ID A0A1Q5UKN6_9EURO Unreviewed; 1862 AA.
AC A0A1Q5UKN6;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE RecName: Full=chitin synthase {ECO:0000256|ARBA:ARBA00012543};
DE EC=2.4.1.16 {ECO:0000256|ARBA:ARBA00012543};
GN ORFNames=PENSUB_1146 {ECO:0000313|EMBL:OKP13046.1};
OS Penicillium subrubescens.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX NCBI_TaxID=1316194 {ECO:0000313|EMBL:OKP13046.1, ECO:0000313|Proteomes:UP000186955};
RN [1] {ECO:0000313|EMBL:OKP13046.1, ECO:0000313|Proteomes:UP000186955}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 132785 {ECO:0000313|EMBL:OKP13046.1,
RC ECO:0000313|Proteomes:UP000186955};
RA De Vries R.P., Peng M., Dilokpimol A., Hilden K., Makela M.R.,
RA Grigoriev I., Riley R., Granchi Z.;
RT "Genome sequence of the ascomycete fungus Penicillium subrubescens.";
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Polymerizes chitin, a structural polymer of the cell wall and
CC septum, by transferring the sugar moiety of UDP-GlcNAc to the non-
CC reducing end of the growing chitin polymer.
CC {ECO:0000256|ARBA:ARBA00024009}.
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: Cell membrane {ECO:0000256|ARBA:ARBA00004651};
CC Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651}. Membrane
CC {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: Belongs to the TRAFAC class myosin-kinesin ATPase
CC superfamily. Myosin family. {ECO:0000256|PROSITE-ProRule:PRU00782}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00782}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:OKP13046.1}.
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DR EMBL; MNBE01000157; OKP13046.1; -; Genomic_DNA.
DR STRING; 1316194.A0A1Q5UKN6; -.
DR OrthoDB; 1331060at2759; -.
DR Proteomes; UP000186955; Unassembled WGS sequence.
DR GO; GO:0016459; C:myosin complex; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0003779; F:actin binding; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004100; F:chitin synthase activity; IEA:UniProtKB-EC.
DR GO; GO:0003774; F:cytoskeletal motor activity; IEA:UniProtKB-UniRule.
DR GO; GO:0048315; P:conidium formation; IEA:UniProt.
DR CDD; cd14879; MYSc_Myo17; 1.
DR Gene3D; 1.20.58.530; -; 1.
DR Gene3D; 3.10.120.10; Cytochrome b5-like heme/steroid binding domain; 1.
DR Gene3D; 1.10.10.60; Homeodomain-like; 1.
DR Gene3D; 3.40.850.10; Kinesin motor domain; 1.
DR Gene3D; 1.20.120.720; Myosin VI head, motor domain, U50 subdomain; 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; IPR036961; Kinesin_motor_dom_sf.
DR InterPro; IPR001609; Myosin_head_motor_dom.
DR InterPro; IPR036037; MYSc_Myo17.
DR InterPro; IPR029044; Nucleotide-diphossugar_trans.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR22914; CHITIN SYNTHASE; 1.
DR PANTHER; PTHR22914:SF45; CHITIN SYNTHASE; 1.
DR Pfam; PF03142; Chitin_synth_2; 1.
DR Pfam; PF00173; Cyt-b5; 1.
DR Pfam; PF08766; DEK_C; 1.
DR Pfam; PF00063; Myosin_head; 1.
DR SMART; SM01117; Cyt-b5; 2.
DR SMART; SM00242; MYSc; 1.
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 SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR PROSITE; PS50255; CYTOCHROME_B5_2; 1.
DR PROSITE; PS51998; DEK_C; 1.
DR PROSITE; PS51456; MYOSIN_MOTOR; 1.
