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Database: UniProt
Entry: A0A0V1DA12_TRIBR
LinkDB: A0A0V1DA12_TRIBR
Original site: A0A0V1DA12_TRIBR 
ID   A0A0V1DA12_TRIBR        Unreviewed;      1633 AA.
AC   A0A0V1DA12;
DT   16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT   16-MAR-2016, sequence version 1.
DT   24-JAN-2024, entry version 36.
DE   RecName: Full=protein adenylyltransferase {ECO:0000256|ARBA:ARBA00034531};
DE            EC=2.7.7.108 {ECO:0000256|ARBA:ARBA00034531};
DE   Flags: Fragment;
GN   Name=FICD {ECO:0000313|EMBL:KRY58277.1};
GN   ORFNames=T03_2217 {ECO:0000313|EMBL:KRY58277.1};
OS   Trichinella britovi (Parasitic roundworm).
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC   Trichinellida; Trichinellidae; Trichinella.
OX   NCBI_TaxID=45882 {ECO:0000313|EMBL:KRY58277.1, ECO:0000313|Proteomes:UP000054653};
RN   [1] {ECO:0000313|EMBL:KRY58277.1, ECO:0000313|Proteomes:UP000054653}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ISS120 {ECO:0000313|EMBL:KRY58277.1};
RA   Korhonen P.K., Edoardo P., Giuseppe L.R., Gasser R.B.;
RT   "Evolution of Trichinella species and genotypes.";
RL   Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=3-O-(5'-adenylyl)-L-threonyl-[protein] + H2O = AMP + H(+) + L-
CC         threonyl-[protein]; Xref=Rhea:RHEA:55932, Rhea:RHEA-COMP:11060,
CC         Rhea:RHEA-COMP:13847, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:30013, ChEBI:CHEBI:138113, ChEBI:CHEBI:456215;
CC         Evidence={ECO:0000256|ARBA:ARBA00000155};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + L-threonyl-[protein] = 3-O-(5'-adenylyl)-L-threonyl-
CC         [protein] + diphosphate; Xref=Rhea:RHEA:54292, Rhea:RHEA-COMP:11060,
CC         Rhea:RHEA-COMP:13847, ChEBI:CHEBI:30013, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:33019, ChEBI:CHEBI:138113; EC=2.7.7.108;
CC         Evidence={ECO:0000256|ARBA:ARBA00034433};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + L-tyrosyl-[protein] = diphosphate + O-(5'-adenylyl)-L-
CC         tyrosyl-[protein]; Xref=Rhea:RHEA:54288, Rhea:RHEA-COMP:10136,
CC         Rhea:RHEA-COMP:13846, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019,
CC         ChEBI:CHEBI:46858, ChEBI:CHEBI:83624; EC=2.7.7.108;
CC         Evidence={ECO:0000256|ARBA:ARBA00034429};
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004167}; Single-
CC       pass membrane protein {ECO:0000256|ARBA:ARBA00004167}.
CC   -!- SIMILARITY: Belongs to the ATG8 family.
CC       {ECO:0000256|ARBA:ARBA00007293}.
CC   -!- SIMILARITY: Belongs to the EPS8 family.
CC       {ECO:0000256|ARBA:ARBA00006197}.
CC   -!- SIMILARITY: Belongs to the fic family. {ECO:0000256|ARBA:ARBA00009742}.
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:KRY58277.1}.
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DR   EMBL; JYDI01000022; KRY58277.1; -; Genomic_DNA.
DR   Proteomes; UP000054653; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016779; F:nucleotidyltransferase activity; IEA:UniProtKB-KW.
DR   CDD; cd01210; PTB_EPS8; 1.
DR   CDD; cd16129; Ubl_ATG8_MAP1LC3; 1.
DR   Gene3D; 1.10.3290.10; Fido-like domain; 1.
DR   Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 1.
DR   Gene3D; 2.30.30.40; SH3 Domains; 1.
