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Database: UniProt
Entry: A0A1I8IQX2_9PLAT
LinkDB: A0A1I8IQX2_9PLAT
Original site: A0A1I8IQX2_9PLAT 
ID   A0A1I8IQX2_9PLAT        Unreviewed;       976 AA.
AC   A0A1I8IQX2;
DT   18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT   18-JAN-2017, sequence version 1.
DT   24-JAN-2024, entry version 23.
DE   SubName: Full=Doublecortin domain-containing protein {ECO:0000313|WBParaSite:maker-uti_cns_0015311-snap-gene-0.3-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_0015311-snap-gene-0.3-mRNA-1};
RN   [1] {ECO:0000313|WBParaSite:maker-uti_cns_0015311-snap-gene-0.3-mRNA-1}
RP   IDENTIFICATION.
RG   WormBaseParasite;
RL   Submitted (NOV-2016) to UniProtKB.
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DR   AlphaFoldDB; A0A1I8IQX2; -.
DR   WBParaSite; maker-uti_cns_0015311-snap-gene-0.3-mRNA-1; maker-uti_cns_0015311-snap-gene-0.3-mRNA-1; maker-uti_cns_0015311-snap-gene-0.3.
DR   Proteomes; UP000095280; Unplaced.
DR   GO; GO:0036211; P:protein modification process; IEA:InterPro.
DR   Gene3D; 3.30.470.20; ATP-grasp fold, B domain; 1.
DR   InterPro; IPR004344; TTL/TTLL_fam.
DR   InterPro; IPR027752; TTLL10.
DR   PANTHER; PTHR46810; INACTIVE POLYGLYCYLASE TTLL10; 1.
DR   PANTHER; PTHR46810:SF1; INACTIVE POLYGLYCYLASE TTLL10; 1.
DR   Pfam; PF03133; TTL; 1.
DR   SUPFAM; SSF56059; Glutathione synthetase ATP-binding domain-like; 1.
DR   PROSITE; PS51221; TTL; 1.
PE   4: Predicted;
FT   REGION          74..386
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        86..100
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        101..124
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        140..164
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        165..184
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        203..257
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        273..324
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        331..369
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   976 AA;  110298 MW;  3173A26931404229 CRC64;
     PDAGSGHIQV IHALAFKVAV LSPNNARNLQ RSVGAAPTLV QLAKPSPKLH RPRAEARDTP
     VTLATATVQS LDTKTESRLK SESLFKNVRT KSNSRTKTDS QTKTVESRTK IDSKSKENTK
     SKTDSQSKPE AFVSDYANQV EDEPTKKSDS KSKTKTESKT KSESANKVET TAGKAATKTS
     TTHSKSDSGS KEDVGGTAKR PGNASELGNQ ADHTGTSAEE QQEATEVQQP NEVPQSRTNK
     TETTSKPESS NNVEVTGFGS GGRRESATAS AVGTGLRRAS ASSSAALDAR RGSAGNSRRS
     SAELAAENPE SSHNQESPAS AMEKPNDQSA PEEATPEQQG VPTASPESAG ATSETKSPMK
     KTSRAGTSGR SVMIPDDVNP NILPTKNNPL YNTTAALDKL DKFPTLKMRR DGKYYLKMKD
     IVIERHPKVK RNKRGDVIPT IKKEKMGAIE RVVSRFCEDV LCISRAQFLP LTSQGERHVV
     WVGKKKANHI IRYLNGNGCY VVNRFPGDIF VKDKQVMGII LRDHMLMRSN HCYWKCGVPK
     EDILNPKMPN EDEEENPITY RICRHMVKTM HMDEEGCEDK GCYNFEKHTC KHLDVFIPEV
     QSFCTYNALQ DFSNRLDDDL KGQTFVCKPA YLYKGYGFRF FRTAAEFQEF YHMTEGKETS
     RHDFMVQRLV DKPFLFNGKK LDIRAFLLVV VLRYRRVISF IHYGFCRVAS TEFEINEEEE
     ELNIEEPMTD KEMEKKKAEN YEKDMKMFVC TYRTAEEKVE RARRIDTQTF YEEADDRSQE
     LQAVFQKEEE LQGVKEQIKH IGLRISQAIE NKVWDAFGCF QIFGLDLCVD EDMKVWLIEI
     NSHAMSDVDT LSPTQRKVVP AVIMESLGLV VETTYKSFHH LRLRKSPTNE FEETGFLFRQ
     NYDFIFSTLA KKRMDYVWPK PPKKPDPPFY ERIGVVDQQI KNVDRRKKAC LAMKIAVREE
     QLALKRKRNA KDEEES
//
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