ID V9K9I6_CALMI Unreviewed; 1211 AA.
AC V9K9I6;
DT 19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT 19-MAR-2014, sequence version 1.
DT 27-MAR-2024, entry version 34.
DE RecName: Full=RNA uridylyltransferase {ECO:0000256|ARBA:ARBA00012472};
DE EC=2.7.7.52 {ECO:0000256|ARBA:ARBA00012472};
DE Flags: Fragment;
OS Callorhinchus milii (Ghost shark).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Chondrichthyes;
OC Holocephali; Chimaeriformes; Callorhinchidae; Callorhinchus.
OX NCBI_TaxID=7868 {ECO:0000313|EMBL:AFO94280.1};
RN [1] {ECO:0000313|EMBL:AFO94280.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Testis {ECO:0000313|EMBL:AFO94280.1};
RX PubMed=24402279; DOI=10.1038/nature12826;
RG International Elephant Shark Genome Sequencing Consortium;
RA Venkatesh B., Lee A.P., Ravi V., Maurya A.K., Lian M.M., Swann J.B.,
RA Ohta Y., Flajnik M.F., Sutoh Y., Kasahara M., Hoon S., Gangu V., Roy S.W.,
RA Irimia M., Korzh V., Kondrychyn I., Lim Z.W., Tay B.H., Tohari S.,
RA Kong K.W., Ho S., Lorente-Galdos B., Quilez J., Marques-Bonet T.,
RA Raney B.J., Ingham P.W., Tay A., Hillier L.W., Minx P., Boehm T.,
RA Wilson R.K., Brenner S., Warren W.C.;
RT "Elephant shark genome provides unique insights into gnathostome
RT evolution.";
RL Nature 505:174-179(2014).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=RNA(n) + UTP = diphosphate + RNA(n)-3'-uridine ribonucleotide;
CC Xref=Rhea:RHEA:14785, Rhea:RHEA-COMP:14527, Rhea:RHEA-COMP:17348,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:46398, ChEBI:CHEBI:140395,
CC ChEBI:CHEBI:173116; EC=2.7.7.52;
CC Evidence={ECO:0000256|ARBA:ARBA00024498};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000256|ARBA:ARBA00001936};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
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DR EMBL; JW861763; AFO94280.1; -; mRNA.
DR AlphaFoldDB; V9K9I6; -.
DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR GO; GO:0016779; F:nucleotidyltransferase activity; IEA:UniProtKB-KW.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0006402; P:mRNA catabolic process; IEA:UniProt.
DR GO; GO:0061157; P:mRNA destabilization; IEA:UniProt.
DR CDD; cd05402; NT_PAP_TUTase; 1.
DR Gene3D; 1.10.1410.10; -; 2.
DR Gene3D; 3.30.460.10; Beta Polymerase, domain 2; 1.
DR Gene3D; 4.10.60.10; Zinc finger, CCHC-type; 1.
DR InterPro; IPR043519; NT_sf.
DR InterPro; IPR002058; PAP_assoc.
DR InterPro; IPR002934; Polymerase_NTP_transf_dom.
DR InterPro; IPR045100; TUTase_dom.
DR InterPro; IPR001878; Znf_CCHC.
DR InterPro; IPR036875; Znf_CCHC_sf.
DR PANTHER; PTHR12271; POLY A POLYMERASE CID PAP -RELATED; 1.
DR PANTHER; PTHR12271:SF34; TERMINAL URIDYLYLTRANSFERASE 7; 1.
DR Pfam; PF01909; NTP_transf_2; 1.
DR Pfam; PF03828; PAP_assoc; 2.
DR Pfam; PF19088; TUTase; 1.
DR Pfam; PF00098; zf-CCHC; 2.
DR SMART; SM00343; ZnF_C2HC; 3.
DR SUPFAM; SSF81301; Nucleotidyltransferase; 1.
DR SUPFAM; SSF81631; PAP/OAS1 substrate-binding domain; 2.
DR SUPFAM; SSF57756; Retrovirus zinc finger-like domains; 2.
DR PROSITE; PS50158; ZF_CCHC; 3.
