ID A0A085NTN9_9BILA Unreviewed; 2902 AA.
AC A0A085NTN9;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 27-MAR-2024, entry version 44.
DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:KFD72835.1};
GN ORFNames=M514_14739 {ECO:0000313|EMBL:KFD72835.1};
OS Trichuris suis (pig whipworm).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Trichinellida; Trichuridae; Trichuris.
OX NCBI_TaxID=68888 {ECO:0000313|EMBL:KFD72835.1};
RN [1] {ECO:0000313|EMBL:KFD72835.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DCEP-RM93F {ECO:0000313|EMBL:KFD72835.1};
RX PubMed=24929829; DOI=10.1038/ng.3012;
RA Jex A.R., Nejsum P., Schwarz E.M., Hu L., Young N.D., Hall R.S.,
RA Korhonen P.K., Liao S., Thamsborg S., Xia J., Xu P., Wang S.,
RA Scheerlinck J.P., Hofmann A., Sternberg P.W., Wang J., Gasser R.B.;
RT "Genome and transcriptome of the porcine whipworm Trichuris suis.";
RL Nat. Genet. 46:701-706(2014).
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DR EMBL; KL367475; KFD72835.1; -; Genomic_DNA.
DR UniPathway; UPA00189; UER00296.
DR Proteomes; UP000030758; Unassembled WGS sequence.
DR GO; GO:0042575; C:DNA polymerase complex; IEA:UniProt.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0019899; F:enzyme binding; IEA:UniProt.
DR GO; GO:0003921; F:GMP synthase activity; IEA:InterPro.
DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0015074; P:DNA integration; IEA:InterPro.
DR GO; GO:0006541; P:glutamine metabolic process; IEA:UniProtKB-UniRule.
DR CDD; cd01742; GATase1_GMP_Synthase; 1.
DR CDD; cd00303; retropepsin_like; 1.
DR Gene3D; 3.30.300.10; -; 2.
DR Gene3D; 3.30.70.270; -; 1.
DR Gene3D; 3.40.50.880; -; 1.
DR Gene3D; 3.10.10.10; HIV Type 1 Reverse Transcriptase, subunit A, domain 1; 1.
DR Gene3D; 3.40.50.620; HUPs; 1.
DR Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 3.
DR Gene3D; 3.30.420.10; Ribonuclease H-like superfamily/Ribonuclease H; 3.
DR Gene3D; 4.10.60.10; Zinc finger, CCHC-type; 1.
DR InterPro; IPR029062; Class_I_gatase-like.
DR InterPro; IPR043502; DNA/RNA_pol_sf.
DR InterPro; IPR017926; GATASE.
DR InterPro; IPR004739; GMP_synth_GATase.
DR InterPro; IPR025777; GMPS_ATP_PPase_dom.
DR InterPro; IPR001584; Integrase_cat-core.
DR InterPro; IPR022310; NAD/GMP_synthase.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR043128; Rev_trsase/Diguanyl_cyclase.
DR InterPro; IPR001763; Rhodanese-like_dom.
DR InterPro; IPR012337; RNaseH-like_sf.
DR InterPro; IPR036397; RNaseH_sf.
DR InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR InterPro; IPR000477; RT_dom.
DR InterPro; IPR001878; Znf_CCHC.
DR InterPro; IPR036875; Znf_CCHC_sf.
DR PANTHER; PTHR11922:SF2; GMP SYNTHASE [GLUTAMINE-HYDROLYZING]; 1.
DR PANTHER; PTHR11922; GMP SYNTHASE-RELATED; 1.
DR Pfam; PF00117; GATase; 1.
DR Pfam; PF02540; NAD_synthase; 1.
DR Pfam; PF00098; zf-CCHC; 1.
DR SMART; SM00343; ZnF_C2HC; 1.
DR SUPFAM; SSF52402; Adenine nucleotide alpha hydrolases-like; 1.
DR SUPFAM; SSF52317; Class I glutamine amidotransferase-like; 1.
DR SUPFAM; SSF56672; DNA/RNA polymerases; 1.
DR SUPFAM; SSF54810; GMP synthetase C-terminal dimerisation domain; 2.
DR SUPFAM; SSF57756; Retrovirus zinc finger-like domains; 1.
DR SUPFAM; SSF53098; Ribonuclease H-like; 2.
DR PROSITE; PS51273; GATASE_TYPE_1; 1.
DR PROSITE; PS51553; GMPS_ATP_PPASE; 1.
DR PROSITE; PS50994; INTEGRASE; 2.
DR PROSITE; PS50206; RHODANESE_3; 1.
DR PROSITE; PS50878; RT_POL; 1.
