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Database: UniProt
Entry: A0A2C9JEB4_BIOGL
LinkDB: A0A2C9JEB4_BIOGL
Original site: A0A2C9JEB4_BIOGL 
ID   A0A2C9JEB4_BIOGL        Unreviewed;      1068 AA.
AC   A0A2C9JEB4;
DT   20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT   20-DEC-2017, sequence version 1.
DT   27-MAR-2024, entry version 27.
DE   RecName: Full=ATP-grasp domain-containing protein {ECO:0000259|PROSITE:PS50975};
GN   Name=106055000 {ECO:0000313|EnsemblMetazoa:BGLB001338-PK};
OS   Biomphalaria glabrata (Bloodfluke planorb) (Freshwater snail).
OC   Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Mollusca; Gastropoda;
OC   Heterobranchia; Euthyneura; Panpulmonata; Hygrophila; Lymnaeoidea;
OC   Planorbidae; Biomphalaria.
OX   NCBI_TaxID=6526 {ECO:0000313|EnsemblMetazoa:BGLB001338-PK, ECO:0000313|Proteomes:UP000076420};
RN   [1] {ECO:0000313|EnsemblMetazoa:BGLB001338-PK}
RP   IDENTIFICATION.
RC   STRAIN=BB02 {ECO:0000313|EnsemblMetazoa:BGLB001338-PK};
RG   EnsemblMetazoa;
RL   Submitted (MAY-2020) to UniProtKB.
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DR   RefSeq; XP_013066557.1; XM_013211103.1.
DR   AlphaFoldDB; A0A2C9JEB4; -.
DR   EnsemblMetazoa; BGLB001338-RK; BGLB001338-PK; BGLB001338.
DR   VEuPathDB; VectorBase:BGLB001338; -.
DR   OrthoDB; 7265at2759; -.
DR   Proteomes; UP000076420; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR   GO; GO:0070735; F:protein-glycine ligase activity; IEA:UniProt.
DR   GO; GO:0036211; P:protein modification process; IEA:InterPro.
DR   Gene3D; 3.30.470.20; ATP-grasp fold, B domain; 1.
DR   InterPro; IPR011761; ATP-grasp.
DR   InterPro; IPR004344; TTL/TTLL_fam.
DR   PANTHER; PTHR45870; TUBULIN MONOGLYCYLASE TTLL3; 1.
DR   PANTHER; PTHR45870:SF2; TUBULIN MONOGLYCYLASE TTLL3; 1.
DR   Pfam; PF03133; TTL; 1.
DR   SUPFAM; SSF56059; Glutathione synthetase ATP-binding domain-like; 1.
DR   PROSITE; PS50975; ATP_GRASP; 1.
DR   PROSITE; PS51221; TTL; 1.
PE   4: Predicted;
KW   ATP-binding {ECO:0000256|PROSITE-ProRule:PRU00409};
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW   Nucleotide-binding {ECO:0000256|PROSITE-ProRule:PRU00409}.
FT   DOMAIN          864..908
FT                   /note="ATP-grasp"
FT                   /evidence="ECO:0000259|PROSITE:PS50975"
FT   REGION          97..149
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          192..290
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          384..432
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          547..594
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1042..1068
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        97..117
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        192..221
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        222..269
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        270..290
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        397..421
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        547..579
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1044..1068
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1068 AA;  121749 MW;  97536975D14C6B9B CRC64;
     MGGSRFCQDT VSDTGKTNFT SRGKLDPSIF LCDEGLVNHY KTQRSATQVD ASGQVPPKYF
     NDFDILKDLA SDLLRLQNER MLLLKNKLVE MNVDPNQSAS LPLHENVNAN AVTKSDSKER
     NQSAKNSLNR QKANEFSLSE RTDAENKASK PRKICWPKLD EVKPDKVVFA WDEPRKPGSA
     TLTELKQLEK SIKQHRLSDQ NSKKADVSRK ELKEETNGDV KVNTEVSRAS KMSPSNNFTL
     ARTKTNVSPG IDTEVNGPLA QNNPESLSQH SDSEKLDLAD ISNNKPKEPK LNIKENEMSD
     AYLIARSKTM PTLNRMKISP QKLGTNANEG ERLRLAKEMA ERATKYKKVF TIQGGYSTIR
     QSLRKRGWVE KFYKIPLTLK KSNSLQKEKK NSDDDDNNND DNDDDDAAID DDDDDDVDDM
     DNDQPKVPPW EEEDGIYGIM SRLVRNVNPT LFWVLKRDAI DYRFLTKDQM VNHYCKAGSF
     TTKVGLCINM RNVVWFDSTD HNTFFPRCYR LSHDEDKDAF VDDYRLTACM CIVKVAVRQT
     SSFPDHISED EEEIKISDPP AAKPGDDDKK KENENTKTEE VETPLNPMGM TNKKRKKTRA
     IIPVRVLETA VYQCEKFLAS KDHEDIDMPI QTGVLTEQQW DDLIQWYYQL VHEEGSFINV
     PVDLVKQCES LTRRLAQHCP QFEMDGIRNV WIVKPGAKSR GRGIICYEKL EDMLKLVSSQ
     VVKKDGKYVV QKYIERPLLI YNTKFDIRQW FLVTDWNPLT LWFYRDSYLR FCSQQFTLED
     FDQSIHLSNN AIQKHYKNGP RSPRLPDENM WTHYEFKDYL KSKKQPNAWD ELIYPSMKKA
     IICSLLVTQD LVEYRKSSFE LYGADFMLTE DLSPWLIEIN SSPSMESSTA VTAKLCAAVL
     DDTIKVVIDR KLDRNCDIGA FELAYKQALV TVPPYIGINL CVEGQSVRKP GTFTKPQPKQ
     SDPNLADSLF TPRAVTMRQT MADRTLEVKR STVAGDSSPI RNDKSKNFEA ATSKLQQAGL
     SKEIPAKIST FRASGDLEKL KANKVTTASP QNTSSAESKW NSGNTVIL
//
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