ID A0A163JDV8_ABSGL Unreviewed; 1276 AA.
AC A0A163JDV8;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE RecName: Full=chitin synthase {ECO:0000256|ARBA:ARBA00012543};
DE EC=2.4.1.16 {ECO:0000256|ARBA:ARBA00012543};
GN Name=ABSGL_04269.1 scaffold 5264 {ECO:0000313|EMBL:SAL98713.1};
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:SAL98713.1};
RN [1] {ECO:0000313|EMBL:SAL98713.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 101.48 {ECO:0000313|EMBL:SAL98713.1};
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; LT552303; SAL98713.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A163JDV8; -.
DR STRING; 4829.A0A163JDV8; -.
DR InParanoid; A0A163JDV8; -.
DR OMA; ISIGCMA; -.
DR OrthoDB; 1331060at2759; -.
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:SF16; CHITIN SYNTHASE 3; 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 190..206
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 226..245
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 491..518
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1020..1039
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1046..1063
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1069..1095
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT REGION 1..140
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 163..182
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1198..1276
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..28
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 40..69
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 70..95
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1199..1243
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1244..1270
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1276 AA; 141375 MW; 8E1CBC3D290652F6 CRC64;
MARPVSTQKA SYQPALNREL SFSSSSDMEE AIGLPAMSSG GIPYNNNDDD NRQEQQGKQQ
QQQQTPKRTK SLVRPERERI DKTHRQYHYR QAANKQDPDK VAPSTTGHLP ARSVERQATT
TDHRGLGGGD ASTTLIGTST DVTGADSTGL LLRRGKSILG REEKQTWEED EASDTVDSDK
DNKRKWPSPW YAYCLLITLC IPKPMLRCAG IPDGPAQSAW REKIGLVSLI ILVMAFVGFL
TFGFTQAVCP IPPTSVHGGE VSNGYLIIHG WAYMLSDWNG HPAIPGVTED SKTNVLYPPL
NGGGMDASFL FQQQVDTSAC KNVLTSKQGD QSVYFPCQLF SPNSTVPPPS SQFSNHTSCH
ISATATQQFN AFYNDGVPKT NDGGGFNKAA RVYYNWEDLT QENQYMAYNG DVLNLKLLQS
LPSEYFGTLQ GGLIQSIINN GSEFAGKDMT TSIQGYRQPD SRWEEEAACL QSLIKIGSID
TFSIGCIASD IVLYVSLVVI LAVIFIKFSM AVIFGWFLSW KLGHFNEDKD YAARMRREAE
IENWTRNMDA SAPYAALQPN NPYNNKKQNR KTLLPQTSRY TKPEHGMHHF DINGMGGGSP
SSVSVAALAN NSSTWNPSAP NPPFMSRSSM ISLPNGFGSN RPNSAFFGSN RPNSAFFGGA
SSPRLSYYEN ASRNRLSALS TPRLSSASLS LSSGGESNNS GSLKCPLPVS PFANPQPPAD
FMPFNFVLAP TICLVTCYSE GEDGIRTTLD SVAVSDYPNS HKLLLVICDG IITGHGNSKS
TPEVCVDMMR DLIVPADQVE AYPYIAIADG QKKNNMAKVY AGFYKFDDTT VDPSLQQRVP
MITIVKCGTP EEAATAGKPG NRGKRDSQMV LMQFMQKVIF DERMTRMEYE LFNSFWQISN
LPADAFELCL MVDADTKLYP DALTRLVSCA VKDPSISGLC DRYLSTLMLK TFPNRKMMFV
PQAVCKTVVP DTFMVLLSQR RRWINSTIHN LMELLFVNDL CGTFCFSMQF VVFIDLVGTL
ALPAAITFTL YLIICALIGR PSVISLILLA LILGLPGVLI MMTSRKIVYV GWMLLYLISL
PVWNFVLPMY AYWHFDDFSW GDTRKVEGEQ KGGGHGDKEG EFDASVFTMK RWHEFERERR
IQYAIDHQLP APRFMERPRS EAFRDSMMIL RRPRQGSLNS NESDWPLAHM AVVPAGMLDT
PSPSSSPSSY FNGASASRTI PSNHSGNNSS TNSNNTSSNV PSKMRHELQE DLVEEVPLSD
MHHHHHDNPP PSPPSK
//