DR PROSITE; PS50158; ZF_CCHC; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU00886};
KW Glutamine amidotransferase {ECO:0000256|ARBA:ARBA00022962,
KW ECO:0000256|PROSITE-ProRule:PRU00605};
KW GMP biosynthesis {ECO:0000256|ARBA:ARBA00022749, ECO:0000256|PROSITE-
KW ProRule:PRU00886}; Ligase {ECO:0000256|ARBA:ARBA00022598};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|PROSITE-ProRule:PRU00047};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU00886};
KW Purine biosynthesis {ECO:0000256|ARBA:ARBA00022755, ECO:0000256|PROSITE-
KW ProRule:PRU00886}; Signal {ECO:0000256|SAM:SignalP};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius};
KW Zinc {ECO:0000256|PROSITE-ProRule:PRU00047};
KW Zinc-finger {ECO:0000256|PROSITE-ProRule:PRU00047}.
FT SIGNAL 1..17
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 18..2902
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5001796163"
FT TRANSMEM 135..164
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 441..456
FT /note="CCHC-type"
FT /evidence="ECO:0000259|PROSITE:PS50158"
FT DOMAIN 656..866
FT /note="Reverse transcriptase"
FT /evidence="ECO:0000259|PROSITE:PS50878"
FT DOMAIN 1130..1251
FT /note="Integrase catalytic"
FT /evidence="ECO:0000259|PROSITE:PS50994"
FT DOMAIN 1316..1375
FT /note="Integrase catalytic"
FT /evidence="ECO:0000259|PROSITE:PS50994"
FT DOMAIN 1797..2011
FT /note="GMPS ATP-PPase"
FT /evidence="ECO:0000259|PROSITE:PS51553"
FT DOMAIN 1815..1865
FT /note="Rhodanese"
FT /evidence="ECO:0000259|PROSITE:PS50206"
FT REGION 1488..1555
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1488..1506
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1515..1544
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 1684
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT ACT_SITE 1770
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT ACT_SITE 1772
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT BINDING 1824..1830
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00886"
SQ SEQUENCE 2902 AA; 325277 MW; 5886B9911F821818 CRC64;
MHRISGLLAT FIVIAIGVDD FSKYPENLAN LYLINKNGSY YFTFDSEEYY SMKKNAVAMS
VALVPFVDIN HVKNVQWRLI NSMAFSGNFA LGTQLNVSSA IVLEELLNGS FLDNNSTVNG
NVSSFSKDVN IRWPFWQIAF VAGSTMATGF IVMAFVGAVT LTYCRWKKHG HSNKGSIYSV
PERWDSLSLN YINNPNDLWK GSMDDLADDA YLARLDKEMA RRIACMHAYR NPIVNSCETN
YRGLMEAPFA GKVFDVKLIP EFDGSSQPVL EWLEKLELVC ELCGIVDIAR VLPLRLTGGA
LAVYQQLANE DRKDVGRIKE ALTAAFAVDR FAAHRQFASR RLNMGESPDV FLADLRRLGT
LAGGVSESFL GCAFVAGLPE YVQDLLRAGA RMEELTLNQL VARARAVMVN EISTCEKNDG
LAAGAAEASL RIASRKPAIQ CYACGGANHF ARECPKRNSV RTSARPRKKA LPTALMKVDG
VLRRALVDTG STRCIIYAPC CRSWRKQQIH VTTVSGEQLH CIGVGSVKLQ LSEGEPVTIE
