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Database: UniProt
Entry: A0A0V0ZMA0_9BILA
LinkDB: A0A0V0ZMA0_9BILA
Original site: A0A0V0ZMA0_9BILA 
ID   A0A0V0ZMA0_9BILA        Unreviewed;      1046 AA.
AC   A0A0V0ZMA0;
DT   16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT   16-MAR-2016, sequence version 1.
DT   27-MAR-2024, entry version 34.
DE   RecName: Full=RPB5 homolog {ECO:0000256|ARBA:ARBA00032836};
GN   Name=COASY {ECO:0000313|EMBL:KRY13370.1};
GN   ORFNames=T12_5353 {ECO:0000313|EMBL:KRY13370.1};
OS   Trichinella patagoniensis.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC   Trichinellida; Trichinellidae; Trichinella.
OX   NCBI_TaxID=990121 {ECO:0000313|EMBL:KRY13370.1, ECO:0000313|Proteomes:UP000054783};
RN   [1] {ECO:0000313|EMBL:KRY13370.1, ECO:0000313|Proteomes:UP000054783}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ISS2496 {ECO:0000313|EMBL:KRY13370.1};
RA   Korhonen P.K., Edoardo P., Giuseppe L.R., Gasser R.B.;
RT   "Evolution of Trichinella species and genotypes.";
RL   Submitted (JAN-2015) 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:KRY13370.1}.
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DR   EMBL; JYDQ01000141; KRY13370.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0V0ZMA0; -.
DR   Proteomes; UP000054783; Unassembled WGS sequence.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004140; F:dephospho-CoA kinase activity; IEA:InterPro.
DR   GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR   GO; GO:0003899; F:DNA-directed 5'-3' RNA polymerase activity; IEA:InterPro.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR   GO; GO:0015937; P:coenzyme A biosynthetic process; IEA:InterPro.
DR   GO; GO:0006351; P:DNA-templated transcription; IEA:InterPro.
DR   CDD; cd02022; DPCK; 1.
DR   CDD; cd05327; retinol-DH_like_SDR_c_like; 1.
DR   Gene3D; 3.40.50.620; HUPs; 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   Gene3D; 3.40.1340.10; RNA polymerase, Rpb5, N-terminal domain; 1.
DR   Gene3D; 3.90.940.20; RPB5-like RNA polymerase subunit; 1.
DR   HAMAP; MF_00376; Dephospho_CoA_kinase; 1.
DR   InterPro; IPR004821; Cyt_trans-like.
DR   InterPro; IPR001977; Depp_CoAkinase.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR005571; RNA_pol_Rpb5_N.
DR   InterPro; IPR036710; RNA_pol_Rpb5_N_sf.
DR   InterPro; IPR000783; RNA_pol_subH/Rpb5_C.
DR   InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR   InterPro; IPR035913; RPB5-like_sf.
DR   InterPro; IPR002347; SDR_fam.
DR   NCBIfam; TIGR00152; dephospho-CoA kinase; 1.
DR   PANTHER; PTHR43157:SF69; DEHYDROGENASES, SHORT CHAIN; 1.
DR   PANTHER; PTHR43157; PHOSPHATIDYLINOSITOL-GLYCAN BIOSYNTHESIS CLASS F PROTEIN-RELATED; 1.
DR   Pfam; PF00106; adh_short; 1.
DR   Pfam; PF01121; CoaE; 1.
DR   Pfam; PF01467; CTP_transf_like; 1.
DR   Pfam; PF01191; RNA_pol_Rpb5_C; 1.
DR   Pfam; PF03871; RNA_pol_Rpb5_N; 1.
DR   PRINTS; PR00081; GDHRDH.
DR   SUPFAM; SSF53036; Eukaryotic RPB5 N-terminal domain; 1.
DR   SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR   SUPFAM; SSF52374; Nucleotidylyl transferase; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   SUPFAM; SSF55287; RPB5-like RNA polymerase subunit; 1.
DR   PROSITE; PS51219; DPCK; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Reference proteome {ECO:0000313|Proteomes:UP000054783}.
FT   DOMAIN          5..94
FT                   /note="RNA polymerase Rpb5 N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF03871"
FT   DOMAIN          138..191
FT                   /note="RNA polymerase subunit H/Rpb5 C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF01191"
FT   DOMAIN          670..807
FT                   /note="Cytidyltransferase-like"
FT                   /evidence="ECO:0000259|Pfam:PF01467"
SQ   SEQUENCE   1046 AA;  118828 MW;  425CEC8C0429BAD2 CRC64;
     MAEDDREIFR LWKIRQNAFQ MCRDRGFLVT SYELDQSFED FVRQYGDRPS EGKPARSDLS
     FLVSHEEDAA ENLFVYFADE RKVGIKTIKN VCLRLQSENM SRAIMIVQEP MTAIARHSVA
     DLSPKYKLEQ FLEAELMVNI IRHELVPRHV IMSSKEKDEL LDRYKIKEHQ LPRIQSTDPV
     ARYYGVVRGQ LYLFSFYFKG SQFYGKEKCK GRIYVVTGAN SGIGKEIVRE LNYRGAVVYM
     ACRSMEKGYS AIDDLVKLGC SADRLHILEL DQSSFESVKA FVDKLNNLTN KLDGIVLNAG
     VMYVPRYQLT KDGHEYIWQV NYLSTVLLCE SLIPLLEKCR DEGRVVIISS NAHLWINDLN
     IHSIDRRNYW SSVKAYGRSK LAQVMYTVAR SAMLRREGYL VTINACHPGV VNTPLFRQVP
     ILGSSTFQSV IAPFAWYFLK NAKDGAQTPL YCLLSKELGS VSGKYFCEMK QAEVNPLVEN
     SEARQALFEY SLEACNLFKD EKAVLRFQMN STGLLILTQR SSTLKIGIEF LLLKACQHVK
     GTLFISVHEN LVRQLTTENI WNFVQHTYNA SCSLDKSLDV RLMVDSLKRV GDYKRKLNPE
     TCLLLDCDLS QLGDFFTSKE RLHLPMQMVM LHFDKQLADM SGLPTQMTTF CSMEKFSKAP
     QTLPMYKHIV LGGTFDRMHD GHKFLLTIAL LLTKRQLTCG ITCGSMLTKL IQPVKERCKI
     VEQFLTDVDP SVHLDIVPIE DSFGPSIDDA SMDCIVGSEE TASGILRVNE KRKNKNLPEL
     AAYAVSLLQV TQKNDCVNKL SSSEARKQLL GSTLRPFEKL KSKSESKPFI IGLTGGIASG
     KSKIAEYLNH WGACVIDCDK IGHQSYSPNT AVYEKLVNTF GKRIVNQCTG EIDRGCLGKI
     VFSNPAALKE LNEIVWPEIL SLVKFQLDSM KERKKIVVIE AAVLIQAGWQ NFVDEVWASF
     IPVDEAVKRL VERNKLTEED ARRRLNAQLS NDEIIKNSHV VFCSLWHYNC TKMQALDHLL
     QKHGVICGNA SICNRSAHST FDGPMR
//
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