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Database: UniProt
Entry: A0A2C6LBM2_9APIC
LinkDB: A0A2C6LBM2_9APIC
Original site: A0A2C6LBM2_9APIC 
ID   A0A2C6LBM2_9APIC        Unreviewed;      2322 AA.
AC   A0A2C6LBM2;
DT   20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT   20-DEC-2017, sequence version 1.
DT   24-JAN-2024, entry version 25.
DE   SubName: Full=Sec63 domain-containing dead deah box {ECO:0000313|EMBL:PHJ24434.1};
GN   ORFNames=CSUI_001711 {ECO:0000313|EMBL:PHJ24434.1};
OS   Cystoisospora suis.
OC   Eukaryota; Sar; Alveolata; Apicomplexa; Conoidasida; Coccidia;
OC   Eucoccidiorida; Eimeriorina; Sarcocystidae; Cystoisospora.
OX   NCBI_TaxID=483139 {ECO:0000313|EMBL:PHJ24434.1, ECO:0000313|Proteomes:UP000221165};
RN   [1] {ECO:0000313|EMBL:PHJ24434.1, ECO:0000313|Proteomes:UP000221165}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Wien I {ECO:0000313|EMBL:PHJ24434.1,
RC   ECO:0000313|Proteomes:UP000221165};
RX   PubMed=28161402; DOI=10.1016/j.ijpara.2016.11.007;
RA   Palmieri N., Shrestha A., Ruttkowski B., Beck T., Vogl C., Tomley F.,
RA   Blake D.P., Joachim A.;
RT   "The genome of the protozoan parasite Cystoisospora suis and a reverse
RT   vaccinology approach to identify vaccine candidates.";
RL   Int. J. Parasitol. 47:189-202(2017).
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:PHJ24434.1}.
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DR   EMBL; MIGC01000678; PHJ24434.1; -; Genomic_DNA.
DR   VEuPathDB; ToxoDB:CSUI_001711; -.
DR   OrthoDB; 57056at2759; -.
DR   Proteomes; UP000221165; Unassembled WGS sequence.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR   GO; GO:0004386; F:helicase activity; IEA:UniProtKB-KW.
DR   GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR   GO; GO:0006397; P:mRNA processing; IEA:UniProt.
DR   CDD; cd18021; DEXHc_Brr2_2; 1.
DR   CDD; cd18795; SF2_C_Ski2; 1.
DR   Gene3D; 1.10.150.20; 5' to 3' exonuclease, C-terminal subdomain; 2.
DR   Gene3D; 2.60.40.150; C2 domain; 2.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 4.
DR   Gene3D; 1.10.3380.10; Sec63 N-terminal domain-like domain; 2.
DR   Gene3D; 1.10.10.10; Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain; 2.
DR   InterPro; IPR003593; AAA+_ATPase.
DR   InterPro; IPR041094; Brr2_helicase_PWI.
DR   InterPro; IPR048863; BRR2_plug.
DR   InterPro; IPR035892; C2_domain_sf.
DR   InterPro; IPR011545; DEAD/DEAH_box_helicase_dom.
DR   InterPro; IPR014001; Helicase_ATP-bd.
DR   InterPro; IPR001650; Helicase_C.
DR   InterPro; IPR014756; Ig_E-set.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR004179; Sec63-dom.
DR   InterPro; IPR036388; WH-like_DNA-bd_sf.
DR   InterPro; IPR036390; WH_DNA-bd_sf.
DR   PANTHER; PTHR47961; DNA POLYMERASE THETA, PUTATIVE (AFU_ORTHOLOGUE AFUA_1G05260)-RELATED; 1.
DR   PANTHER; PTHR47961:SF4; U5 SMALL NUCLEAR RIBONUCLEOPROTEIN HELICASE; 1.
DR   Pfam; PF21188; BRR2_plug; 1.
DR   Pfam; PF00270; DEAD; 2.
DR   Pfam; PF00271; Helicase_C; 1.
DR   Pfam; PF18149; Helicase_PWI; 1.
DR   Pfam; PF02889; Sec63; 2.
DR   PIRSF; PIRSF039073; BRR2; 2.
DR   SMART; SM00382; AAA; 1.
DR   SMART; SM00487; DEXDc; 2.
DR   SMART; SM00490; HELICc; 2.
DR   SMART; SM00973; Sec63; 2.
DR   SUPFAM; SSF81296; E set domains; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 4.
DR   SUPFAM; SSF158702; Sec63 N-terminal domain-like; 2.
DR   SUPFAM; SSF46785; Winged helix' DNA-binding domain; 2.
DR   PROSITE; PS51192; HELICASE_ATP_BIND_1; 2.
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:UP000221165}.