GVIADKKPLG FDVIIGMNGI SALGGVTVNA QGQVQFGTAK AVVVASAAAS IRVDEKDFVA
TYDPATNTWT TAWKWANDAA PEVLRNTKEE FPLPEGIREA YTEELEQWIQ NGWLIPYDES
KFGPAKALIP LMAVIQRSKG KVRPVMDFRE LNSYIDTYTA KSDVCAQMLR EWRRQGVNVS
ILDLRKAYLQ VCVDRTLWPY QTVVVKDRRY CLTRLGFGLN VAPMIMKAVI SRVLSLDPDI
QKGTSAYIDD IFVNENVVSA NHVIQHLAKY GLSCKVPERV ADGARVLGLN VRGQQGTLVW
SRGNETGEPP KPLTRRTVFA YCGALVGHYP VCGWLRPATA FIKREANRVT SRWDEPILDE
QVQEHLREIA ARLKVHDPAQ GRWDVASTKV RLWVDASALA LGVVLEVNGA VIEDAAWLRS
DDTQHINMAE LDAVIKGLNL GLSWQMKDIE LMTDSLTVHR WLNDSHSGRT RLKTKAASEM
LIRRRMATIL ALVEEHNLNL GVTLVRFAET LKNALTRVPR RWLTPTERTE VAACVSAAAS
QTDQLIAEIH CTSGHPGVKR TLYFAKRRDP TVSKTQKNRV VSNCHICRSI DPAPVKWRHG
NHGVAGWRQR VSIDVTQFRG KAYLTLIDCG PSRFAIWRPL KYHTSVDICE QLESIFCERG
APDELLADND TAFRSQIFSK LVERWNLRLR FRCAYAPSGN GIIERCHRSV KVIAARKGCA
VCEAVYWYNL MPRDDCSEAT APANAIYRYP VRVRGVDSVV HEAQDVRSPV DICEQLESIF
CERGAPDELL ADNDTAFRSQ IFSKLVERWN LRLRFRCAYA PSGNGIIERC HRSVKVIAAR
KGCAVCEAVY WYNLMPRDDC SEATAPANAI YRYPVRVRGV DSVVHEAQDV RSPYVIGDEV
WIKQPGRKCY SQFGRGIVTK VLSGQAVEVD GTPRHIKDIR RQTTLHLERQ SEPETCRHES
EEETLLYLPE RNQVIDSERA TSPATSSPPQ EEAPDTSQAL EPQETGPRRS KRTRRSRHCY
GIQLMSEKPS ANCVNVNGSV KRFAGENSPK AVENTVHMDD GTDRPCDLVA ILDCGAQYGK
VIDRRVRELC VGTDMLPLST SVDKLLGRYK AIIISGSPHS VYETTAPVYD RRIFHCGIPV
LGICYGFHLI NMEFGGTVEK KPIREDGQHT IWIDQTCPLF KNLKQHEVVL LTHGDSIDKI
APSFNVIARS GDLVAGMANV NAGIYGVQFH PEVDLTISGK TILQNFLFCL AGCQPTFTME
NRMQACLDHI QKEVKDKRVI VLCSGGVDSS VCAALLNRAL GKEKVVAVFV DTGFLRKNET
ETVVESLLSC GVNVKVLQKS LEFYYASPHC GDTSMAAVEN LMLNRTVDPE MKRRIIGDTF
MMIVKEVMTE LNLSFGQVYL AQGTLRPDLI ESASSIASMH ANVIKTHHND TRVVRQLRQR
GYIIEPLKDF HKDEVRCLGR DLGLPETILE RHPFPGPGLA VRIICRIEPF IPIQFQDTQN
ILRRILSLNE NMTEAHVDLL LLFVYNDLET LFKIPDEIFA TLLPIQSVGV QGDRRSYSFV
VALSTDQKKT PWKALFFLSK VIPRLLQNVN RVVYAFGTAV RHPVLDITPT FLTSNVIHIA
READYIANKV AEVYNIRKSI SQMPVVLLPI HFDRSDGIQK SPSFKWSICL RPVITSDFMT
CLPAYPGSHI PEEVHRSILV KNGRRVKSFH LTEMESTSAA ADRCDDSSLQ RSRLRNGKIR
QRKVTNDITS FVRSNPKATC NYRMGIASVY AWPLHTQCSR KKPCDRFFFV KMTCPRRTKP
QLSRPSASAA MKARKALMRR LQKQEVRRLQ SALPPEVRRR RGLNEIQVIN EATRYIDQLH
NVIVARVKAG LLPPGLETIL LSCVPPDDEV RMDFDSQKEC LEFEGRLLEA KQWKTRLFIA
RQCSHCSAAS QLKVYKKGKL KKTINLDECY GMESVFRISL FRPFDLPTFG LMTQTCLSLV
SYASVGSEKP LDPGIRSALG RIGASGFPTD PVEAMLECPR SKGDGQMAGV TCEELMQKRS
SDGNMICGSP LNGAQIQWLG VLIHGEVFTL SVICLCDTLV IAFNHENSLL EFESWLRGYL
GFSKNCQCSL KFYAIHFVSR ILHLQDSRFC LVTGIPGSVM LKFFISDLQC YGAIRNKFCF
QVKSDYNSTP PGRPLKYNTG FVFEVVPLLY DGQSHDCLNE LQNFDSATTV AREGSFSCRS
LRKELPCNCR KPKVKSSLSL NNEVNDTFSC ESGGYLIRMY SDSLLGSPPP KMCHRCFQHK
YINQAFVDSL EFYDNCKFTR NYGVVSVLFM VSIESFIDLH VLKEKSKVHD GDVEACSEHL
NILRREFPTR VEGIVGMEIP VG
//
