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
//