DR   Gene3D; 1.25.40.10; Tetratricopeptide repeat domain; 1.
DR   Gene3D; 1.10.150.50; Transcription Factor, Ets-1; 1.
DR   InterPro; IPR004241; Atg8-like.
DR   InterPro; IPR039801; EPS8-like.
DR   InterPro; IPR033928; EPS8_PTB.
DR   InterPro; IPR003812; Fido.
DR   InterPro; IPR036597; Fido-like_dom_sf.
DR   InterPro; IPR011993; PH-like_dom_sf.
DR   InterPro; IPR013625; PTB.
DR   InterPro; IPR006020; PTB/PI_dom.
DR   InterPro; IPR013761; SAM/pointed_sf.
DR   InterPro; IPR041418; SAM_3.
DR   InterPro; IPR036028; SH3-like_dom_sf.
DR   InterPro; IPR001452; SH3_domain.
DR   InterPro; IPR011990; TPR-like_helical_dom_sf.
DR   InterPro; IPR019734; TPR_repeat.
DR   InterPro; IPR029071; Ubiquitin-like_domsf.
DR   PANTHER; PTHR12287:SF23; AROUSER, ISOFORM A-RELATED; 1.
DR   PANTHER; PTHR12287; EPIDERMAL GROWTH FACTOR RECEPTOR KINASE SUBSTRATE EPS8-RELATED PROTEIN; 1.
DR   Pfam; PF02991; ATG8; 1.
DR   Pfam; PF02661; Fic; 1.
DR   Pfam; PF08416; PTB; 1.
DR   Pfam; PF18016; SAM_3; 1.
DR   Pfam; PF00018; SH3_1; 1.
DR   SMART; SM00462; PTB; 1.
DR   SMART; SM00326; SH3; 1.
DR   SUPFAM; SSF140931; Fic-like; 1.
DR   SUPFAM; SSF50729; PH domain-like; 1.
DR   SUPFAM; SSF47769; SAM/Pointed domain; 1.
DR   SUPFAM; SSF50044; SH3-domain; 1.
DR   SUPFAM; SSF48452; TPR-like; 1.
DR   SUPFAM; SSF54236; Ubiquitin-like; 1.
DR   PROSITE; PS51459; FIDO; 1.
DR   PROSITE; PS50002; SH3; 1.
DR   PROSITE; PS50005; TPR; 1.
PE   3: Inferred from homology;
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW   Lipoprotein {ECO:0000256|PIRSR:PIRSR604241-50};
KW   Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695};
KW   Reference proteome {ECO:0000313|Proteomes:UP000054653};
KW   SH3 domain {ECO:0000256|ARBA:ARBA00022443, ECO:0000256|PROSITE-
KW   ProRule:PRU00192};
KW   TPR repeat {ECO:0000256|ARBA:ARBA00022803, ECO:0000256|PROSITE-
KW   ProRule:PRU00339};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:KRY58277.1}.
