ID E0VG29_PEDHC Unreviewed; 893 AA.
AC E0VG29;
DT 02-NOV-2010, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2010, sequence version 1.
DT 24-JAN-2024, entry version 73.
DE RecName: Full=Hydin adenylate kinase-like domain-containing protein {ECO:0000259|Pfam:PF17213};
GN Name=8236728 {ECO:0000313|EnsemblMetazoa:PHUM171820-PA};
GN ORFNames=Phum_PHUM171820 {ECO:0000313|EMBL:EEB12335.1};
OS Pediculus humanus subsp. corporis (Body louse).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Paraneoptera; Psocodea; Phthiraptera; Anoplura; Pediculidae;
OC Pediculus.
OX NCBI_TaxID=121224;
RN [1] {ECO:0000313|EMBL:EEB12335.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=USDA {ECO:0000313|EMBL:EEB12335.1};
RA Kirkness E., Hannick L., Hass B., Bruggner R., Lawson D., Bidwell S.,
RA Joardar V., Caler E., Walenz B., Inman J., Schobel S., Galinsky K.,
RA Amedeo P., Strausberg R.;
RT "Annotation of Pediculus humanus corporis strain USDA.";
RL Submitted (APR-2007) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:EEB12335.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=USDA {ECO:0000313|EMBL:EEB12335.1};
RG The Human Body Louse Genome Consortium;
RA Kirkness E., Walenz B., Hass B., Bruggner R., Strausberg R.;
RT "The genome of the human body louse.";
RL Submitted (APR-2007) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EnsemblMetazoa:PHUM171820-PA}
RP IDENTIFICATION.
RC STRAIN=USDA {ECO:0000313|EnsemblMetazoa:PHUM171820-PA};
RG EnsemblMetazoa;
RL Submitted (MAY-2020) to UniProtKB.
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DR EMBL; AAZO01001996; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; DS235131; EEB12335.1; -; Genomic_DNA.
DR RefSeq; XP_002425073.1; XM_002425028.1.
DR AlphaFoldDB; E0VG29; -.
DR STRING; 121224.E0VG29; -.
DR EnsemblMetazoa; PHUM171820-RA; PHUM171820-PA; PHUM171820.
DR GeneID; 8236728; -.
DR KEGG; phu:Phum_PHUM171820; -.
DR CTD; 8236728; -.
DR VEuPathDB; VectorBase:PHUM171820; -.
DR eggNOG; KOG3078; Eukaryota.
DR HOGENOM; CLU_015567_0_0_1; -.
DR InParanoid; E0VG29; -.
DR OMA; KMAWQNA; -.
DR OrthoDB; 5483389at2759; -.
DR Proteomes; UP000009046; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0019205; F:nucleobase-containing compound kinase activity; IEA:InterPro.
DR GO; GO:0006139; P:nucleobase-containing compound metabolic process; IEA:InterPro.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd22967; DD_AK7; 1.
DR Gene3D; 1.20.890.10; cAMP-dependent protein kinase regulatory subunit, dimerization-anchoring domain; 1.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR InterPro; IPR000850; Adenylat/UMP-CMP_kin.
DR InterPro; IPR047499; DD_AK7.
DR InterPro; IPR007858; Dpy-30_motif.
DR InterPro; IPR033768; Hydin_ADK.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR23359:SF105; ADENYLATE KINASE 7; 1.
DR PANTHER; PTHR23359; NUCLEOTIDE KINASE; 1.
DR Pfam; PF05186; Dpy-30; 1.
DR Pfam; PF17213; Hydin_ADK; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Kinase {ECO:0000256|ARBA:ARBA00022777};
KW Reference proteome {ECO:0000313|Proteomes:UP000009046};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 367..475
FT /note="Hydin adenylate kinase-like"
FT /evidence="ECO:0000259|Pfam:PF17213"
FT REGION 1..48
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 416..444
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 804..885
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 647..678
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 1..16
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 31..48
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 425..444
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 804..868
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 893 AA; 103505 MW; F536D9A49544AEF5 CRC64;
MVLEDDEEED EEMRSEYSNV DNDFDGTMDD KNDDELYPES EEKRPTSKYY RSDEYEVIGS
LNFLKNPDYK RPEGIIEILD NENKSEYLEK ILMCGVIVYD ITNDLYCHPS QIEEAKWVAE
CRIFLIFNEK TQPKFFAKYQ DCRTFILVST LLTWAKTKPI DPDDPSLPFT ERDFRKRKPH
SNYKIHCQLE KRITELGKKY PKNFRTVVIG AGIPYGHEED ILHIYFKMAW LNSPHLPIFG
SGKNILPVIH IDSLSSIIRN IIDDFPEKMS YIVAMDPQTI TLNEVAKLLA KNLGNGKVLK
VNKEEAFLYN EVEQKIFDML TANINIYPNY IMNKENIVWG TDRPFNENIK KLIEEYKIAR
GLLPVKIFMH GPPASGKSFM ASRLSKYYDI PHLHVKKIIQ DTIQEMKDKI QAIKNKNESV
KEKDDNDENL EEEEDDEEEE EEEEDLDTLV AKLAEIEQNM NSSEKKRLDE EYVIQFFKKK
MMSNACLNKG FVIDGYPKTM EDTKKLYEVD EETQIEKDAA DDEEQIDVSA LSNALILPEY
VESLDASDEY LINRVIKMPE KSVLNSHYEE AEMCRRLSQF RALNTEDNTP LIYYDELEIH
PMIYDIENDT DPLMSSTFKA IVNRIGPPRN YNKSVEDIIN EQRKFCEDQM KENLRLQKED
IKKKNEEKRE NIEQWMLLKN RELEMEEKAL LVMGMPLRHY LMKYIFPTLT RGLVEVARLR
PDDPVDFLSE FLFQENPEGK MFQPNFEERE KKLEDALKEY EGYSTSSTTS EPFSSTKTYS
TEKSAKSHAI SKVSSYKCSL VSKKSTKSSK SKQSPRSTKS TKSSKSTKSK AGSKTESCTC
AKSPSLSTCS SDIDPPTPTS CSCTLSESYE TPEDDEPLKR KGQPGTCKCP CVT
//
