ID A0A1A9ZZF1_GLOPL Unreviewed; 3327 AA.
AC A0A1A9ZZF1;
DT 05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2016, sequence version 1.
DT 27-MAR-2024, entry version 37.
DE RecName: Full=Chromo domain-containing protein {ECO:0008006|Google:ProtNLM};
OS Glossina pallidipes (Tsetse fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Hippoboscoidea;
OC Glossinidae; Glossina.
OX NCBI_TaxID=7398 {ECO:0000313|EnsemblMetazoa:GPAI029678-PA, ECO:0000313|Proteomes:UP000092445};
RN [1] {ECO:0000313|Proteomes:UP000092445}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IAEA {ECO:0000313|Proteomes:UP000092445};
RA Aksoy S., Warren W., Wilson R.K.;
RL Submitted (MAR-2014) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EnsemblMetazoa:GPAI029678-PA}
RP IDENTIFICATION.
RC STRAIN=IAEA {ECO:0000313|EnsemblMetazoa:GPAI029678-PA};
RG EnsemblMetazoa;
RL Submitted (MAY-2020) to UniProtKB.
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DR STRING; 7398.A0A1A9ZZF1; -.
DR EnsemblMetazoa; GPAI029678-RA; GPAI029678-PA; GPAI029678.
DR VEuPathDB; VectorBase:GPAI029678; -.
DR Proteomes; UP000092445; Unassembled WGS sequence.
DR GO; GO:0005694; C:chromosome; IEA:UniProt.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0140658; F:ATP-dependent chromatin remodeler activity; IEA:InterPro.
DR CDD; cd18668; CD1_tandem_CHD5-9_like; 1.
DR CDD; cd18663; CD2_tandem_CHD5-9_like; 1.
DR CDD; cd17995; DEXHc_CHD6_7_8_9; 1.
DR CDD; cd18793; SF2_C_SNF; 1.
DR Gene3D; 2.40.50.40; -; 2.
DR Gene3D; 1.10.10.60; Homeodomain-like; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR Gene3D; 3.40.50.10810; Tandem AAA-ATPase domain; 1.
DR InterPro; IPR016197; Chromo-like_dom_sf.
DR InterPro; IPR000953; Chromo/chromo_shadow_dom.
DR InterPro; IPR023780; Chromo_domain.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR001650; Helicase_C.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR038718; SNF2-like_sf.
DR InterPro; IPR049730; SNF2/RAD54-like_C.
DR InterPro; IPR000330; SNF2_N.
DR PANTHER; PTHR45623; CHROMODOMAIN-HELICASE-DNA-BINDING PROTEIN 3-RELATED-RELATED; 1.
DR PANTHER; PTHR45623:SF11; KISMET, ISOFORM C; 1.
DR Pfam; PF00385; Chromo; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR Pfam; PF00176; SNF2-rel_dom; 1.
DR SMART; SM00298; CHROMO; 2.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00490; HELICc; 1.
