ID F2UNP7_SALR5 Unreviewed; 1320 AA.
AC F2UNP7;
DT 31-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 31-MAY-2011, sequence version 1.
DT 27-MAR-2024, entry version 47.
DE SubName: Full=Ttll3 protein {ECO:0000313|EMBL:EGD79252.1};
GN ORFNames=PTSG_09974 {ECO:0000313|EMBL:EGD79252.1};
OS Salpingoeca rosetta (strain ATCC 50818 / BSB-021).
OC Eukaryota; Choanoflagellata; Craspedida; Salpingoecidae; Salpingoeca.
OX NCBI_TaxID=946362 {ECO:0000313|Proteomes:UP000007799};
RN [1] {ECO:0000313|Proteomes:UP000007799}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 50818 {ECO:0000313|Proteomes:UP000007799};
RA Russ C., Cuomo C., Burger G., Gray M.W., Holland P.W.H., King N.,
RA Lang F.B.F., Roger A.J., Ruiz-Trillo I., Young S.K., Zeng Q., Gargeya S.,
RA Alvarado L., Berlin A., Chapman S.B., Chen Z., Freedman E., Gellesch M.,
RA Goldberg J., Griggs A., Gujja S., Heilman E., Heiman D., Howarth C.,
RA Mehta T., Neiman D., Pearson M., Roberts A., Saif S., Shea T., Shenoy N.,
RA Sisk P., Stolte C., Sykes S., White J., Yandava C., Haas B., Nusbaum C.,
RA Birren B.;
RT "Annotation of Salpingoeca rosetta.";
RL Submitted (AUG-2009) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; GL832984; EGD79252.1; -; Genomic_DNA.
DR RefSeq; XP_004989337.1; XM_004989280.1.
DR STRING; 946362.F2UNP7; -.
DR EnsemblProtists; EGD79252; EGD79252; PTSG_09974.
DR GeneID; 16069881; -.
DR KEGG; sre:PTSG_09974; -.
DR eggNOG; KOG2157; Eukaryota.
DR InParanoid; F2UNP7; -.
DR OrthoDB; 7265at2759; -.
DR Proteomes; UP000007799; 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000007799}.
FT DOMAIN 1165..1212
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT REGION 36..94
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 146..235
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 324..595
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 863..926
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1257..1311
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 49..94
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 148..169
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 170..188
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 361..381
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 402..425
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 514..528
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 529..564
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 871..901
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1320 AA; 144567 MW; FF86FFA841D5B92D CRC64;
MPTQPTPWYE RLSVRPPPVE WYDDNCTHTP TLNARSRALA KHRRESPARP QQQNTPSPTT
SASSTIATTS ATARTITTTT TTTPATTPAT TPATTISTTI ATTTTTTTVA TAATAAATIL
TEPLPPVHAS PSPSLSPSRV LQVPAITVPA PPGSPRIASI KPSSPPPTSP TASTATLKRS
TSLPASPSRP QVGRAPGSPR SPRSLARRVG ASPQPARRSP GPRRSRSRNL DGEEHFTFRP
RISSASRRLA GRRTNGYLEA RRQSNLERIV KEAKAEEVFQ PRLNKRSAQL VTSSFFERQQ
QFLHRKAELQ AVSDLYRLES EQKMHRRSPP VRIAPLPPPH APAASTHQEH ADAGHLHSPT
PTAAAATTAA AAATTTAGRG LRSPQRRIAA VVRRDKLAAK AKQQQQLLQH HQHTRATNTS
KNGGGGGGGG VSPSKRTALV RLRRPRSAGG AVGDSAQRNK RGGGGGGRGV GGLEEGQHAD
QMVRPATASS ALIRRRTPSA TPKPRALRRT HSVACARPTE HRERTMCSPT QESQHLVSDL
LSPRTTTSSD SSASNNSSSG GGGGTPTRRA RPAEMGGRTT PTGKSSKPRS KPPCINQERL
RDLHAAREAR AAAVAAAKKK NVFTICGRYQ DLRNALEQRG WVEKLPPREP GLGANDDCSG
LRIRTEAEMN KKKAQLQKRA EKEGFDLSAS NSVDVFSGSE EPADRALVSR ALGEFPANFI
WTCHRADVDF RTLKPGQSVN HFKCNGNITT KFGLAASLTN VQWTSNRDED EFYPRCYFIS
SEDDFVAFVR DYRLKAAVSV LKRINEWSPP RQIFDFALAH CQRHIDMLQH LDLDERLPSP
TDIEFETLLQ FTYEKLGCAN ASRSINEEEP EACSSSDDDT DDDGDEDDDD DDNDDDSDSD
DEDERKKAPV PKTKKKAVNR AAATVSASSR RALHRLVRRF TDGGMLQSAR ERVAAMMKSP
VAVTPSARAN AERILQELAA VDPQLQASGF RNVWVVKPAA KSRGRGIFCE NRLDFILPIV
VDGSSRERWV AQKYIERPLL IHNTKFDIRQ WVVVTSWLPL TVWMYRDCYL RFSSVPFDLD
NLHTKESKHV HLCNNSIQKV AVSTATSTFA PGCMWSSDEF KSFLDQQGQG SVWDEMIVPQ
MKEIAIASLA SAQDSAETRK HSFELFGFDY MIDAENKVWL VEINSSPDLS HSTAVTSQLV
ENMFEDMVKL VVDRRTNRKC DTGGFERIFR GPAVDSPLGA MSRDIFIEGT QITRKRMANP
SHLSRLSRRR ASTSNLEVGN GKSTKRGANA ATPTKAGLTS PRHQTSDPQL SVRRLAASIV
//