FT   DOMAIN          629..688
FT                   /note="SH3"
FT                   /evidence="ECO:0000259|PROSITE:PS50002"
FT   REPEAT          1131..1164
FT                   /note="TPR"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00339"
FT   DOMAIN          1311..1446
FT                   /note="Fido"
FT                   /evidence="ECO:0000259|PROSITE:PS51459"
FT   REGION          562..593
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          690..775
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          803..855
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        719..760
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        761..775
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        817..855
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   LIPID           1633
FT                   /note="Phosphatidylserine amidated glycine; alternate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR604241-50"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:KRY58277.1"
SQ   SEQUENCE   1633 AA;  184124 MW;  E77D8FDB8002D2E7 CRC64;
     LACDLLGIAS MPVLGQNSFF RSSSTAGPLP ASMNGNVRRL NGNFGGSMPS FVDGQNFDVD
     MRKAYMQEDS PSYFVEHLAT FGVGPQFGLQ WPSDGIRKLK QMERSSAIWA QRMILRLRHT
     AVVVEDENGD VVEQFPLNLV SEPTAHVSSD PRDLYNNLLV FIVNGSKGKK TATPTEMHIF
     QCVQVSASEV ADDIKQFLRG RFKAVPTGRR ISGFAMPSGG VEAGSPEMVA TDGPSLLHGR
     SMFSRSDQRY FSQDRPRVST VPVMMENGRS PSNFNYREVD QKSTFSDSSV VEFFERDVNI
     LNRCFDDIER FVARIQSAAI AQRELEALQQ QRRAMKPSSS RSSQSRMPGE GLLLMRAQLP
     PEFEFFDILQ KFKLCFNLLA KLKNHIHEPN APELLHFLFT PLAIILDACQ WGFGRNIAPQ
     VVSPLVSPAA KALLLNCLTS KESEIWASLG DAWRTTADEW TGPLPGHYSP TFAHNYGPYS
     TTTTTGTTVP DHGGQAGRSN RNLLIDTQLA GDFGRVSLER ERLDLEKEKL QEEGRRIQFE
     KRILEEERRR LLEEKRQFYE EQEQRSVVSE RLPRPPPAAA NGLYSSTMSR SRPDLYRETT
     LREQESRRHF SPSNVTDDAS FFFEQARARG SQIAQVVYER HGMNEKELTV RKGEFLEVLN
     NKKNWWECRN AHRQVGFVPH TILSVVDSGI HHNSTPHQQS KSFDEPLFVR PPPPSTSTFG
     PAMGNSATAF GSYEDDSSAR RSSPVTRTAT PANNSGDTPE VIRQRRGKLD EPKNKEVMMF
     SSTCLVNSKR PYVACAPPVP PPAPPPPPPP LPRTSGGVEA VSSSTGEKKA STSNGTIPHG
     LSKENGTSIR NGKVPSNVTV DSRRMLNEEL LMTLNKSNLK GSFDFKAKPW PNSSLVTVQE
     MSSISTKQDV AEWLQAKCFS GRAINLLREH DGEKLLSMNK IQLEELIGRE EGARLYSQLQ
     LQKTTAKYLM KSDDSQLSSI LATRRNLNEE KMDDDKSLES QICVEKSLKS FAMPKSIFSY
     NWYTLVVLVL LVAVIAYQTL HLLNNNNRSW LSDYLLHCFK SNQKNVSKYL SREVAFYLSS
     FDMPSPVEDT SVSQSSLVPA KGKKYTFLLL HVRLLCQYAE QVGISGTESE ALAVLQAAEL
     FLKSGKVDKA RKLFEHAVFL QPQHPDILTG YGLFTEKIGG DVVKANFMFS RALIYSPDHS
     LAKWHKGRTQ PIVQEIDAEM MRILDQKRNK FLRIPRGSSG LRRAMREAYF SHIYHTVAME
     GNTMNFVQTK SLLETRMAIG GKSILEHNEI LGMDAALRFV NQSLIHRIGS LSVEDILDIH
     RRVLGFVDPV ESGRFRTHQV YIGSFEPSLP ENIEKEVDEL LEWLNSDTAM SIHPVELAAL
     LHYKFVVIHP FVDGNGRTSR LLMNLILMQA GFPPVIIRVE DRLQYYESLK LANEGDLRPF
     VRFIAECTRR TLDEYLANSM CSVDEASNPL EPIVDNGRTI ILPKVLAHFL DIPLNETFIA
     VFIATQVCLT MNSMGGGLTF RQRRPYNTRV REIQEIRRAY PDKIPIVIER FEGEKYLPVL
     DRCKFLVPDH VTMTELMQIV RRRLELHPEQ ALFLLVNEKS LVSHSTTLAE LYEAEKDTDG
     FLYIVYTSQP GFG
//
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