ID A0A0V0UYN4_9BILA Unreviewed; 1686 AA.
AC A0A0V0UYN4;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 38.
DE RecName: Full=protein adenylyltransferase {ECO:0000256|ARBA:ARBA00034531};
DE EC=2.7.7.108 {ECO:0000256|ARBA:ARBA00034531};
DE Flags: Fragment;
GN ORFNames=T09_10928 {ECO:0000313|EMBL:KRX56399.1};
OS Trichinella sp. T9.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Trichinellida; Trichinellidae; Trichinella.
OX NCBI_TaxID=181606 {ECO:0000313|EMBL:KRX56399.1, ECO:0000313|Proteomes:UP000054681};
RN [1] {ECO:0000313|EMBL:KRX56399.1, ECO:0000313|Proteomes:UP000054681}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ISS409 {ECO:0000313|EMBL:KRX56399.1};
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:KRX56399.1}.
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DR EMBL; JYDN01000123; KRX56399.1; -; Genomic_DNA.
DR EMBL; JYDN01000123; KRX56402.1; -; Genomic_DNA.
DR STRING; 181606.A0A0V0UYN4; -.
DR Proteomes; UP000054681; 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 Coiled coil {ECO:0000256|SAM:Coils};
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:UP000054681};
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:KRX56399.1}.
FT DOMAIN 655..714
FT /note="SH3"
FT /evidence="ECO:0000259|PROSITE:PS50002"
FT REPEAT 1184..1217
FT /note="TPR"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00339"
FT DOMAIN 1364..1499
FT /note="Fido"
FT /evidence="ECO:0000259|PROSITE:PS51459"
FT REGION 591..620
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 716..801
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 823..881
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 513..540
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 745..786
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 787..801
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 823..840
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 843..881
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT LIPID 1686
FT /note="Phosphatidylserine amidated glycine; alternate"
FT /evidence="ECO:0000256|PIRSR:PIRSR604241-50"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KRX56399.1"
SQ SEQUENCE 1686 AA; 190273 MW; F8739E06F26A5AFB 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
KRILEVCCCC CCCCCCTINY ANERMLFDLI QEERRRLLEE KRQFYEEQEQ RSVVSERLPR
PPPAAANGLY SSTMSRSRPD LYRETTLREQ ESRRHFSPSN VTDDASFFFE QARARGSQIA
QVVYERHGMN EKELTVRKGE FLEVLNNKKN WWECRNAHRQ VGFVPHTILS VVDSGIHHNS
TPHQQSKSFD EPLFVRPPPP STSTFGPAMG NSATAFGSYE DDSSARRSSP VTRTATPANN
SGDTPEVIRQ RRGKLDEPKN KEVMMFSSTC LVNSKRPYVA CAPPVPPPAP PPPPPPLPRT
SGGAEAVSSS TGEKKASTSN GTIPHGLSKE NGTSIRNGKV PSNVTVDSRR MLNEELLMTL
NKSNLKGSFD FKAKPWPNSS LVTVQEMSSI STKQDVAEWL QAKCFSGRAI NLLREHDGEK
LLSMNKIQLE ELIGREEGAR LYSQLQLQKT TAKYLMKSDD SQLSSILATR RNLNEEKMDD
DKSLESQIYV VHVMQLVPNK TYKLMKIEAD AVFSYDGEWF SILMMNGRDV LSRYTMIKVC
VEKSLKSFAM PKSIFSYNWY TLAVLVLLVA VIAYQTLHLL NNNNRSWLSD YLLHCFKSNQ
KNVSKYLSRE VAFYLSSFDM PSPVEDTSVS QSSLVPAKGT ESEALAVLQA AELFLKSGKV
DKARKLFEHA VFLQPQHPDI LTGYGLFTEK IGGDVVKANF MFSRALIYSP DHSLAKWHKG
RTQPIVQEID AEMMRILDQK RNKFLRIPRG SSGLRRAMRE AYFSHIYHTV AMEGNTMNFV
QTKSLLETRM AIGGKSILEH NEILGMDAAL RFVNQSLIHR IGSLSVEDIL DIHRRVLGFV
DPVESGRFRT HQVYIGSFEP SLPENIEKEV DELLEWLNSD TAMSIHPVEL AALLHYKFVV
IHPFVDGNGR TSRLLMNLIL MQAGFPPVII RVEDRLQYYE SLKLANEGDL RPFVRFIAEC
TRRTLDEYLA NSMCSVDEAS NPLEPIVDNG RTIILPKVLA HFLDIPLNET FIAVFIATQV
CLTMNSMGGG LTFRQRRPYN TRVREIQEIR RAYPDKIPIV IERFEGEKYL PVLDRCKFLV
PDHVTMTELM QIVRRRLELH PEQALFLLVN EKSLVSHSTT LAELYEAEKD TDGFLYIVYT
SQPGFG
//
