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Database: UniProt
Entry: A0AAD9IZQ6_9ANNE
LinkDB: A0AAD9IZQ6_9ANNE
Original site: A0AAD9IZQ6_9ANNE 
ID   A0AAD9IZQ6_9ANNE        Unreviewed;      1280 AA.
AC   A0AAD9IZQ6;
DT   29-MAY-2024, integrated into UniProtKB/TrEMBL.
DT   29-MAY-2024, sequence version 1.
DT   28-JAN-2026, entry version 8.
DE   RecName: Full=Integrase catalytic domain-containing protein {ECO:0000259|PROSITE:PS50994};
GN   ORFNames=LSH36_803g00021 {ECO:0000313|EMBL:KAK2143892.1};
OS   Paralvinella palmiformis.
OC   Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Annelida; Polychaeta;
OC   Sedentaria; Canalipalpata; Terebellida; Terebelliformia; Alvinellidae;
OC   Paralvinella.
OX   NCBI_TaxID=53620 {ECO:0000313|EMBL:KAK2143892.1, ECO:0000313|Proteomes:UP001208570};
RN   [1] {ECO:0000313|EMBL:KAK2143892.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=P08H-3 {ECO:0000313|EMBL:KAK2143892.1};
RX   PubMed=37494294; DOI=10.1093/molbev/msad172;
RA   Perez M., Aroh O., Sun Y., Lan Y., Juniper S.K., Young C.R., Angers B.,
RA   Qian P.Y.;
RT   "Third-Generation Sequencing Reveals the Adaptive Role of the Epigenome in
RT   Three Deep-Sea Polychaetes.";
RL   Mol. Biol. Evol. 40:msad172-msad172(2023).
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:KAK2143892.1}.
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DR   EMBL; JAODUP010000803; KAK2143892.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0AAD9IZQ6; -.
DR   Proteomes; UP001208570; Unassembled WGS sequence.
DR   GO; GO:0005581; C:collagen trimer; IEA:UniProtKB-KW.
DR   GO; GO:0031012; C:extracellular matrix; IEA:TreeGrafter.
DR   GO; GO:0005615; C:extracellular space; IEA:TreeGrafter.
DR   GO; GO:0030020; F:extracellular matrix structural constituent conferring tensile strength; IEA:TreeGrafter.
DR   GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR   GO; GO:0015074; P:DNA integration; IEA:InterPro.
DR   GO; GO:0030198; P:extracellular matrix organization; IEA:TreeGrafter.
DR   Gene3D; 2.60.120.200; -; 1.
DR   Gene3D; 3.40.1620.70; -; 1.
DR   Gene3D; 3.10.100.10; Mannose-Binding Protein A, subunit A; 1.
DR   Gene3D; 3.30.420.10; Ribonuclease H-like superfamily/Ribonuclease H; 1.
DR   InterPro; IPR016186; C-type_lectin-like/link_sf.
DR   InterPro; IPR008160; Collagen.
DR   InterPro; IPR050149; Collagen_superfamily.
DR   InterPro; IPR010515; Collagenase_NC10/endostatin.
DR   InterPro; IPR013320; ConA-like_dom_sf.
DR   InterPro; IPR016187; CTDL_fold.
DR   InterPro; IPR001584; Integrase_cat-core.
DR   InterPro; IPR012337; RNaseH-like_sf.
DR   InterPro; IPR036397; RNaseH_sf.
DR   InterPro; IPR048287; TSPN-like_N.
DR   InterPro; IPR045463; XV/XVIII_trimerization_dom.
DR   PANTHER; PTHR24023; COLLAGEN ALPHA; 1.
DR   PANTHER; PTHR24023:SF1113; COLLAGEN ALPHA-2(IX) CHAIN-LIKE ISOFORM X1; 1.
DR   Pfam; PF01391; Collagen; 2.
DR   Pfam; PF20010; Collagen_trimer; 1.
DR   Pfam; PF06482; Endostatin; 1.
DR   SMART; SM00210; TSPN; 1.
DR   SUPFAM; SSF56436; C-type lectin-like; 1.
DR   SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 1.
