ID S2JF45_MUCC1 Unreviewed; 1832 AA.
AC S2JF45;
DT 18-SEP-2013, integrated into UniProtKB/TrEMBL.
DT 18-SEP-2013, sequence version 1.
DT 27-MAR-2024, entry version 50.
DE RecName: Full=chitin synthase {ECO:0000256|ARBA:ARBA00012543};
DE EC=2.4.1.16 {ECO:0000256|ARBA:ARBA00012543};
GN ORFNames=HMPREF1544_04729 {ECO:0000313|EMBL:EPB88494.1};
OS Mucor circinelloides f. circinelloides (strain 1006PhL) (Mucormycosis
OS agent) (Calyptromyces circinelloides).
OC Eukaryota; Fungi; Fungi incertae sedis; Mucoromycota; Mucoromycotina;
OC Mucoromycetes; Mucorales; Mucorineae; Mucoraceae; Mucor.
OX NCBI_TaxID=1220926 {ECO:0000313|EMBL:EPB88494.1, ECO:0000313|Proteomes:UP000014254};
RN [1] {ECO:0000313|Proteomes:UP000014254}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=1006PhL {ECO:0000313|Proteomes:UP000014254};
RG The Broad Institute Genomics Platform;
RA Cuomo C., Earl A., Findley K., Lee S.C., Walker B., Young S., Zeng Q.,
RA Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Allen A.W., Alvarado L.,
RA Arachchi H.M., Berlin A.M., Chapman S.B., Gainer-Dewar J., Goldberg J.,
RA Griggs A., Gujja S., Hansen M., Howarth C., Imamovic A., Ireland A.,
RA Larimer J., McCowan C., Murphy C., Pearson M., Poon T.W., Priest M.,
RA Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J., Nusbaum C.,
RA Birren B.;
RT "The Genome sequence of Mucor circinelloides f. circinelloides 1006PhL.";
RL Submitted (MAY-2013) 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 -!- SIMILARITY: Belongs to the TRAFAC class myosin-kinesin ATPase
CC superfamily. Myosin family. {ECO:0000256|PROSITE-ProRule:PRU00782}.
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DR EMBL; KE123950; EPB88494.1; -; Genomic_DNA.
DR STRING; 1220926.S2JF45; -.
DR VEuPathDB; FungiDB:HMPREF1544_04729; -.
DR eggNOG; KOG2571; Eukaryota.
DR eggNOG; KOG4229; Eukaryota.
DR InParanoid; S2JF45; -.
DR OMA; CQFSTYF; -.
DR OrthoDB; 1331060at2759; -.
DR Proteomes; UP000014254; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016459; C:myosin complex; IEA:UniProtKB-KW.
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 CDD; cd04190; Chitin_synth_C; 1.
DR Gene3D; 1.10.10.820; -; 1.
DR Gene3D; 1.20.58.530; -; 1.
DR Gene3D; 3.10.120.10; Cytochrome b5-like heme/steroid binding domain; 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; IPR036961; Kinesin_motor_dom_sf.
DR InterPro; IPR001609; Myosin_head_motor_dom.
DR InterPro; IPR029044; Nucleotide-diphossugar_trans.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR025662; Sigma_54_int_dom_ATP-bd_1.
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; PF00063; Myosin_head; 1.
DR PRINTS; PR00193; MYOSINHEAVY.
DR SMART; SM01117; Cyt-b5; 2.
DR SMART; SM00242; MYSc; 1.
DR SUPFAM; SSF55856; Cytochrome b5-like heme/steroid binding 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; PS51456; MYOSIN_MOTOR; 1.
DR PROSITE; PS00675; SIGMA54_INTERACT_1; 1.
