ID A0A0V1B3U9_TRISP Unreviewed; 1608 AA.
AC A0A0V1B3U9;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 36.
DE RecName: Full=protein adenylyltransferase {ECO:0000256|ARBA:ARBA00034531};
DE EC=2.7.7.108 {ECO:0000256|ARBA:ARBA00034531};
GN Name=FICD {ECO:0000313|EMBL:KRY31244.1};
GN ORFNames=T01_16091 {ECO:0000313|EMBL:KRY31244.1};
OS Trichinella spiralis (Trichina worm).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Trichinellida; Trichinellidae; Trichinella.
OX NCBI_TaxID=6334 {ECO:0000313|EMBL:KRY31244.1, ECO:0000313|Proteomes:UP000054776};
RN [1] {ECO:0000313|EMBL:KRY31244.1, ECO:0000313|Proteomes:UP000054776}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ISS3 {ECO:0000313|EMBL:KRY31244.1};
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:KRY31244.1}.
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DR EMBL; JYDH01000122; KRY31244.1; -; Genomic_DNA.
DR Proteomes; UP000054776; 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 Lipoprotein {ECO:0000256|PIRSR:PIRSR604241-50};
KW Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695};
KW Reference proteome {ECO:0000313|Proteomes:UP000054776};
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:KRY31244.1}.
FT DOMAIN 618..677
FT /note="SH3"
FT /evidence="ECO:0000259|PROSITE:PS50002"
FT REPEAT 1095..1128
FT /note="TPR"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00339"
FT DOMAIN 1275..1410
FT /note="Fido"
FT /evidence="ECO:0000259|PROSITE:PS51459"
FT REGION 551..581
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 679..751
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 787..844
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 708..749
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 787..803
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 806..844
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT LIPID 1608
FT /note="Phosphatidylserine amidated glycine; alternate"
FT /evidence="ECO:0000256|PIRSR:PIRSR604241-50"
SQ SEQUENCE 1608 AA; 182074 MW; B00974DBDDC298F3 CRC64;
MPVLGQNSFF RSSSTAGPLP ASMNGNVRRL NGNFGGSMPS FVDGQNFDVD MRKAYMQEDS
PSYFVEHLAT FGVGPQFGLQ WPSDGIRKLK QMERSSAIWA QRMILRLRHT AVVVEDENGD
VVEQFPLNLV SEPTAHVSSD PRDLYNNLLV FIVNGSKGKK TATPTEMHIF QCVQVSASEV
ADDIKQFLRG RFKAVPTGRR ISGFAMPSGG VEAGSPEMVT TDGTSLLHGR SMFSRSDQRY
FSQDRPRVST VPVMMENGRS PSNFNYREVD QKSTFSDSSV VEFFERDVNI LNRCFDDIER
FVARIQSAAI AQRELEALQQ QRRAMKPSSS RSSQSRMPGE GILLMRAQLP PELEFFDILQ
KFKLCFNLLA KLKNHIHEPN APELLHFLFT PLAIILDACQ WGFGRNIAPQ VVSPLISRAA
KALLLNCLTS KESEIWASLG DAWRTTAEEW TGPSPGNYSP TFAHSYGPYS TTTTGTTVPD
HGGQAGRSNR NLLIDTQLAG DFGRVSLERE RLDLEKEKLQ EEERRIQFEK RILEEERRRL
LEEKRQFYEE QEQRSVVSER LPRPPPAAAN GLYSSTMSRS RPDLYRETTL REQESRRHFS
PPNVTDDASF FFEQARARGS QIAQVVYERH GMNEKELTVR KGEFLEVLNN KKNWWECRNA
HRQVGFVPHT ILSVVDSGIH HNSTPHQQSK SFDEPLFVRP PPPSTSTFGP AMGNSATAFG
SYEDDSSARR SSPVTRTATP ANNNGDTPEV IRQRRGKLDE PKNKEVMMFS STCLVNSKRP
YVACAPPVPP PAPPPPPPPL PRTSGGVEAV SSTGEKKAST SNGTIPHGLS KENGTSIRNG
KLPSNVTVDS RRMLNEELLM TLNKSNLKGS FDFKAKPLPN SSLVTVQEMS SMSTKQDVAE
WLQAKCFSGR AINLLREHDG EKLLSMNKIQ LEELIGREEG ARLYSQLQLQ KTTAKYLMKS
DDSQLSSILA TRRNLNEEKM DDDKSLESQI CVEKSLKSFA MPKSMFSYNW YTLAVLVLLV
AVIAYQTLHL LNNNNRSWLS DYLLHCFKSN QKNVSKYLSR EVAFYLSSFD MPSPVEDTSV
LQSSLVPAKG TESEALAVLQ AAELFLKSGK VDKARKLFEH AVFLQPQHPD ILTGYGLFTE
KIGGDVVKAN FMFSRALIYS PDHSLAKWHK GRTQPIVQEI DAEMMRILDQ KRNKFLRIPR
GSSGLRRAMR EAYFSHIYHT VAMEGNTMNF VQTKSLLETR MAIGGKSILE HNEILGMDAA
LRFVNQSLIH RIGSLSVEDI LDIHRRVLGF VDPVESGRFR THQVYIGSFE PSLPENIEKE
VDELLEWLNS DTAMSIHPVE LAALLHYKFV VIHPFVDGNG RTSRLLMNLI LMQAGFPPVI
IRVEDRLQYY ESLKLANEGD LRPFVRFIAE CTRRTLDEYL ANSMCSVDEA SNPLEPIVDN
GRTIIIRHYY KFDALKESML FIFFCYFKVR ILFKTVFIGT QVYLTMNSMG GGLTFRQRRP
YNTRVREIQE IRRAYPDKIP IVIERFEGEK YLPVLDRCKF LVPDHVTMTE LMQIVRRRLE
LHPEQALFLL VNEKSLVSHS TTLAELYEAE KDTDGFLYIV YTSQPGFG
//