DR   SUPFAM; SSF53098; Ribonuclease H-like; 1.
DR   PROSITE; PS50994; INTEGRASE; 1.
PE   4: Predicted;
KW   Collagen {ECO:0000256|ARBA:ARBA00023119};
KW   Reference proteome {ECO:0000313|Proteomes:UP001208570};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT   DOMAIN          1016..1108
FT                   /note="Integrase catalytic"
FT                   /evidence="ECO:0000259|PROSITE:PS50994"
FT   REGION          240..390
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          490..823
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        240..256
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        264..274
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        340..349
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        351..361
FT                   /note="Low complexity"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        362..372
FT                   /note="Gly residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        490..503
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        509..526
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        528..542
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        544..557
FT                   /note="Low complexity"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        677..686
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        740..785
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        792..807
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1280 AA;  135006 MW;  864C8DDAFDE483F8 CRC64;
     MDLMQAIDPP RGSPLGQITD ITNISGNDSI SYLKGIDGYP AFLIKRNANI QKPAAAFLTT
     LPDDFAILIT VIPSDDLGGF LFSVVNPAST IIQLGVSLSP SSSEGMMDIK LYYTDYRKSE
     TSEVLVRFSV PSFVHQWTSI GLKIKNDVVT LYMDCMEYSR SETTGRKRGL RFDSGSSLFI
     GRGPIQNEKS FAGGLQQLTI VEDADKAESQ CDDIDPYQEF SGSPDTSIIP RPGSRYMIKG
     EKGDRGAPGL KGDRGPPGET VFITPPPITP PPPDFLGTKG EKGERGLQGP KGDRGTTGVK
     GDKGDTGIPG IPGTGEQGLP GPPGLPGLPG KIGERGLPGP AIPGPPGPPG RDGIPGPRGL
     PGTPGGNLGS GEDGTNLPGI SGLPGKPGVA GPRGEKSCTY LRAVHISELY LSQSCTYLRA
     ELISELYLSQ SCTYLRAVLI SELYLTQSCS YLRAVLISEL YLSQSCTYLR AVLNSELYLS
     QSCTYLRAGD RGDQGLRGHD GRDGMPGTPG LPGPPGPPGP PGPPSYIPEE EIFGGSGDED
     ELLPSYPSGG SSGSVYPTWK GDRGFPGTPG LPGPRGPPGR DGTPGLSGTP GDSGQPGPRG
     QKGDMGNPGI GTPGLPGSPG LQGPPGPPGR VVTAKGVDIT GPPGYPGQKG NKGEPGEGSS
     RSCNDICYGV KGEIGPQGPP GSPGPRGPAG IMGEIGLPGF PGKPGDRGLP GLAVKGSKGD
     RGSPGPPGTV VGDSGGIYIP APPGPPGPPG PPGHCPPGPP GPPGVGVPGP PGPPGNVPRP
     EPPGHPADSP VQCPPGPPGP PGPPGPPGTG NGNTIIPSFG GDEQFTPGAG AVIFRNKDDL
     FMVAHNIPFG TIIFLLDTEV LYVRVSEGFR EILTKVEYFP ANHFVQPTTP EPEIIPPPQD
     TSEITGPMIQ FALESRLKKC KQANMPRAAA EDGCPWTPNI SVYAHKPLSK TPKAITKSDT
     TSDEILNRVQ TKKKHSDRRY PVSTSTVQEM HVHNVTLHPM RDEDKQQQES KVITAVPPRP
     WQKVASDLFA WGGNDYSICT DYYSSFFEID VLGETTSGEV IAKLKNSCAR YGIPETRVSD
     NGSQYSSTSF SAFLKNGIFI NGSSTPLHLI AANQPYKGDI NGISGADYIC FKEAKAIGLQ
     GTYRAFLSSR VQDLISIVHR KYDRKFPVVN LHNQKLFNSW NDIFNGAGAY FNDRVPIYSF
     DGKDVLYDPK WPQKIIWHGA TSTGQRNEKS YCNAWSSESS TETGVASSLI KSMILDNEQF
     ACNNGFILLC AENSYRTYRK
//
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