PE 2: Evidence at transcript level;
KW Metal-binding {ECO:0000256|PROSITE-ProRule:PRU00047};
KW Nucleotidyltransferase {ECO:0000313|EMBL:AFO94280.1};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:AFO94280.1};
KW Zinc {ECO:0000256|PROSITE-ProRule:PRU00047};
KW Zinc-finger {ECO:0000256|PROSITE-ProRule:PRU00047}.
FT DOMAIN 620..635
FT /note="CCHC-type"
FT /evidence="ECO:0000259|PROSITE:PS50158"
FT DOMAIN 1002..1016
FT /note="CCHC-type"
FT /evidence="ECO:0000259|PROSITE:PS50158"
FT DOMAIN 1121..1137
FT /note="CCHC-type"
FT /evidence="ECO:0000259|PROSITE:PS50158"
FT REGION 258..287
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 336..412
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 438..508
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1024..1066
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1133..1211
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 340..370
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 377..408
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 488..503
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1044..1066
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1142..1164
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1180..1211
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:AFO94280.1"
SQ SEQUENCE 1211 AA; 138448 MW; CD9AB9123FEDC1E9 CRC64;
SLKNSITFID VEAEFHARVP VVLCREKQSG LLCKVSAGNE NAWLTTCHLA TLAKLEPRLT
PLVTAFRYWG KLCHIDSPEE GGLPPYAFAL MIIYFLQQRK EAVLPVYLGL WIEGFSLDNL
ANFSLKGVED NQVIWELKAV STDDVISNEG KVALTFREDE QSSSPMGQLW VELLRFYALE
FALADYVIGI RIREPLSREA KDWPKRRIAI EDPYSVKRNV ARTLNSQMVY DYIIHCLRAT
YKYFALPKNK AAKCNRKGNT KVDSESTKKL DSIKTGGAIP AGTPNGGYLQ LHTDSDKINA
VDSFRNEQTI QNCGSEGIAE EELISDFENI LITSYEPNDK NHPEQSEDKQ SSDDVLESGN
DEERFDMPGK QKKSSAATSR VWEEDKGNHS TEVDKETSSD EEMGTRVKNS YFRDNFYSES
LSDSEGFLNP QNMECDEFGL EDCSQQEGKD EEEIVLNDED RESSDSVDLL PCTPEKPMHQ
LVGAVSRNEE DEEDDEEEEE DELDLNISRI HLDTADEEFE NICTESSEED DQSGEGTVIH
DELLNCKGQT SAKSQDGATA QLFKHSVDNE VTMKQKQELQ LDEMNKETLH QESQTSGEDD
MFYTFNRIDF TKGKASIIVC NLCKREGHLK QDCPEDFKKV DLDPLPQMTP IFLEFLDQVC
FHCYKDFSPD SLEIQAREHI LLCLEDFIRT ELDATANLCL FGSSKNGFGF KQSDLDICMT
FEGRETAEGL NCIRIIEDLA RVLRKHPGLR SILPITTAKV PIVKFFHVRS GLEGDISLYN
TLALHNTGLL ASYAAIDPRV KYLGYTMKIF AKICDIGDAS RGSLSSYAYT LMALYFLQQR
KPPVIPVLQE IFDGEKKSVF VDGWNVYYFD KLDELKNRWP DYGKNEESVG ELWLGLLRFY
TEEFDFKEHV ISIRRKNLLT TFKKQWTSKY IVIEDPFDLN HNLGAGLSRK MTNFIMKALI
NGRKIFGTPV RWIPKEYPAF LEYFFDPEIL TEGEVAPNDR CCRICGKIGH FMKDCPMRRC
KTRRRENRED VRTKMGLNDQ FQKPIESKPK RKHEEKEPQN KDVQKMYRES LKDVPKIEGE
LYGEARTPRK TKEEKVTNEI LRDRTPRQYA EQRRKQEQDK RCFTCGKEGH IKKECPQYKG
GSGAENASSV RMTVPSSVSN VIGNENKIHM KEKRKQKQKG FLNSQPAGLS NKFSTNSSAQ
GKSSHKRAQP E
//
