ID A0A162UW18_PHYB8 Unreviewed; 969 AA.
AC A0A162UW18;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 24-JAN-2024, entry version 31.
DE RecName: Full=chitin synthase {ECO:0000256|ARBA:ARBA00012543};
DE EC=2.4.1.16 {ECO:0000256|ARBA:ARBA00012543};
GN ORFNames=PHYBLDRAFT_154371 {ECO:0000313|EMBL:OAD78363.1};
OS Phycomyces blakesleeanus (strain ATCC 8743b / DSM 1359 / FGSC 10004 / NBRC
OS 33097 / NRRL 1555).
OC Eukaryota; Fungi; Fungi incertae sedis; Mucoromycota; Mucoromycotina;
OC Mucoromycetes; Mucorales; Phycomycetaceae; Phycomyces.
OX NCBI_TaxID=763407 {ECO:0000313|EMBL:OAD78363.1, ECO:0000313|Proteomes:UP000077315};
RN [1] {ECO:0000313|Proteomes:UP000077315}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL 1555(-) {ECO:0000313|Proteomes:UP000077315};
RG DOE Joint Genome Institute;
RA Corrochano L.M., Kuo A., Marcet-Houben M., Polaino S., Salamov A.,
RA Villalobos J.M., Alvarez M.I., Avalos J., Benito E.P., Benoit I.,
RA Burger G., Camino L.P., Canovas D., Cerda-Olmedo E., Cheng J.-F.,
RA Dominguez A., Elias M., Eslava A.P., Glaser F., Grimwood J., Gutierrez G.,
RA Heitman J., Henrissat B., Iturriaga E.A., Lang B.F., Lavin J.L., Lee S.,
RA Li W., Lindquist E., Lopez-Garcia S., Luque E.M., Marcos A.T., Martin J.,
RA McCluskey K., Medina H.R., Miralles-Duran A., Miyazaki A., Munoz-Torres E.,
RA Oguiza J.A., Ohm R., Olmedo M., Orejas M., Ortiz-Castellanos L.,
RA Pisabarro A.G., Rodriguez-Romero J., Ruiz-Herrera J., Ruiz-Vazquez R.,
RA Sanz C., Schackwitz W., Schmutz J., Shahriari M., Shelest E.,
RA Silva-Franco F., Soanes D., Syed K., Tagua V.G., Talbot N.J., Thon M.,
RA De vries R.P., Wiebenga A., Yadav J.S., Braun E.L., Baker S., Garre V.,
RA Horwitz B., Torres-Martinez S., Idnurm A., Herrera-Estrella A.,
RA Gabaldon T., Grigoriev I.V.;
RT "Expansion of signal transduction pathways in fungi by whole-genome
RT duplication.";
RL Submitted (JUN-2015) 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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; KV440973; OAD78363.1; -; Genomic_DNA.
DR RefSeq; XP_018296403.1; XM_018433319.1.
DR AlphaFoldDB; A0A162UW18; -.
DR STRING; 763407.A0A162UW18; -.
DR GeneID; 28994225; -.
DR VEuPathDB; FungiDB:PHYBL_154371; -.
DR InParanoid; A0A162UW18; -.
DR OrthoDB; 1331060at2759; -.
DR Proteomes; UP000077315; 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; 2.
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; 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 SMART; SM01117; Cyt-b5; 2.
DR SUPFAM; SSF55856; Cytochrome b5-like heme/steroid binding domain; 1.
DR SUPFAM; SSF53448; Nucleotide-diphospho-sugar transferases; 1.
DR PROSITE; PS50255; CYTOCHROME_B5_2; 1.
PE 4: Predicted;
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000077315};
KW Transferase {ECO:0000313|EMBL:OAD78363.1};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 24..41
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 62..81
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 326..348
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 725..746
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 752..773
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 780..803
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 89..149
FT /note="Cytochrome b5 heme-binding"
FT /evidence="ECO:0000259|PROSITE:PS50255"
FT REGION 920..946
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 969 AA; 110679 MW; E7B5E4E3080E50B0 CRC64;
MVEDYRVQPE EQVEEVPITR VRRYWSRFVW IATWWIPSWS LRWIGRMHRQ DVRMAWREKV
TLCLLIFLLS GSIIFFIVGL GEVICQGTKE IYSAEDVTNH QTINDYWVSI HGKVFDMTKF
VATDHGSSSY MAGKINMEPL AGRDLSHTFP TPLTTACAGL VTDDSVIVTP NETIVLGAFV
HYSSAQQPDK NLEKLRDPNW TTRYFNPMMN QYKKGDLVIP MKQIKSDYSS WGRLIAVMDQ
KVYDITDYMA TAHQYPIDSP GVPNYHYLDS SLEMVFKKYG GSDITEQWKK VSAFMNDSTR
AQNQACLDNA FYIGRLDYRD SLRCTFVNYL LLSFAVVMSL VILVKFLAAL QFGGAPTPED
HDKFVICQVP CYTEDEESLR KTIDSLTAMT YDDKRKLMFL IADGMIIGGG NDKPTPQILL
AILGHTTDGP DVEPLMFKSI GEGSKQLNYG KVYSGLYENE GHVVPYIVVV KVGKATERTK
PGNRGKRDSQ IICMNFLNKV HFDSEMTPLE LEIYYHIKQI IGVDPSLYEY ILMVDSDTEV
YPDALNRMIA CMLHDSRIIG LCGETELGNE DRSWTTMIQV YEYYISHHLV KAFESLFGSV
TCLPGCFCMY RIRTANKRQP LIVAPAVIHG YSDNQVDTLH KKNLLHLGED RYLTTLMMKN
FPQYKMMFTP YAKCRTVAPD EWSVLLSQRR RWINSTIHNL LELILLQELC GFCCFSMRFV
VIIDLIGTIT LPSSVIYLAY LIYIATSGTG PIPVIALGML AGVYGLQALI FIIKRQWQHI
GWMVIYIAAI PIFSFFIPLY SFWHFDDFSW GNTRVVVGDK TKQIIVTDDE KFDERMIPLK
TWAVYEQEQW EKTQTNTTRS RRKSASFCQD TDSIVTRSSG SARSGVSAED RPPFLPPLIT
GLSEQRLSEF SVDLSAVLHS ATHGKERRGE EEGEGKTVSL PEDEDMEREI HRILATANLM
TLTKKQGKE
//
