMHSRAF AIDRMFLPLD LTTVLYLKLG QDITPYFDKR
NLTSQPDIYR QCLQDLFQVG ITDAGKVEEC LRINPALWAT MGLGLLYFLT KMNLANLSRL
KWVQRSLFKS NPEVSMTGNS RIWPLTLLLI PCYAETADTI RDTLNSLART NYEDSRKMLV
FVCDGLAQSA QDTKETYVCV LEALGCSATA QATTSHAYVS LGQHHRKINF AKVYSGFYET
GRNRVPFMVI VKVGAPREVS VGRAPGNRGK RDSMVLVLGF LERCTNLASN RMTPLEYELF
NQCYNVLGID PRRFKYMLVT DADTQVQNDV VHKLVTRLER DRRMLAVSGH IRPANPEQNL
ITMLQIFPLY MTFFTGLAYE ACLGNVLTIN GGLVMYKLWT EILPSSTPLG GTAFGSRQQR
FSKSQTTSQS SIRSKWPKVS DEIQFDNDDD DPFATLPKDT AVRPQSTNAG DSMSDRPSFI
TGRESQLSLS PNTSTRSCCI HPTVLRSFAA PQADTLHMKN VLLLGEDQYF GTVLLRSHPH
HHLGFEPDAV GYATIPTNYW ALQALQSRNI RASFHNQVEM TRAARHIGFA AWFLSVTKIL
DMIFSMPIIV YLYGVFIRCF MRRGSAYDII AYSFCALFFL HIVYFVIRRQ FKYVLWFILY
CLLSVPLFAI WFPLVAIWCD DYAETWYDVW PTVGGWRWFD RLHGCVDDDY SRRIEQRHHK
KEPQQRDGSK EDKPAFDDMG HRINDYSYNI HASTRSEQDD DDSVVRMQLN EYEAIEAQRA
YERATEEAAA LDAKFAGFTA FGQSQSLMKP TMEIDTPPSP LAQPKDDNAS FRGTTSGYRS
VVDLYGTIRT KRYGEKMNPG DLDNDLLPRF RLADRRSTSS PTDSLATNPF ADSHDNPFDD
GYAITTSNNN NSSNSSTESP TSSSMYPLGE VLTHFHQPPS HQHRRQHYQQ HKPSHSQSSY
FSNRSSRSYD YYTNAPGMFI PMEETHSATP GNDEHNFGHY RSYSAESVIP TPTDRRSIVS
QAPTTDSCLS FDPETTLESR SGLEEDEDGR SMAIHGRVGL KIPERTAAAL TAAVYRQRQA
SHSKNDDTDG RRYPTQHHPL RRSSSRNHQR NTSDTSQHNV ASFADLIQAE IRSYLSRADL
DSTTRAQVKE HLATTLGDRT RADALQDMIN QCIEATTLEL LADQP
//