PE 3: Inferred from homology;
KW Actin-binding {ECO:0000256|PROSITE-ProRule:PRU00782};
KW ATP-binding {ECO:0000256|PROSITE-ProRule:PRU00782};
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:UP000014254};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 893..909
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 929..948
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1196..1215
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1591..1612
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1618..1638
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1645..1669
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 12..753
FT /note="Myosin motor"
FT /evidence="ECO:0000259|PROSITE:PS51456"
FT DOMAIN 956..1013
FT /note="Cytochrome b5 heme-binding"
FT /evidence="ECO:0000259|PROSITE:PS50255"
FT REGION 587..612
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 631..653
FT /note="Actin-binding"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00782"
FT REGION 860..883
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 116..123
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00782"
SQ SEQUENCE 1832 AA; 206578 MW; 61CF018D2349BC6B CRC64;
MNRRSMHAPP SDTINDLSTV DNLTDKQLTD ILHQKFLNYN VYSYIGACHL VAINPFKALA
QNDAQTSDDY VTSYKDIASP ANPISSKLNP HVFELVNRAY FHMRRTGNDQ SIFLCGESGT
GKTEISNLVI RHLIHLSANK KRCKVQNQML NGQKVLRAFG CAKTCFNDNA ASRYGVYIET
HYNERGKMVG AKTLHYFLEK SRLCHGKLGE GNFNVFYWLL AGTEPDEKQV LQLKDDPKAY
LYLAKYGRML QSGDAADYNE LKGVMRAAGF RGEHFNRIIQ LLAAILHLGN ISFTDPAGLS
VTDESVTIKN RDTLEFVAEL LGLDAQALES VLTLKTTMIG KDVTTLILNA DQAAAQRDEL
AQTLYSLLFS WLVEHVNQKT YTDQFNSFIG LLDFPGTQPS GFGSVGFEQF CIDYANERIY
NFIMDRTFAS DNDSEFQAES IQLPQVDYTC NTACIDLYEK PTRGINAILN KMSEKTMSGK
RIFTDANAVE AITKYNTDNP SFASKLSDTN ARQFAIQHYS GQVTYEPTGF IAKNNNQLLV
DFIALIRGNA DMPASWNSFV LDLFSDDNLA IDSHPLGGMS ALVAAQQSAK PTRLPSMRRS
QRKANREKPN VSAVVDDSSK KTVLAQVQSA IDDLVSSFQE TTMWCVHCIR PNATASTTQF
DSLLVQSQIK AFHLDTMAAK MQRFYMISVP HSSFLSRYAV PFSHMGLDHS GSPQEQCMSI
KEMNHWTDRD IAIGTNKVFL SYASWHLLEE QLRALEKQEQ KSLKVFDPNI GMPALLDNEQ
GMDIHTRDIP ATTPTPMLSQ DFDNATLETL PLPSVAGRSV YSDDDHHNTR YSRGSFYNTS
QDADFRFGNY VNQAGDYTAT DGGSFSPPMA PPTTDLDATD EKESTMTPGR KRWLWFVTLM
TWWIPKILLV KWGRMKRKDV RIAWREKVVL CMIITCMCGF VIWFLVFFGE IICPNQNVYS
INELSSHNSD QDGYVAIRGE VFDLGSFAPH HYPSIVPTSS VLSYAGKDAT DLFPIQVSDL
CENVSPYVSL DYNRNYTDPN AQYHDFRFAS GNYRPNWYYD QMTMLRRNYK KGDMGVEWKG
IRDQAQGAYK LNGVSTNRQW AVINEHIYDL TTYLMGGRYL AAPNNGTVPT DVSTDFLDPQ
VVELFQANAG TDLTEKFNAL SLSADQKYRE LACIRNLYFV GMVDQRNSTK CQFSTYFLLA
VTICLCIVVF FKFIAAIRIG SARVPEELDK FVICQVTCYT EDEDSLRKTI DSLATLRYDD
KRKLIVVICD GMIIGSGNDR PTPRIVLDIF GVDPQVDPEA LSFISVGEGM KQHNRAKIYS
GLYEIGGHVV PYLVIAKVGA PNERQKPGNR GKRDSQLVLM QFLNRVQYDA PMNPMQLEMY
HQMRNVIGVS PELYEYVLMV DADTEVMPTG LNYLVSSMSH DAKIIGICGE TTLSNEKDTW
VTMIQVYEYF ISHHMIKAFE SLFSTVSCLP GCFTMYRIRT VDGKRPLFVS NEVIQDYTVN
VVDTLHKKNL LYLGEDRYLT TLLLKHHPNY KTKFNADAQC KTNAPDTWDV LISQRRRWIN
STVHNLGELV FLPKLCGFCC FSMRFVVMLD LISTLVQPAL LGYLGFLIYK LVEAKNQIPY
ITIITLGCTY GLQIILFIMY RRWEYIAWFF LSILALPVFS FYIPIYSYWH FDDFSWGNTR
VVVGEKGKQV AVGDEGEFDP KSIPLMSWSQ YEKFMLSENY SDGLSQASYS YPPAPMSSAH
GAGGAGGVYP NNSSSASVAY SNYGSRYSYG PGSVHSFAGR SMADGHQSVA SGASGYASRF
RYGPTMMHDA MSDTMSASMV NSYYAQNQQH NR
//
