ID A0A2G5VUP2_9PELO Unreviewed; 2913 AA.
AC A0A2G5VUP2;
DT 31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT 31-JAN-2018, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:PIC55525.1};
GN Name=Cni-chd-7 {ECO:0000313|EMBL:PIC55525.1};
GN Synonyms=Cnig_chr_I.g763 {ECO:0000313|EMBL:PIC55525.1};
GN ORFNames=B9Z55_000763 {ECO:0000313|EMBL:PIC55525.1};
OS Caenorhabditis nigoni.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=1611254 {ECO:0000313|EMBL:PIC55525.1, ECO:0000313|Proteomes:UP000230233};
RN [1] {ECO:0000313|Proteomes:UP000230233}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JU1422 {ECO:0000313|Proteomes:UP000230233};
RA Yin D., Schwarz E.M., Thomas C.G., Felde R.L., Korf I.F., Cutter A.D.,
RA Schartner C.M., Ralston E.J., Meyer B.J., Haag E.S.;
RT "Rapid genome shrinkage in a self-fertile nematode reveals novel sperm
RT competition proteins.";
RL Submitted (OCT-2017) to the EMBL/GenBank/DDBJ databases.
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:PIC55525.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; PDUG01000001; PIC55525.1; -; Genomic_DNA.
DR STRING; 1611254.A0A2G5VUP2; -.
DR Proteomes; UP000230233; Chromosome i.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0140658; F:ATP-dependent chromatin remodeler activity; IEA:InterPro.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR CDD; cd18659; CD2_tandem; 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; 3.40.5.120; -; 1.
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; IPR006576; BRK_domain.
DR InterPro; IPR037259; BRK_sf.
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; IPR001005; SANT/Myb.
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; PF07533; BRK; 1.
DR Pfam; PF00385; Chromo; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR Pfam; PF00176; SNF2-rel_dom; 1.
DR SMART; SM00592; BRK; 1.
DR SMART; SM00298; CHROMO; 2.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00490; HELICc; 1.
DR SMART; SM00717; SANT; 1.
DR SUPFAM; SSF160481; BRK domain-like; 1.
DR SUPFAM; SSF54160; Chromo domain-like; 2.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR PROSITE; PS50013; CHROMO_2; 2.
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 Reference proteome {ECO:0000313|Proteomes:UP000230233};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT DOMAIN 932..1043
FT /note="Chromo"
FT /evidence="ECO:0000259|PROSITE:PS50013"
FT DOMAIN 1051..1118
FT /note="Chromo"
FT /evidence="ECO:0000259|PROSITE:PS50013"
FT DOMAIN 1146..1324
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 1462..1626
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 1..289
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 347..382
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 410..926
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 956..989
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1708..1777
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2229..2259
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2401..2434
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2551..2583
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2818..2861
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 21..43
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 44..70
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 71..87
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 164..182
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 183..204
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 205..242
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 243..257
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 411..425
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 450..465
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 476..525
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 540..573
