ID A0A2B4SD22_STYPI Unreviewed; 917 AA.
AC A0A2B4SD22;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 22-FEB-2023, entry version 17.
DE SubName: Full=Protein polyglycylase TTLL10 {ECO:0000313|EMBL:PFX27781.1};
GN Name=Ttll10 {ECO:0000313|EMBL:PFX27781.1};
GN ORFNames=AWC38_SpisGene7506 {ECO:0000313|EMBL:PFX27781.1};
OS Stylophora pistillata (Smooth cauliflower coral).
OC Eukaryota; Metazoa; Cnidaria; Anthozoa; Hexacorallia; Scleractinia;
OC Astrocoeniina; Pocilloporidae; Stylophora.
OX NCBI_TaxID=50429 {ECO:0000313|EMBL:PFX27781.1, ECO:0000313|Proteomes:UP000225706};
RN [1] {ECO:0000313|Proteomes:UP000225706}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Voolstra C.R., Li Y., Liew Y.J., Baumgarten S., Zoccola D., Flot J.-F.,
RA Tambutte S., Allemand D., Aranda M.;
RT "Comparative analysis of the genomes of Stylophora pistillata and Acropora
RT digitifera provides evidence for extensive differences between species of
RT corals.";
RL bioRxiv 0:0-0(2017).
CC -!- SIMILARITY: Belongs to the peptidase C40 family.
CC {ECO:0000256|ARBA:ARBA00007074}.
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:PFX27781.1}.
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DR EMBL; LSMT01000095; PFX27781.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2B4SD22; -.
DR STRING; 50429.A0A2B4SD22; -.
DR EnsemblMetazoa; XM_022931213.1; XP_022786948.1; LOC111327109.
DR Proteomes; UP000225706; Unassembled WGS sequence.
DR GO; GO:0036211; P:protein modification process; IEA:InterPro.
DR Gene3D; 3.30.470.20; ATP-grasp fold, B domain; 1.
DR Gene3D; 3.90.1720.10; endopeptidase domain like (from Nostoc punctiforme); 1.
DR InterPro; IPR000064; NLP_P60_dom.
DR InterPro; IPR038765; Papain-like_cys_pep_sf.
DR InterPro; IPR004344; TTL/TTLL_fam.
DR PANTHER; PTHR47664; NLPC_P60 DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR47664:SF1; NLPC_P60 DOMAIN-CONTAINING PROTEIN; 1.
DR Pfam; PF03133; TTL; 1.
DR SUPFAM; SSF54001; Cysteine proteinases; 1.
DR SUPFAM; SSF56059; Glutathione synthetase ATP-binding domain-like; 1.
DR PROSITE; PS51935; NLPC_P60; 1.
DR PROSITE; PS51221; TTL; 1.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000225706}.
FT DOMAIN 68..214
FT /note="NlpC/P60"
FT /evidence="ECO:0000259|PROSITE:PS51935"
FT REGION 249..289
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 371..402
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 480..544
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 373..389
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 480..531
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 917 AA; 105373 MW; 8AFDC8DAD286777C CRC64;
MEESKRKNTT ESEDILTLCG AAEEKAKSGE SLQDAFKKFR KKRQNAIRLS KQVDKETTKW
RADPVKMNKL RMKFVEQCKL YFGVPYAKKY QEPGTAEFNA PFFLDCCGLI RRVLRDLKED
FGFEVGPWNQ AYMYDTLPLD AEKTDDLKPG DLVFVSGIYH NTKSKKQRHN MVHVEVWAGD
GEKTIGARWQ KGKVQYHDSY KFNAKSYHSM QYHFKSIDTW LMGICQSHCP EHSWKRSQYR
PGKRSIFAED QANEREDQNA EELSDEEMGS QVNDDKQRPP CSENEIQSSS DKKNLICQKA
VSLHITSPDS NTCHETVSSD CPSTTTTAQL SQKNFNNLDE CVSWLLTKIS MDIESECYDR
ISDVEAIKLH SSPQHAEHSS SNNPNNDMIP KDHSARKTKM DSTVQSNTDQ DCHCPQCCHA
KVSCIHQRCG CHYGFPQDND ENDFENLDDC KENSSSLECF DFMHTGMNCD QFVINQCPNN
SDSNHSGSKS RRSVSPSKAT KNGKDSGSGP SGNRRGNGNE KNNNRDSPGR SGTRSVRGYM
NDKQPPFFIG GGNGNWMIES TLVSLGWSRI EDKLDESFKL KWVECKSQIN YGNFRDGEHL
ANHISNINLL TTKLGLLCSL EEYQRVQEKM AKNKLKFPMS EFVPETHKLM NATEKAKFVN
EVYKDGEIWI CKPTGMNQGK GIYLVNSKEQ LIEKLNMNGG DNVSARRSLV RPPQGRVIQR
YVMNPLLLNG CKFDIRTYML IASTTPFIVF YHPGYVRLSC VPYTPYTPDA AGLHAHLTNQ
YVQKKHPLYS SMKEDTVWSF ERLQSYIDEK YSKEKELPEN WVYTTFTKRM HQIMTTCFHS
VRQKLHKRAG TFDLLGFDFL IDDNFNMSYK TALPQSRFAA RLRSLRNFRR MAEERKEREY
ERGLDRAAIL KSYGNDQ
//