FT   DOMAIN          623..808
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51192"
FT   DOMAIN          843..1036
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51194"
FT   DOMAIN          1472..1611
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51192"
FT   REGION          24..44
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          212..248
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          418..529
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        212..243
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        428..473
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        485..499
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   2322 AA;  259051 MW;  3DD15F7FB828F1A5 CRC64;
     MAEEFERFKR FEYRQNSNLV LQRDTSTGGA PALHLTEPTG EPESLAGRKL YPMGDKVERG
     LKKEEKQAGK VSAAQRKSKL RRNKLDIKRG ATVLDTDVTE IFFYKPTTQQ TRQVYEQLLV
     TLQQQLGDQP DEVLKGAADE VLAALKVDGC KDSERKKNVE QVLGPLTSDR FSRLFQLAKN
     ITDYSVGGEE EAGASGGGLD SNTGVAVVFD EEEEEDADGN DLMEVEVLDG DDEDEDEDEG
     ETEDKERTYL ASKNLDDNED LEERDAYELD IAKIDPHWLQ RELNNIFGDP NRAVATEKEI
     LSILATPDIQ ECENKLVVIL KYENFELAKL ILKNRWKIFY AVRLGQAQSK EEKNAIYEEM
     KNTPEGQEVL ELLDSLSSRR NKEKEMAINV RKEAASLAAK AQARAAASLR ALEFADEDEA
     GTRTGGGAGA GGSSSSATSG SGAVGSSSTG TGTGTSVSGS GGVSSSSGSS SSRREGLDDG
     KGGGAGPSSS SSRSGQGFAA GSSGGVGGGG GLGGTSSSTS VGGGLKGSGA GAALKPTATV
     DLGALTFHQG GHLMSNVRVK LPDGAQRIET KSYDEVIVQA FKKPQTDSDS RVSVSSMPTW
     AQDAFKVANI EQLNAMQSKV YKVAFEDFKE NLLLCAPTGA GKTNVAMLAM LNVVGRYRNP
     KAGGAIDLSG FKIIYISPMK ALVAEQVQAF TQRFQPYGIT VRELTGDVNL TRQQIEDTQV
     IVTTPEKWDI ITRKAGERAY TQLVRLVIID EIHLLHDTRG PVLESIIART IRQIETAQEH
     IRLVGLSATL PNYEDVAVFL RVRPERGLFF FGNHYRPVPL KQTYIGIKDK KAIKRYNTMN
     EVTYEKLMES AGKSQVLIFV HSRKETVKTA RFIRDMALQK DTLPRFLQHM TASREILQAE
     AEAVKTSDLK ELLPYGFAVH HAGLPRTDRK LVEDLFADRH VQVLVSTATL AWGVNLPAHT
     VIIKGTQVYL PEKGTWSELS PMDVLQMMGR AGRPQYDTAG HAILITQHSE LQYYLSLNNQ
     QLPIESQMIS CLPDMLNAEV VLGSVRSRED AVNWLGYTYL YVRMLKNPSL YGIPPDEAAH
     DKLLEQHCVN LVDSALKILD KNFLIKYDRR VGCIQVTALG RVASHYYIKY PTIAIYNQHM
     KPLMSDIELL RLFSLSSEFK YMPVREEEKV ELQRLMERVP IPVKGSPDET SSKVNVLLQA
     YISKLKLEGL AMMADMVYVQ QSANRIMRAI FEICLRRGWA MLAMRALQFC KEIDRRMWST
     MTPLRQFKVL PEELLRKIEK KDLPFERYYD LTSTEIGELV RVPKMGKLLH RLIHQFPKLE
     LAAFVQPLTR TCLVVELTIT PDFQWDFKVH GTGEVFWIIV EDVDGEQILH HEMFIMPPFT
     GEVEHTLCFT LPITDPLPPN YSIRVVSDRW LRSQSSLPIS FKTLILPERT PPHTELLDLQ
     PLPITALRNS TAEQIYSGSF KAFNPIQTQV FSTLYTTNEN VLLCLPPTSG KEVCLEFALL
     RMFNTEPSNQ WKAVYIAPHP MVVKERFEDW VAKLGRGMGV KLAELTGEMQ HDLKLLEQSQ
     VVLATPEKWD FISRRWKTRK VLQSIRLLLV DDLHLLNSSM GSTLEVCLSR TRYISAQLQR
     PIRVVAIGNS LANAKDVGDW LGVSSTGLFN FHPSVRTIPL EISLHGFDVY NREARLLAMS
     KAVYQAIKLY TSVGDDEPGG SVHSSSSRKL KNVIVFCSDR RHCRLAAIDL LLQAAADDDP
     KKFLHVSDAV MSKYTSVVRD KMLLETLSYG VGLFHSGLSE AEQQLVQQLH AGGAIQVVVV
     AEECAWGLQM YAHLVVVVDT KKYTENGYED YTVADVLQML GHATRPAVDK HGYAVLFCPS
     SKREFYKKFI FEPLPVESQL EQNLVDHVNA EVVLKTIENK QDAVDWLTWT FLYRRLAKNP
     NYYGLQGVSH QHLSDYLSEL VESSVHTLEQ AQCVSEHNDV DLEPLNLGLI AAFYYVKVNT
     IELFNRSLTP TCKRRALLEI LAASSELSTI PLRPGEEGTL RGLAQRLGVR LSQNSEDINK
     PSTKALILLY AHFNRLPLPS DLVADQKFVL EPCIRLLHAL VDVISSNGWL VPALSAMEIC
     QAVVQAMTTT ALGGGNATQC SPLKQLPHFT DELIETAKEM GVEDIFDLMN MEDKEREKLL
     KPLTPSQLKA SVYTSSLPKL RMRETVLLPF ACLFPQDVAK ASNRYPVINV EYHLSKKDDI
     APNESIQCTV TLERDCAETQ GLVYAPFFPR EKEEQWWLVV GQASSNSLAA IKRLTMNKQT
     TTVNLSFDAP ETPGKHTYVL YLMGDSYVGG DQEYKLDFRV RA
//
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