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 585..620
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 644..676
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 793..819
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 820..845
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 862..882
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 893..922
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 956..975
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1712..1774
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2229..2245
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2913 AA; 323227 MW; 80CCA4D62C08FBB1 CRC64;
MDEGDDYVPQ MSQMTDYTMM GGPPVPPPGQ QQQPPPMPQQ QRYPGQPMNP YEQHQHQMMM
MQQQQHMHQM GPPPVQPPVP PPAAPAKKPR GKSKKAQQAE AAAAAAAAAQ AMDPMASMAA
MSNNPMMNRN PYPNQMGMYG GAGPPPQHYP GANGQQGYRP GPASGGQPPN PYAQPPQQTP
PPTSQNYMYH QQQQQQQQRG PTPQQAQPGY PPPYGYPPQP SPAYPPSQQS PYAPPPQAQM
RHPQFPPHTQ QQQPPGYWDS YPGYGGAPPQ PPATSQPMPT QMPQQEQWAR ANQELLNIIN
QLEKSVHDHK ARINQIYTMP RNATAEAEAQ QLHAKLSALQ ADHYRYSQQL HHQQQQQQWQ
QQQQAAHHQP PPTSSQQQGP VHVAQTGNQV QLNITADKSR TLISVYHEGY GGSGASSTES
KESIVPPEPT PSEVPAKIEE KPAGYPYNGM ENGASSSGMP STSMPPNPYA QQPSQPPPQH
QMYAQYQQQQ HHGQQHPQQH PQQHQQQHQQ QHQQQHQNMN SGYPPHHQQP PHPHQQQPHP
SGYGIGTPSG SSAPPIKQEQ PQHQHQQPQQ QQPFPGYPDY PPSSSGYQKA EQQQQQQSPL
VSDPAPMMPS QPQMSQEMPI QQEAAVIEAP KIEEPYFAAE QEPQEVIPEE KPEVLEEEPT
TSQEVENPKE EEVESSVPAE ASVEAEAPGV ETEEAPYVNG NSDVGPQEEE EGEKEEEPTD
APAPAPAGSQ EEEEKEEEAP RESEESTSSG DSSRSSPGPP IATPDEEETT PVRLEEIENF
SGVQETYGEE EEDDVASSAK SSSKDSKDVE DDDDNLSMNT KDMSEAPSET NDGFTEPSTP
LMGATPSRKK SYKRPAVVVA KSRKKKSIDD SDDDDFYPAR GKGGAKKRGG GGGSRKKVAE
PENNGEAAQK SDDDDDEFLM KIDAPAPDPN AMVVEKILNV RVQKVQVPIQ KEEAEVVKEE
AAETSETKAE TSEAKEEPTT NGASEEVPTE EVEQEQFLIK WKGRAYCHCD WKTLPELLEL
DKRVEAKIKR FKAKKAVSYI EDDEDFNSDF VIVDRVVDYI IEDDGQEFVL IKWKSLGYDE
VTWEPIEHIP EDKVELWRQR QVIDPAKVRD KQRPEPEEWK KLSTKKVWKN GNSLREYQFE
GVDWLLYCYY NAQNCILADE MGLGKTVQTI TFLSQVYDYG IHGPFLVVVP LSTIQNWVRE
FETWTDMNAI VYHGSAHARE VLQQYEVFYD KRHCGAKNWK KNFVKIDALI TTFETVVSDV
EFLKKIPWRV CVIDEAHRLK NRNCKLLVNG LLAFRMEHRV LLTGTPLQNN IEELFSLLNF
LHPQQFDNSA TFLEQFGSCQ TDDQVQKLQE ILKPMMLRRL KEDVEKSLGP KEETIIEVQL
SDMQKKFYRA ILERNFSHLC KGTSAPSLMN VMMELRKCCN HPFLINGAEE TIMNDFRLAH
PDWDDETLAQ KALVQASGKV VLIEKLLPKL RKDGHKVLIF SQMVKVLDLL EEFLITMSYP
FERIDGNVRG DMRQAAIDRF SKENSDRFVF LLCTRAGGLG INLTAADTVI IFDSDWNPQN
DLQAQARCHR IGQKKLVKVY RLITSNTYER EMFDKASLKL GLDKAVLQST TALKAEGTAL
SKKDVEELLK KGAYGSIMDE ENDSAKFNEE DIETILQRRT QTITLEAGQK GSLFAKATFN
STHNKGDDID IDDPEFWTKW AEKAQVDVEK ATATPDGREL IIEEPRKRTK RFEENKMEDV
DSDGSEESGK RKRGNPEKRK RRKGEDEDGD YSSSYRPDEL ATSKAEYFKM EKVLANYGWG
RWAEIKKYGD LEIEEQDIEH MSRTLLLHCV REFRGDDRVR QFVFNLIKPK EIGANSKYSA
GSMYNQGWAA LPEFNPPSFA LDSSFQRHVH RHANKLMLKI DMLKHLEVYI IAEERSLVED
FEVKWTDIKL KEMPIVAETF VEGWDTDCDK CFLIGCWRHG LENYDAMRAD ENLCFHEKNI
PAWPIATEFW VRFRRLLSTH QRSIHDPVYD KSKWNRKEEV EFLRVLKSYG VKAPKGDQTG
EDWTVFRTFS PMFEKRSDEE LHEHFMCVLA MCKRAQGNND LKPIDLKRAM SIDPIAHRKA
IKLLNRINVM RKVHTLAESL TVASLMNCQT TGMPSGWSTE HDKELIEICA QGGLDGLAAN
VLNKPAFAKI VRPSETTLLR RVIEIVTTVE TGKWCGCADV EAVNDSDSED KKEMAVAAAQ
AQFLQRMQQQ QLQQQASSAA AANSANRKAA NRKRPNNDND AKMRAMQQML MGAAGGSGGA
EYANMIALML MPQMMAAAGG GQNMTAAQQQ TINQMLTMLV ASAMQQQQQP STSKSSSSQQ
AQQQAQLQAA VVALAQLAQA TSSSSSATAG SSSSASTADQ QNAAILEALM AMALQPGAMQ
AMASSGTSTP SAAKKAKPTP APTPKQDTSQ ATATAQAAAL AAAAAAAQQQ QQQQAQAAQQ
AQQAQVTKSQ EELIILRILE IAGVGMNELA KLNTMSKESK IPMVHKTTKE PLPEAKRPQI
RDLTVFAMSH PEWTIDLTLF KDMPGTSTSS AALAAKAASN RPTPVATPKA PTPAPKEPQT
PSASATCNIK VGNSLQLDNM ISVFNRKTGE PLAASKWPKS ENLAAWLDAN PDYNVNSQSA
LPAHLALNGK HTDRIGGEPA VVPSVPTTPA PALTPSTPTT TAQVNAQTQL TNAQAAQLMA
LAAAQQVQQQ QTPTSSKSRS GKFYKTNRMH SNESKVLIAN AAAQAAAAQS QQDKITQQQL
EMLQMQMILQ QYQQAAAIQQ LMYGGYSMPS TSSASSTNNQ AATMAALAAA QAAQVASVPS
TPTTKQPKLQ TASAATPAAT SSATPASSST PSTSQAATSS ANSIDDINPL LLTALLQNPQ
VLNQMMVSDP NMLAMLAAAA QQQQQPSSTK KSK
//
