ID   A0A085NM07_9BILA        Unreviewed;      1227 AA.
AC   A0A085NM07;
DT   29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   29-OCT-2014, sequence version 1.
DT   27-MAR-2024, entry version 25.
DE   RecName: Full=Integrase catalytic domain-containing protein {ECO:0000259|PROSITE:PS50994};
GN   ORFNames=M514_01000 {ECO:0000313|EMBL:KFD70503.1};
OS   Trichuris suis (pig whipworm).
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC   Trichinellida; Trichuridae; Trichuris.
OX   NCBI_TaxID=68888 {ECO:0000313|EMBL:KFD70503.1};
RN   [1] {ECO:0000313|EMBL:KFD70503.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DCEP-RM93F {ECO:0000313|EMBL:KFD70503.1};
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; KL367487; KFD70503.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A085NM07; -.
DR   Proteomes; UP000030758; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0004066; F:asparagine synthase (glutamine-hydrolyzing) activity; IEA:InterPro.
DR   GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR   GO; GO:0006529; P:asparagine biosynthetic process; IEA:InterPro.
DR   GO; GO:0015074; P:DNA integration; IEA:InterPro.
DR   GO; GO:0006541; P:glutamine metabolic process; IEA:UniProtKB-KW.
DR   CDD; cd01991; Asn_Synthase_B_C; 1.
DR   Gene3D; 3.40.50.620; HUPs; 1.
DR   Gene3D; 3.30.420.10; Ribonuclease H-like superfamily/Ribonuclease H; 2.
DR   InterPro; IPR001962; Asn_synthase.
DR   InterPro; IPR001584; Integrase_cat-core.
DR   InterPro; IPR012337; RNaseH-like_sf.
DR   InterPro; IPR036397; RNaseH_sf.
DR   InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR   PANTHER; PTHR45937; ASPARAGINE SYNTHETASE DOMAIN-CONTAINING PROTEIN 1; 1.
DR   PANTHER; PTHR45937:SF1; ASPARAGINE SYNTHETASE DOMAIN-CONTAINING PROTEIN 1; 1.
DR   Pfam; PF00733; Asn_synthase; 1.
DR   SUPFAM; SSF52402; Adenine nucleotide alpha hydrolases-like; 1.
DR   SUPFAM; SSF53098; Ribonuclease H-like; 2.
DR   PROSITE; PS50994; INTEGRASE; 1.
PE   4: Predicted;
KW   Glutamine amidotransferase {ECO:0000256|ARBA:ARBA00022962};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        153..173
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          826..933
FT                   /note="Integrase catalytic"
FT                   /evidence="ECO:0000259|PROSITE:PS50994"
FT   REGION          1..31
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          914..934
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1111..1142
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1173..1207
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..20
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1121..1142
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1173..1200
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1227 AA;  138206 MW;  B5B14A19D9F5793A CRC64;
     MSDADARKSS SPQCLEITGA LSSPTDPVER RPLDGEITEL SEHAHSFVSI SQHGLSGPLR
     GRRWSKEWSR AADVDVSERM LNAGGSPALP FLTLFFGWGV VSANQLMRNC PITMETGRCV
     SHTSTINISS LLNALETDGI VETMRKVDGP WTLVFYMVVR FTAPIILAVY ITLVVQSKEN
     CLWFGRDCFG RKSLLLYDSI AQEPHLGQEG KLLILSTLHP VDLPGNSVEV PVGRLYCLKL
     SDMTYSVFQL FSSTPLAVSS CVPGIMPSGI TKYEDFNGLF SVSKTSTNSS EERKSREHDE
     KDLIKHFIKE NKVEIEELIA RLRRSISCQL NVLPHQSFCG TKSPETTAAT VSVLFSGGID
     SLLIAVLLGT VLPAGSEVDL LNVAFTVDEL HNCSSTVPDR QTGIKGYMAL KARCSHVHWN
     LLLVDVTKKE LYDPTVQLHV RRLIKPACTV RDESIGYAIW FASKGKGILY EKASLTDRKD
     QIQSSARILF LGSGADELFA GYMRHRSCFA EGGYNALAVT LEEELFRIGH RSLSLCDRMI
     SDHCLLVHLP YLNENFVRYV NNIPLDVKTD LSLARGLGDK LILRAALWLL GYEEFCFSLK
     RAIQFGSRIA KVSGSKGKVF SYCGELVGHY PVCGWLRVAT AFIKREANRV SSRWDEPIHD
     DRIQEHLDGV AREVTKNDPV CGVALEVDNS VIEDGVWLRP SDARHINMAE LDAVIKGLNL
     AIAWRMGTIE LMTDSAAVHR WLSDGVSKTV LALVRQYQLT TTVTLVWSME NKADRRTRVP
     RRCEKSFERL IAEVHHAAGY PGVRRTLYFA RRRDPGIAKR EWRYGGLEVP KVWQRGGVDV
     MHWGKELYLT LIDCGPSRFC IWRRLSQHSS TEIARHLESV FYERGAPEEL LTDNDTAFQS
     NEISVCLRRM RQRHNGTVPS DDQSDREEDR IHGPGSRLSV RRGIACGNGI TERCHRTIKV
     IARRTGFTVQ EAVYRQRYLP IHRKGSGGIV DLLHRAKHTL PVCRCDSVWI RPHANGCDTR
     YDNVFVTRVI SDQTMEVDGM PRHVGDIRRR TGTPRQPLGL TFDASGRGVI ELHVTRYEDE
     PGTIRFTVAA EPQPAEQPVT DNSVSQESLQ TLQEEGTCAS TRAGERMRRG REDETGAERE
     QRLRANRERM RTTRARLRGE PEAEDVAVRE AQRLRKRRGE KTEAERSMRR RVDREHGRSV
     RQNVASMSRR ESISLRCFSA HSKMNKC
//