ID A0A2P5BX64_PARAD Unreviewed; 1017 AA.
AC A0A2P5BX64;
DT 23-MAY-2018, integrated into UniProtKB/TrEMBL.
DT 23-MAY-2018, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE SubName: Full=Cdk-activating kinase assembly factor {ECO:0000313|EMBL:PON53378.1};
GN ORFNames=PanWU01x14_202600 {ECO:0000313|EMBL:PON53378.1};
OS Parasponia andersonii (Sponia andersonii).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Rosales; Cannabaceae; Parasponia.
OX NCBI_TaxID=3476 {ECO:0000313|EMBL:PON53378.1, ECO:0000313|Proteomes:UP000237105};
RN [1] {ECO:0000313|Proteomes:UP000237105}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. WU1-14 {ECO:0000313|Proteomes:UP000237105};
RA Van Velzen R., Holmer R., Bu F., Rutten L., Van Zeijl A., Liu W.,
RA Santuari L., Cao Q., Sharma T., Shen D., Roswanjaya Y., Wardhani T.,
RA Kalhor M.S., Jansen J., Van den Hoogen J., Gungor B., Hartog M.,
RA Hontelez J., Verver J., Yang W.-C., Schijlen E., Repin R., Schilthuizen M.,
RA Schranz E., Heidstra R., Miyata K., Fedorova E., Kohlen W., Bisseling T.,
RA Smit S., Geurts R.;
RT "Parallel loss of symbiosis genes in relatives of nitrogen-fixing non-
RT legume Parasponia.";
RL Submitted (JUN-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the SNF2/RAD54 helicase family. RAD16 subfamily.
CC {ECO:0000256|ARBA:ARBA00008438}.
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:PON53378.1}.
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DR EMBL; JXTB01000207; PON53378.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2P5BX64; -.
DR STRING; 3476.A0A2P5BX64; -.
DR OrthoDB; 11932at2759; -.
DR Proteomes; UP000237105; Unassembled WGS sequence.
DR GO; GO:0016746; F:acyltransferase activity; IEA:UniProt.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0140658; F:ATP-dependent chromatin remodeler activity; IEA:InterPro.
DR GO; GO:0140096; F:catalytic activity, acting on a protein; IEA:UniProt.
DR GO; GO:0016818; F:hydrolase activity, acting on acid anhydrides, in phosphorus-containing anhydrides; IEA:InterPro.
DR GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd18008; DEXDc_SHPRH-like; 1.
DR CDD; cd18793; SF2_C_SNF; 1.
DR CDD; cd14318; UBA_Cbl_like; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR Gene3D; 3.40.50.10810; Tandem AAA-ATPase domain; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR001650; Helicase_C.
DR InterPro; IPR014905; HIRAN.
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 InterPro; IPR009060; UBA-like_sf.
DR InterPro; IPR027370; Znf-RING_euk.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR InterPro; IPR017907; Znf_RING_CS.
DR PANTHER; PTHR45626:SF45; DNA REPAIR PROTEIN RAD5A; 1.
DR PANTHER; PTHR45626; TRANSCRIPTION TERMINATION FACTOR 2-RELATED; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR Pfam; PF08797; HIRAN; 1.
DR Pfam; PF00176; SNF2-rel_dom; 1.
DR Pfam; PF13445; zf-RING_UBOX; 1.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00490; HELICc; 1.
DR SMART; SM00910; HIRAN; 1.
DR SMART; SM00184; RING; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR SUPFAM; SSF57850; RING/U-box; 1.
DR SUPFAM; SSF46934; UBA-like; 1.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR PROSITE; PS51194; HELICASE_CTER; 1.
DR PROSITE; PS00518; ZF_RING_1; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Kinase {ECO:0000313|EMBL:PON53378.1};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000237105};
KW Transferase {ECO:0000313|EMBL:PON53378.1};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00175}.
FT DOMAIN 423..640
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 782..822
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT DOMAIN 855..1017
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 60..111
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 457..487
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 60..93
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 94..111
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1017 AA; 112541 MW; 829BB40B9A0C37CE CRC64;
MGNKVTEELV STVRSIVGSD YSDMDVIRAL HMANNDLTAA INIIFDTPSF NSKANLGLQR
NPEISNRNSS SETQPVSSVN SKENGGENKN CSLRSEGNVE DRPSESGDVP VEDVCRREGP
VEDKWWLVGC GEVAGLSTCK GRRVKPGDEV IFTFPLKGLS STRSPGKNFG RGRNAAAACS
EIVRFSTRDS GEIGRIPNEW TRCLLPLVRD KKIRVEGSCK HTPEVLSIMD TVDLSISVYI
NSSMFDKQHD TSLKAASSST EESVVHPVPT LFRLLGLTPV MKAEFTPGEL YSRKRHLDLK
GSSGFQASAL LPNKFRNPSE NKNEVTNEES ISDADLDSIV GVGDSSELEE MDPPRTLQCD
LRPYQKQALY WMTQLEKGLC MDGAATTLHP CWEAYHLADK RGHIVYLNAF SGDATTQFPS
ALQMARGGLH LKILADAMGL GKTIMTIALL LANSERGGSS GSQSTSQPSG EGSEVSNGSG
NSLNVQKKTT KFPGFDKLMK QKSTLMDGGS LIVCPMTLLG QWKAEIETHV KPGSITLYVH
YGHSRPKDAK VLTQSNVVIT TYGVLASEFS AENSEGSGGL YSVRWFRVVL DEAHTIKSSK
SQISTAAAAL VADCRWCLTG TPIQPIMLRR TKFSTDRDGR QVTGLGHFVL LRPFACCRPI
LVLPPADVQV IYCELTEAEK DFYEALFKRS KLKFDQFVDQ GRVLHNYASI LELLLRLRQC
CDHPFLVMSR GDTQEFSDLN KLAKHFLKGS QNSVEGEVKD MPSRAYIQEV MEELRNGEQG
ECPICLEAFE DAVLTPCAHR LCRECLLASW RNTTSGLCPV CRKIVNRQDL ITAPTESRFQ
VDIDKNWVES TKVAVLLREL EALRLSGSKS IVFSQWTAFL DLLEIPLSRS NIPFVRLDGT
LNLQQREKVI RQFSEDSSVL VLLMSLKAGG VGINLTAASS AFVLDPWWNP AVEEQAVMRI
HRIGQTKKVM IKRFIVKGTV EERMEAVQAR KQRMISGALT DQEVRSARLE ELKMLFS
//
