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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
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
//