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Database: UniProt
Entry: Q2HI27_CHAGB
LinkDB: Q2HI27_CHAGB
Original site: Q2HI27_CHAGB 
ID   Q2HI27_CHAGB            Unreviewed;      1714 AA.
AC   Q2HI27;
DT   21-MAR-2006, integrated into UniProtKB/TrEMBL.
DT   21-MAR-2006, sequence version 1.
DT   27-MAR-2024, entry version 76.
DE   RecName: Full=Integrase catalytic domain-containing protein {ECO:0000259|PROSITE:PS50994};
GN   ORFNames=CHGG_00127 {ECO:0000313|EMBL:EAQ91892.1};
OS   Chaetomium globosum (strain ATCC 6205 / CBS 148.51 / DSM 1962 / NBRC 6347 /
OS   NRRL 1970) (Soil fungus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Sordariomycetidae; Sordariales; Chaetomiaceae; Chaetomium.
OX   NCBI_TaxID=306901 {ECO:0000313|EMBL:EAQ91892.1, ECO:0000313|Proteomes:UP000001056};
RN   [1] {ECO:0000313|Proteomes:UP000001056}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 6205 / CBS 148.51 / DSM 1962 / NBRC 6347 / NRRL 1970
RC   {ECO:0000313|Proteomes:UP000001056};
RX   PubMed=25720678; DOI=10.1128/genomeA.00021-15;
RA   Cuomo C.A., Untereiner W.A., Ma L.-J., Grabherr M., Birren B.W.;
RT   "Draft genome sequence of the cellulolytic fungus Chaetomium globosum.";
RL   Genome Announc. 3:E0002115-E0002115(2015).
CC   -!- SIMILARITY: Belongs to the aminoglycoside phosphotransferase family.
CC       {ECO:0000256|ARBA:ARBA00006219}.
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DR   EMBL; CH408029; EAQ91892.1; -; Genomic_DNA.
DR   RefSeq; XP_001219348.1; XM_001219347.1.
DR   GeneID; 4387950; -.
DR   VEuPathDB; FungiDB:CHGG_00127; -.
DR   eggNOG; KOG0017; Eukaryota.
DR   HOGENOM; CLU_002055_0_0_1; -.
DR   InParanoid; Q2HI27; -.
DR   OMA; HRMAFTH; -.
DR   OrthoDB; 2554338at2759; -.
DR   Proteomes; UP000001056; Unassembled WGS sequence.
DR   GO; GO:0005634; C:nucleus; IEA:UniProt.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
DR   GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0015074; P:DNA integration; IEA:InterPro.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   CDD; cd05120; APH_ChoK_like; 1.
DR   Gene3D; 3.30.200.150; -; 1.
DR   Gene3D; 3.90.1200.10; -; 1.
DR   Gene3D; 3.30.420.10; Ribonuclease H-like superfamily/Ribonuclease H; 1.
DR   InterPro; IPR002575; Aminoglycoside_PTrfase.
DR   InterPro; IPR001584; Integrase_cat-core.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR012337; RNaseH-like_sf.
DR   InterPro; IPR036397; RNaseH_sf.
DR   PANTHER; PTHR21310; AMINOGLYCOSIDE PHOSPHOTRANSFERASE-RELATED-RELATED; 1.
DR   PANTHER; PTHR21310:SF58; APH DOMAIN-CONTAINING PROTEIN; 1.
DR   Pfam; PF01636; APH; 1.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR   SUPFAM; SSF53098; Ribonuclease H-like; 1.
DR   PROSITE; PS50994; INTEGRASE; 1.
PE   3: Inferred from homology;
KW   Reference proteome {ECO:0000313|Proteomes:UP000001056};
KW   RNA-binding {ECO:0000256|ARBA:ARBA00022884};
KW   Transposable element {ECO:0000256|ARBA:ARBA00022464}.
