ID   A0A1I8IKF5_9PLAT        Unreviewed;      1211 AA.
AC   A0A1I8IKF5;
DT   18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT   18-JAN-2017, sequence version 1.
DT   24-JAN-2024, entry version 21.
DE   SubName: Full=Tubulin--tyrosine ligase-like protein 9 {ECO:0000313|WBParaSite:maker-uti_cns_0013386-snap-gene-0.4-mRNA-1};
OS   Macrostomum lignano.
OC   Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Platyhelminthes;
OC   Rhabditophora; Macrostomorpha; Macrostomida; Macrostomidae; Macrostomum.
OX   NCBI_TaxID=282301 {ECO:0000313|Proteomes:UP000095280, ECO:0000313|WBParaSite:maker-uti_cns_0013386-snap-gene-0.4-mRNA-1};
RN   [1] {ECO:0000313|WBParaSite:maker-uti_cns_0013386-snap-gene-0.4-mRNA-1}
RP   IDENTIFICATION.
RG   WormBaseParasite;
RL   Submitted (NOV-2016) to UniProtKB.
CC   -!- SIMILARITY: Belongs to the indoleamine 2,3-dioxygenase family.
CC       {ECO:0000256|ARBA:ARBA00007119}.
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DR   AlphaFoldDB; A0A1I8IKF5; -.
DR   WBParaSite; maker-uti_cns_0013386-snap-gene-0.4-mRNA-1; maker-uti_cns_0013386-snap-gene-0.4-mRNA-1; maker-uti_cns_0013386-snap-gene-0.4.
DR   Proteomes; UP000095280; Unplaced.
DR   GO; GO:0020037; F:heme binding; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR   GO; GO:0016702; F:oxidoreductase activity, acting on single donors with incorporation of molecular oxygen, incorporation of two atoms of oxygen; IEA:UniProt.
DR   GO; GO:0036211; P:protein modification process; IEA:InterPro.
DR   GO; GO:0019441; P:tryptophan catabolic process to kynurenine; IEA:InterPro.
DR   Gene3D; 1.20.58.480; -; 1.
DR   Gene3D; 3.30.470.20; ATP-grasp fold, B domain; 1.
DR   InterPro; IPR000898; Indolamine_dOase.
DR   InterPro; IPR037217; Trp/Indoleamine_2_3_dOase-like.
DR   InterPro; IPR004344; TTL/TTLL_fam.
DR   PANTHER; PTHR28657; INDOLEAMINE 2,3-DIOXYGENASE; 1.
DR   PANTHER; PTHR28657:SF5; INDOLEAMINE 2,3-DIOXYGENASE; 1.
DR   Pfam; PF01231; IDO; 1.
DR   Pfam; PF03133; TTL; 1.
DR   SUPFAM; SSF56059; Glutathione synthetase ATP-binding domain-like; 1.
DR   SUPFAM; SSF140959; Indolic compounds 2,3-dioxygenase-like; 1.
DR   PROSITE; PS51221; TTL; 1.
PE   3: Inferred from homology;
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           20..1211
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5009321028"
SQ   SEQUENCE   1211 AA;  134687 MW;  9C4F6B424CFC21C5 CRC64;
     GSTVLFVLFF HASLLNNAGQ RRRSLVRAPT VRSDTGGLQL MHNGAVLVEQ LDEFAAPVRG
     RQSDDVGCQL GVAPAADARR RSLVRAPTVR SDTGGLQLMH NGAVLVEQLD EFAAPVRGRQ
     SDDVGCQLGV APAADALTLC LHVRHVDLDL FCLALLIVHH HLHCGHPPGQ LHRPPHHRHH
     PGWQRLPRLL GAARRAVLAK GSRHRGASGS PALQKLTRRH RGRIAADLLT RLLLLRLLLL
     LILHPLRLAQ PSQCSLCFCL LLFALPRLAC LPSLCCRCYP LRAWTSKMFR NGFLSDMGFC
     SLSYPDGKAM VQEVFNHLGW ATVANFRTQH PYQPGFFWCH GYTAKSITEW RQSAKFTGLQ
     FVSSLPNIIC LHNKKLLQTL IRQYEQSVLN SVGSLDAPNY LRFPGDIRAY NSDAYLPRTL
     FDLTHEELHH IAESCFKQDS VWIAKPLSQN CGKGICLVRS REQLLELSDR LPNLIVQEYI
     RNPVTLDGRK SDLRVYLLLV CPERGHLMAF YHPGFVRLSL RQYAETTDDL AVHLTNQSVA
     KATEEWTRRR DESTWTPAQM NNNLNARRDS TGFERDFLFR RVHPSMRAVL GIVSRAAYPK
     VTRIGGCFEF LGCDFMLDTS GRVWLIEINC YPGMATSTSL LRTLKPQVVH EAICLSMECI
     SKQYQGKAMY PLESLRQFQL LWNNLTFIDW KNFQQSGMRT LAEYQISSKT GFVLEQPCCQ
     LPPAWQAYDR LASAIVPILS QPDTDKASAD LHLAVADLVV PSDHALMDMA TAWSLETRCR
     LHLCLTCITA SYLWHRGESR APNRLPAQLA RPLLRVAESL GLKPTVGHAT LALANCALPD
     SAWSGRPEHL RLLCQPGPSS AFRAFVLVTC AFELDFARAT PLLLRGAEAR RPDEAADLLD
     RLADCLAGLT ARFDDFGRLL DPDEFYRDVR PYLSGHEGLV FEGCSCEATP LRLSGGSAAQ
     STILQSIDAL LGIRHESAFL AEMVDYMHPA HRQLLKDLAA ETRLPQLVAA SAPESRLRAA
     HGRAVAALAD FRKRHIGLVS RYIVAPASRV RTEFASLAER GTGGQPLIQF LKEVRDEGAL
     PPPLSDPGVD GSGDGIRYPL TWVYDACHPD VCQPNVCQPD VCQPVFASRC LPADVCHPDV
     CQPMFASRCL PADVCQPMFA SRMFASRCLP AGCLPADVCQ PMFASRCLRC LPASRMFASR
     MFADVCQPDI C
//