ID A0A1R2CGI4_9CILI Unreviewed; 1212 AA.
AC A0A1R2CGI4;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE RecName: Full=chitin synthase {ECO:0000256|ARBA:ARBA00012543};
DE EC=2.4.1.16 {ECO:0000256|ARBA:ARBA00012543};
GN ORFNames=SteCoe_10073 {ECO:0000313|EMBL:OMJ88085.1};
OS Stentor coeruleus.
OC Eukaryota; Sar; Alveolata; Ciliophora; Postciliodesmatophora;
OC Heterotrichea; Heterotrichida; Stentoridae; Stentor.
OX NCBI_TaxID=5963 {ECO:0000313|EMBL:OMJ88085.1, ECO:0000313|Proteomes:UP000187209};
RN [1] {ECO:0000313|EMBL:OMJ88085.1, ECO:0000313|Proteomes:UP000187209}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=WM001 {ECO:0000313|EMBL:OMJ88085.1};
RA Slabodnick M., Ruby J.G., Reiff S.B., Swart E.C., Gosai S., Prabakaran S.,
RA Witkowska E., Larue G.E., Fisher S., Freeman R.M., Gunawardena J., Chu W.,
RA Stover N.A., Gregory B.D., Nowacki M., Derisi J., Roy S.W., Marshall W.F.,
RA Sood P.;
RT "The macronuclear genome of Stentor coeruleus: a giant cell with tiny
RT introns.";
RL Submitted (NOV-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}.
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:OMJ88085.1}.
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; MPUH01000160; OMJ88085.1; -; Genomic_DNA.
DR OrthoDB; 1331060at2759; -.
DR Proteomes; UP000187209; 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:SF9; CHITIN SYNTHASE 1; 1.
DR Pfam; PF03142; Chitin_synth_2; 1.
DR SUPFAM; SSF53448; Nucleotide-diphospho-sugar transferases; 1.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000187209};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 946..971
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 991..1015
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1027..1048
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1068..1089
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1095..1116
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1148..1169
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1181..1202
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT REGION 271..299
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 617..644
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 1212 AA; 143159 MW; 19563C8F24AE4305 CRC64;
MCERNADILA TKEYIKYCDM KVNRPINHLS LKFFSENVVY QPFVLRYQER NKVNGLFPLA
SMPAIRNQEI KCDFLRDWTS NGQQNNNQSY FNQRDSANAT FIDANEENKI SSVLSKNCKF
LIVITICNEK AKELDDTLNG IFCNLKNFIH GKEGYKCKLN EIGCIIVADG IEAFNKSYKA
QHNTINNKCE VCDLDKNFIK AHSEKCGNFL YFSQFFNEHC IENFFAEQEI FEEMIKESEV
IEKILNVNEN FRYIFREIYR MEEEKIIEES KDSDKNKIDE EDKEEGSSDK EDKEERSSDK
EEVKEEIKFN FSRDNEKICK LHDILFSLLS LPKQYINLFK DSPTKKATLN SELIKSDKEI
KSKIKNLGKH YNILRNCAHI SDEYYDLAIK FLQIFNLQEY IMKAWINEQE EILINILPHR
EEDNNVVYLF IKDINYEKEE TYSEEAFDEI FENKYSNCEI DYAKDFIYGL IQKYIEKCKS
LNDYLEKISK LKYCEKKWIE KSDXDYAKDF IYGLIQKYIE KCKSLNDYLE KISKLKYCEK
KWIEKSDSRI IETNEILKKL KSSRNKHSEM YKDEENERQM ETINENIIRL TKSTGFMKPD
PYSERGMPKT KSHMNIKDEH ETEMEDLINE RHKFNKEHKS YLEKISDLHP EEKKKYEFTL
IKKLKDLKYI KENEEIAHCF SMKLSFSDDE EQKEQVDRSM QNELGISIIN DSSCNINRQN
QSNEPFLNLI FCVKQLNKRK LNSHRWFLEG FCSIINPNFI MFLDVGTIPK NNSLYSLYYA
MAKDEYLAGC CGEIIPIKPK NCNMVVNAQI VEYKFSHILD KALESVIGYV SVLPGAFSAY
RWKCFDTKIL SKYFHSQYNQ EMSLFEANMY LAEDRILCLE LMCMKNEKYI LRYVNESQAE
TDTPETLDRL MAQRRRWING SWFSMIYTIT KCNKIGKSKH KCLIKFIFRI LMVYYAIVAM
FNWVLVGAFY IGFAISLKKN INEKSSNVDK LLNISTPFII IYIAILIFIT IASLSVSPTK
LEKVFKVISY IYGLYTLGTI GLIFSFIYKS NVVENIIVNH AWKTSISLVS IGIIVFFFVI
VICLNYKSIA PILLGLFHFL FMTGTYVNVF LIYSICNFHD CSWGNRPDNK TEAEKLTEAQ
YKNERTRFVM FWILCNGFFV YAVELLYNSD DDYSHYYLNS VASLAFLIMV IKCIGGIMYF
FCEKCYHRWL IR
//