DR SUPFAM; SSF54160; Chromo domain-like; 2.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR PROSITE; PS50013; CHROMO_2; 1.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR PROSITE; PS51194; HELICASE_CTER; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Helicase {ECO:0000256|ARBA:ARBA00022806};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT DOMAIN 1987..2043
FT /note="Chromo"
FT /evidence="ECO:0000259|PROSITE:PS50013"
FT DOMAIN 2088..2262
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 2401..2552
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 1..58
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 98..694
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 709..821
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 842..879
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1005..1056
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1250..1283
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1331..1698
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1723..1800
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1817..1836
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1850..1901
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2671..2712
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 3024..3081
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 3226..3292
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 107..283
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 296..352
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 370..395
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 403..419
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 421..446
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 447..542
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 561..628
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 643..694
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 709..747
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 759..821
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1017..1055
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1365..1385
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1407..1430
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1574..1600
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1631..1661
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1668..1687
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1725..1800
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 3042..3070
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 3226..3262
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 3327 AA; 366956 MW; EFD14AD8F4FD5EA4 CRC64;
MDGNAQNMFH GNHQGDPYYR YDPGASPRAM GPPGGYPPRH RAPHPLQQQS QYPAYQPTPE
NIYGLGAADQ LAGMGMGELT GWGAAPTVPG QASAYPGTAI GAYGHPQAGP STQQRQSSSQ
PSYRQHMPAY GQQEQQKLPY GPQQGMMSSL LQQPGSNVGA GGYSALTQQP QQQQATTAQQ
QQQQSQQSRL PQHYPQPPTQ HQLYPGGPTQ GQTGGPSNVP SGPQTYSHSP YTASMHQQTG
RSSQHGGYGH AGLDQSSSYS QHATTAPVSV PSHHLSGQQQ VVQLGAHPVA HMGPGPQQQQ
PPTGLQHGVT NLGPPQQQQG SAHLLQGQQS QQQQQQPQQQ QPPQNHVGLM NQHQQLPPPH
GMAVPSSYGG HHQQPPQQQA QQQQPPSQQP QVGGAPAYIP SSGKHQATAS PQYRAPFPQL
SPQMSPRPPT MSPHPQMSPR PGISPAKPPS TQQQQQQQGT QSSTQQQPSS QQQQQPTHHS