FT   DOMAIN          743..920
FT                   /note="Integrase catalytic"
FT                   /evidence="ECO:0000259|PROSITE:PS50994"
FT   REGION          1..33
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          147..204
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          414..439
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          988..1065
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..29
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        147..161
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1036..1050
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1714 AA;  193936 MW;  548635EF14209251 CRC64;
     MPQTTSSPEE LDPGSSTPGN SQTGGNPLTP PIPQHILSFV DHSTWGDLAA IDEIEEPTPK
     QMNSHIYFLM EIFWASTSYA GRKLWGAFKD EFDEWTAQRW DMVPDRTRKH LRAFLSTNGV
     IQDLSQLTPT TPTAPATASP VLATIPTQPQ ASQQIPQAIP APRQQNPIPQ TAPKREADWE
     TTSETRQDPQ TWPRPSEEPY YAPRGNAKHL ADLAKLYSDD MKYGGGDYDI LDTKMAIFRD
     LCNRIQIPRW QASDAFPIML KDRALRYYYD WLCSGPRDFD TMVAKIRGYF ENEEQRHRYL
     AAWRDARLIN MQAEHPDKSK SECLELLINR LALIQRAVPA IGQTEDTLRM QLLNACRGVA
     EARMALFNPA PTFEGVRNQL QAAIGITTEN PGPQQFNTDA TDSETFWTDR TYRGSGRESR
     FGRNQGGPRR GGFSNSKFSR PPTERKCFVC GKPGCWSTTH PIEDRKKSYE SLFYWHEGSE
     LEADYEDNPV SQFFQKYDDH DDDTIDNRGK FHSTFFNDSA PADAIQVTTL LANAATHHFL
     TKEDPFQEQD PSETYTAEGR YSATTFRGIM PDSGAAQFST AGQPQFQALQ RQLPSATLDT
     TRAGEAIVKF GYGTPKASLG TTTVPTPLGT IDFHVMETET PFLLCLRDMD RLGIKFDNLR
     NLLQRGDVEV PVTRKWGHPW LQLTQEEALV CSYLTDGELR RLHRRFGHPS VARLYKLLKT
     AGHPVEIQAL ELIAKVCHHC QMHSARPARF KFTLHDDCEF NYEVIMDIFY VEGNKPVLHL
     VDAATAFNAA RFLPDVSTKY VWEALRLCWI DVYQGPPDYV VTDAGKQFAS TEFRQNAKEM
     AITVKEVPIE AHNSIGKVER YHAPVRRAYE ILRKEDPSAS PELSLQMAVK AVNDTAGPNG
     LVPTLLVFGA YPRMTHNSAP SPTLQQRAQA IKKATDAVRR LHAERKVWRE KSRRWEGPFT
     LIGVHDEDCI VETSRGAQKF RSTVVKPYYE DPAQQDDPAN QKDTAEKPAP EVPDSQPRST
     TPPGNAIEEE PILDSIITPH SQSSSLRADG KVTTPGEPFE ESSKQEIESL ITRGVFEFVK
     YDEDLHGDAE IFKSRIVNEI KGKTTDKPYE KSRLVVQGFG DAGKEAILTQ SPTIQRASQR
     LILAIAPSLQ RQGCLLWLRD ITQAYVQSEK ALQRKILAFL PQQIRHLYPE GTVMRVIKPL
     YGLAEAGTYW WTAFSQREND QLKEGVIQRS KDKQFLTTAE PLVFNGGIVT LNKNGSITLR
     QKGQAQKLQL IDANAPDAKQ HAAQHQEPTP DDIKTLNRRI QWQMDSQDRG LTFLPLNLET
     ARLYVFVDGS FANNRDFTSQ LGFAIILANE DEINDRHEFS ITGNLIHFSS TKSKRVTRSV
     LASEVYGMVA GVDMAYALAS TLRQITAHLN LPAIPTIVCT DSYSLYECLV KLGTTKEKRL
     MIDIMALRQS YERRELQEDG SHVRRPLGDY EGDIWGHQLP FGLYLKMVRL AARHESLINE
     HAALQLVRRH TNLPVPRALD LVSNSTEIYL LTTRIPGHKV GLCLDSMSDQ ATRMLVDELR
     GHLAALRDIP MPGDWQYVIA NAAGGPCFDY RIYAAQPGDG TTWVVGPFLS ENDFNQALRC
     GAIPEVVHRS GHRMAFTHGD LNMRNVLVDE YGRLSGVVDW ENAGWFPEYW DYTKAFFVTK
     YNQRWLRMVE DMFGQFGDFQ RELATETELW NYCF
//
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