PE 3: Inferred from homology;
KW Actin-binding {ECO:0000256|PROSITE-ProRule:PRU00782};
KW ATP-binding {ECO:0000256|PROSITE-ProRule:PRU00782};
KW Glycosyltransferase {ECO:0000256|ARBA:ARBA00022676};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Motor protein {ECO:0000256|ARBA:ARBA00023175, ECO:0000256|PROSITE-
KW ProRule:PRU00782};
KW Myosin {ECO:0000256|ARBA:ARBA00023123, ECO:0000256|PROSITE-
KW ProRule:PRU00782};
KW Nucleotide-binding {ECO:0000256|PROSITE-ProRule:PRU00782};
KW Reference proteome {ECO:0000313|Proteomes:UP000186955};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 892..911
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 932..951
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1201..1223
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1599..1620
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1626..1647
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1654..1677
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 1..785
FT /note="Myosin motor"
FT /evidence="ECO:0000259|PROSITE:PS51456"
FT DOMAIN 955..1014
FT /note="Cytochrome b5 heme-binding"
FT /evidence="ECO:0000259|PROSITE:PS50255"
FT DOMAIN 1804..1859
FT /note="DEK-C"
FT /evidence="ECO:0000259|PROSITE:PS51998"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 596..649
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 605..636
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 101..108
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00782"
SQ SEQUENCE 1862 AA; 207509 MW; 72F638D1CAD2EE30 CRC64;
MAGNTTGNAP AHAQSSLPSL PAHLQSDTHL TAHLASRFHV GLPTARLSSQ ALISFNTYTS
ATKGPDGEKE GSAAGEAEDL ARRAFTRLGA RGENQAVVFL GESGSGKTTI RSHLLSSFLS
FSSTPLSSKL SYAAFVFDTL TTTKSVTTPT ASKAGLFLEL QYDGSSSVNP TLIGGKIIDY
RLERSRISSV PTGERSFHVL YYLLAGTSAA EKSHLGFDNS IHINTGGKLS SDSVSHKRWR
YLGHPTQLKV GVNDHEGFQH FKTALRKLEF SRGEIAEICQ ILASILHIGQ LDFMSGQSTT
TTAEESGGYS HEGGETVTVV RNKDALGNVA AFLGLSVEAL ENSLGYKTKS IHRERVTVML
DPRGARENAD AFARTIYSLL VTYVIETVNQ KICAAEDSVA NTISIVDFPG FAQAPATGST
LDQLLSNAAT ESLYNYCLQS FFDHKADILD REEITVAATS YFDNTDTVRG LLKHGNGLLS
ILDDQTRRGR SDAQFLESVR KRFEGKNPAI SVGSGGTTST GYLSQARTAF TVKHFAGEVD
YSVTGLIEEN GEVISGDLMN LMKSTRSDFV RELFGQEALQ TISHPREKTA IMQAQVSSKP
LRMPSMARRK HDQQARQIFS DRGESEEPDD RDSQATSSRR SVAGRKSGLM TGHVQGAAGQ
FLSGLEIINK SLSSPNLNPY FVICLKPNDR RIANQFDSKC VRMQVQTFGI AEISSRLRNA
DFSVFLPFAE FLGLADIGNV VVGSDREKSE VILDERRWPG NEARVGSTGV FLSERCWADL
AKIGERVVPS YNKIAGSDEG DVGYQAGGAD TKVRLLQPSD QSPGAFIYGD ESKQGYFGSR
ELDGKSDAGA SAFNSGDMFR NLETKEEMLQ KGNEKNMEEV DDVVVSSSRK RWMALVYLLT
FFIPDFLIKW IGRMKRKDVR VAWREKLAIN MIIWFACGVA VFMIVAFPGL VCPTQHVFSK
GELSDHNGKG SASSYIAIRG VVFNFGDFMP AHYPDIVPQK SLKNYAGTDA TNLFPIQVSA
LCQGVDGHVD PSVPLDYRSN MNDSATTTST TDYDVNAKYH DFRYWTDDPR ADWFYEQMVM
MRANYKKGYV GYTAKYMKTL ADDDSKNIVS IDGKVYDMTY YIAGPRIPRY PKGKNATGDV
NTNYMSPLLV TLFQQKSGTD VTKYWNDLAI DATTRARMQL CLDNLFFVGH VDTRNSARCQ
FARYFILAIS IMICVVILFK FLAALQFGKK NLPENLDKFI VCQVPAYTED EDSLRRAIDS
MARMRYDDKR KLLLVICDGM IIGQGNDRPT PRIVLDILGV PESVDPEPLS FESLGEGMKQ
HNMAKIYSGL YEVQGHIVPY LVVVKVGKPS EVSRPGNRGK RDSQMVLMRF LNRVHYNLPM
SPMELEMHHQ IRNIIGVNPT FYEYILQVDA DTVVAQDSAT RFVSAFLSDT RLIAACGETS
LSNAKTSMVT MIQVYEYYIS HNLTKAFESL FGSVTCLPGC FSMYRVRSAE SGKPLFVSKE
VVESYSEIRV DTLHMKNLLH LGEDRYLTTL LLKHHPKFKT KYIFRCHAWT VAPESFAVFL
SQRRRWINST VHNLIELIPL QQLCGFCCFS MRFIVFVDLL STIIQPVTVA YIIYLIVWLV
RDSSVIPWTA FVLLGVIYGL QAFIFIVRRK WEMIGWMFIY ILAIPVFTLA LPLYSFWNMD
DFTWGNTRVI TGEKGRKVVI SDEGKFDPAS IPKKRWEEYQ MELWEAQEGQ TSRDDHSEVS
GYSYGTRAHP FAQSQSEYGF AGSRPVSQLD LPLLASGSRM SVAPSEMMSH HMDMDMSMED
LSHLPSDDAI LAEIREILRT ADLMSVTKKS IKQELERRFG VNLDLKRPYI NSATEAVLSG
LL
//