ISGMVGLTSP RQQTSTANSG GSVPGSKSGG SGQPVNTLQA LEQMVMPSQS MSGGTLDYPS
PYRQSTAGHG PMGPRMPVSP QHHQQWPTHL ALPQSQQPMP GGSMSGPQQM QHQQQIHSQQ
SQQMGIYGVP SPAQSQMNHQ QQQQPAPQSS QTQPPPSHVP TLPTPASMNQ AQASQQQQQS
PQQPQQATSQ QQAQPPPSSQ QQTTQHHHQQ QQLNEQLQHS INDIVGNTSS SQQQQLQAAH
ASMSPMHHQH QQHQAQQQQQ PPLSLTSLHH HHHTVHHQMP TENLLSGRST SSQDTQMNSS
VTTTNNQQHH QQHQTHLQLH QQSPLHSSLQ QPITPSTPTQ HHLISGILNE TANSNDSSTL
AIAANDSNNS SSNSSTNSIV NNQPSSLHDS NSQSSINSVS HNAAATLESS TGGNSGGLLN
SNSNSATNAG IGGGSGGGLL ESAGASIFDN NSMSSTNAAG NAPDSAVPIT AAILDSSSQT
SFMGMVDASN VTEKVIKPIE GEENPTEIET ASQTAIPSEI LVEEATAGDT IPKTNKEELS
LKANATAEDT GETSKSKESV AGANSETSKS ADQFGSDIAD KSEAAKPMVD AITHSEKSQP
IPSTQDQAVL LPKTVASGPH LISHQQKQQQ QHPQGIAGMI TPHHVMPPAQ GLSAMGYDGT
QTQTPIQSHA IPSTHGIMQS YGSNHLSYPP YPVLHQQEIA ALQQQLQELY CMPPGQDHQE
KIMRLQERLN LVQQHEVTDQ CSGGPQCPLY QNMPPSLYGT SAMHQPQVIE SPQVSSTTGR
GRGKGTNKPR KPRVKKGDKI QAASEHVTIS GSVVQQSNVI PPNQLPVSED CVTQGAGDTS
VVGLMEYHES GLGDHSQDVH SANELDTSTD AIGKKKSRKP RTPKDPNKPR RERNPKMKKL
KGLEGTEGGG IEILPHQGRK RNNNGGARRK KLPEDNDYDR CAEGSEGEDN KPLVLRSNVN
DLENENKPET TTVDDIKTSS IAEGETPDYD DIPVSKIPKG DDGTGHTNAE VGDETVDSVP
DSAGDSTTTP SRRNKKRSGR GRGDNDGGSA RRRSQLSAKA LKKRRNRGRI VPESDGEDDN
LASTPPPSPP PDSELDTSKR RSSRNTQRKK YIDDVMLRFS DEETTSLMNT SPLKKEKKAV
SIAVPICSAS SDVEKTEQGA SNSGGEGAAS DQPSTSDDKI SMTGEDGGEG SSGATSTSTN
EKSEKQELAV PTISAKPNYV YINTGDEDSM VVQYVLAVRM GKRELLPDPL PEPLKEEEEK
EKGISERKSE ERPEEQEKAL KTNEEKAEKK EEVNEEKQKD SEVIRPDEAL CEDVKETKEN
EEKIEIEAVA KLMELKEESG QQNDNKKIAN HEISSCDKVE KMDVDETELN VKIDENEKTH
YIQEKNEEKE TSASDKNPEE KSSLAETIDS AKNKIDDKES KSVDVKAVKD EKLGEGSKPE
PVFIEVEEFL VKYRNFSYLH CEWRTEEELY KGDRRVGAKI RRFQQKQAQQ INIFDNIEEE
YFNPDFVEVD RVLDMSIHTD EQSGETTKHY LVKWKSLPYE DCTWELEEDV DAEKIEQYLK
FNKVPPRCDW KNKKRPHPDQ WKKLEKTPVF KGGNTLRPYQ LEGLNWLKFS WYNSHNCILA
DEMGLGKTIQ SLTFVHSVYE YGIRGPFLVI APLSTIPNWQ REFESWTDMN VVVYHGSVTS
KQMIQDYEFY LKSESGKILK EPVKFNVLIT TFEMIVTDHM DLKPFSWRLC VIDEAHRLKN
RNCKLLEGLR QLNLEHRVLL SGTPLQNNMS ELFSLLNFLE PSQFSSAEEF MAEFGSLRTE
EEVNKLQALL KPMMLRRLKD DVEKSLAPKE ETIIEVELTN IQKKYYRGIL EQNFAFLKKG
TTSANIPNLM NTMMELRKCC IHPYLLNGAE EQIQYDYRVQ HGEDPESYYK NLIQSAGKMV
LIDKLLPKLK ANGHRVLIFS QMVRCLDILE DYLVYRKYPF ERIDGRIRGN LRQEAIDRYS
KPGSDRFVFL LCTKAGGLGI NLTAADTVII YDSDWNPQND LQAQARCHRI GQRKMVKIYR
LLCRNTYERE MFDKASLKLG LDKAVLQSMN THASKDGSNK QLSKKEIEDL LKKGAYGAVM
DDDNAGDKFC EEDIDSILQR RTQVITMESE KGSTFSKASF AASGNRSDIT IDDPDFWTKW
AKKADIDPEI CERDETEDLV LSEPRRRTQI KRYGHEDVMD VNSDDSSNDN SDEEGGIGLR
STRRARKEKR DRCREKKAND DYIPRERDAL AALGLEEIQY GNWAKSECFK VEKGLLSFGW
GRWPEILDLG QFKRGWREID IEDCARIILL YCLQVYKGDE KIKTFIWDLI TPTEDGEIQK
ISRDHSGLHN LVPRGRNGGK TQKEFSTVAG AETTPLIVSP NSTSLVNIPT ATKSSVALIE
KEPIVRSPQN PQDPNHWSKQ DKYDADAYLE GAYKKHLSRH ANKVLLRVRM LYYIQHEVIG
DLVQQIKENT PASELPIRPP TMVDQVPASW WNPACCDKSL LVGTFKHGCE MYRQMRSDPM
LCYVGHVGSA DDALIVTNLP INEDDANSKL EDGDEVDDDG TATKDSDSTK LTTGDNKDSL
DPERPSSSGK NKKLAKSATA DEAIVASEDK ADDKVTVVMA EDQYKRDING SEKDDENITK
TESGDIAKTE LDKVAVVGAV IMSNVIDSAS DSSTAAATEA NSVETTLLEI ETTRTLTTVA
SPKAGFMADI ATVKEASNSG SNANNTCTTT TITSTITNTT TIVTNTSTSS TTTTTNTITS
SSSTSSSNEQ TQNETVNPNS CLGLDEEESG AGSYPPTQIP PEDAATSWPS MQDLNTRLRR
VITAYQRNYK KEELKQQQKA KYWQCEQ
//
