ID   A0A2G5B3J6_COERN        Unreviewed;      1008 AA.
AC   A0A2G5B3J6;
DT   31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT   31-JAN-2018, sequence version 1.
DT   28-JUN-2023, entry version 21.
DE   RecName: Full=chitin synthase {ECO:0000256|ARBA:ARBA00012543};
DE            EC=2.4.1.16 {ECO:0000256|ARBA:ARBA00012543};
GN   ORFNames=COEREDRAFT_94493 {ECO:0000313|EMBL:PIA13574.1};
OS   Coemansia reversa (strain ATCC 12441 / NRRL 1564).
OC   Eukaryota; Fungi; Fungi incertae sedis; Zoopagomycota; Kickxellomycotina;
OC   Kickxellomycetes; Kickxellales; Kickxellaceae; Coemansia.
OX   NCBI_TaxID=763665 {ECO:0000313|EMBL:PIA13574.1, ECO:0000313|Proteomes:UP000242474};
RN   [1] {ECO:0000313|EMBL:PIA13574.1, ECO:0000313|Proteomes:UP000242474}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NRRL 1564 {ECO:0000313|EMBL:PIA13574.1,
RC   ECO:0000313|Proteomes:UP000242474};
RX   PubMed=25977457; DOI=10.1093/gbe/evv090;
RA   Chang Y., Wang S., Sekimoto S., Aerts A.L., Choi C., Clum A., LaButti K.M.,
RA   Lindquist E.A., Yee Ngan C., Ohm R.A., Salamov A.A., Grigoriev I.V.,
RA   Spatafora J.W., Berbee M.L.;
RT   "Phylogenomic Analyses Indicate that Early Fungi Evolved Digesting Cell
RT   Walls of Algal Ancestors of Land Plants.";
RL   Genome Biol. Evol. 7:1590-1601(2015).
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; KZ303532; PIA13574.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2G5B3J6; -.
DR   STRING; 763665.A0A2G5B3J6; -.
DR   OrthoDB; 1331060at2759; -.
DR   Proteomes; UP000242474; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0004100; F:chitin synthase activity; IEA:UniProtKB-EC.
DR   Gene3D; 3.10.120.10; Cytochrome b5-like heme/steroid binding domain; 1.
DR   Gene3D; 1.10.10.60; Homeodomain-like; 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; IPR029044; Nucleotide-diphossugar_trans.
DR   PANTHER; PTHR22914; CHITIN SYNTHASE; 1.
DR   PANTHER; PTHR22914:SF13; CHITIN SYNTHASE; 1.
DR   Pfam; PF03142; Chitin_synth_2; 1.
DR   Pfam; PF00173; Cyt-b5; 1.
DR   Pfam; PF08766; DEK_C; 1.
DR   SMART; SM01117; Cyt-b5; 2.
DR   SUPFAM; SSF55856; Cytochrome b5-like heme/steroid binding domain; 1.
DR   SUPFAM; SSF109715; DEK C-terminal domain; 1.
DR   SUPFAM; SSF53448; Nucleotide-diphospho-sugar transferases; 1.
DR   PROSITE; PS50255; CYTOCHROME_B5_2; 1.
DR   PROSITE; PS51998; DEK_C; 1.
PE   4: Predicted;
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000242474};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        25..49
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        294..313
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        682..709
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        715..736
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        743..766
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          53..113
FT                   /note="Cytochrome b5 heme-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS50255"
FT   DOMAIN          950..1005
FT                   /note="DEK-C"
FT                   /evidence="ECO:0000259|PROSITE:PS51998"
SQ   SEQUENCE   1008 AA;  114849 MW;  A4B668DFE74DAA71 CRC64;
     MIPDWLMNCC GLKREDIRMA WREKVAICLI IVLMWCAVLF FIIGLGLIMC PKQYVYNMDE
     VADHTERSDA YVAMRGRVYD ITNFLNQEHG KSRGGASPED MIIYSGQDIN ASFPLSLRAA
     CPELVPAKDD PNWLMYLKSD IETEATFPFV HKAGSLANSK MMMRQDFYHK FVLPKMRMLK
     VGDVVWELDY IKSLHHKGGM YWRVINGEVF NLSPYFMTRD APENADQKKW KFLHRLVESI
     FEDAGARDTD ITKYWKMLPL NRATRRANYK CLKNMFYVGK VDTRHSFRCL FPNFLLLAAA
     CLLMLVILIK FLASLQLSSR RKPQKHDKFI ICQVPCYTEG ESSLRRTIDS LATLGYDDKH
     RLLFIICDGN IVGSGNDRPT PRIVLDILGV DPKLDPPARS FRSIGEGGQQ HNMAKVYSGL
     YEYEGHVVPY LVVAKIGKPT EKSRPGNRGK RDSQMLLLHF LNRVHFESGM SPLDLEIFHQ
     MKNVIGVHPS LYEYLMMVDA DTEVMPDSLT RLVACMVHDA KVIGICGETQ LTNEDFSWTT
     MIQVYEYFIS HHMAKAFESL FGSVTCLPGC FCMYRLRTGR GMPLIISKNV INDYSENHVD
     TLHKKNLLSL GEDRYLTTLM MKYFPQFKMT FTADAKCKTT APDTWSILLS QRRRWINSTV
     HNLVELVFLP EMCGFCCFSM RFVVFIDLFG TLTMPCTLIY LAYLAYLAIT KIADIGYISL
     ILIGAIYGLQ AVIFVLKRQW QHIGWMIIYL LAYPLWSFFI PVYAFWHMDD FSWGNTRIVV
     GEDGKRQIFV KDEEPFNPDE IQMKTWAEYE DEIFKRQIQA KELEEVGQAI DEFGNSGVRP
     VSRFTHITGL DTAGHQHQMI STDMQMGAPY GYGNNNGSGA MSFQQMQQPI GMPGGNPATL
     SHTPALGGVQ GGRPYSSAGF SAYFGSMFNM PQQPVATSSY NLIQASDGQM PSDHAIVSGI
     STILESSDLS TVTMKQVRDE LSRMFGIDLS SRREFINNTV QSMIQHTG
//