ID A0A498L5I4_LABRO Unreviewed; 354 AA.
AC A0A498L5I4;
DT 05-JUN-2019, integrated into UniProtKB/TrEMBL.
DT 05-JUN-2019, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE RecName: Full=Cleavage and polyadenylation specificity factor subunit 4 {ECO:0000256|ARBA:ARBA00016264, ECO:0000256|RuleBase:RU369008};
DE Short=CPSF 30 kDa subunit {ECO:0000256|RuleBase:RU369008};
DE AltName: Full=Cleavage and polyadenylation specificity factor 30 kDa subunit {ECO:0000256|RuleBase:RU369008};
GN ORFNames=ROHU_013508 {ECO:0000313|EMBL:RXN03489.1};
OS Labeo rohita (Indian major carp) (Cyprinus rohita).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Cyprinidae; Labeoninae; Labeonini; Labeo.
OX NCBI_TaxID=84645 {ECO:0000313|EMBL:RXN03489.1, ECO:0000313|Proteomes:UP000290572};
RN [1] {ECO:0000313|EMBL:RXN03489.1, ECO:0000313|Proteomes:UP000290572}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DASCIFA01 {ECO:0000313|EMBL:RXN03489.1};
RC TISSUE=Testis {ECO:0000313|EMBL:RXN03489.1};
RA Das P., Kushwaha B., Joshi C.G., Kumar D., Nagpure N.S., Sahoo L.,
RA Das S.P., Bit A., Patnaik S., Meher P.K., Jayasankar P., Koringa P.G.,
RA Patel N.V., Hinsu A.T., Kumar R., Pandey M., Agarwal S., Srivastava S.,
RA Singh M., Iquebal M.A., Jaiswal S., Angadi U.B., Kumar N., Raza M.,
RA Shah T.M., Rai A., Jena J.K.;
RT "Draft genome sequence of Rohu Carp (Labeo rohita).";
RL Submitted (MAR-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Component of the cleavage and polyadenylation specificity
CC factor (CPSF) complex that play a key role in pre-mRNA 3'-end
CC formation, recognizing the AAUAAA signal sequence and interacting with
CC poly(A) polymerase and other factors to bring about cleavage and
CC poly(A) addition. CPSF4 binds RNA polymers with a preference for
CC poly(U). {ECO:0000256|RuleBase:RU369008}.
CC -!- SUBUNIT: Component of the cleavage and polyadenylation specificity
CC factor (CPSF) complex. {ECO:0000256|RuleBase:RU369008}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123,
CC ECO:0000256|RuleBase:RU369008}.
CC -!- SIMILARITY: Belongs to the BUD31 (G10) family.
CC {ECO:0000256|ARBA:ARBA00005287}.
CC -!- SIMILARITY: Belongs to the CPSF4/YTH1 family.
CC {ECO:0000256|RuleBase:RU369008}.
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:RXN03489.1}.
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DR EMBL; QBIY01013482; RXN03489.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A498L5I4; -.
DR STRING; 84645.A0A498L5I4; -.
DR Proteomes; UP000290572; Unassembled WGS sequence.
DR GO; GO:0005847; C:mRNA cleavage and polyadenylation specificity factor complex; IEA:UniProtKB-UniRule.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0031124; P:mRNA 3'-end processing; IEA:UniProtKB-UniRule.
DR Gene3D; 3.30.1370.210; -; 1.
DR Gene3D; 4.10.1000.10; Zinc finger, CCCH-type; 1.
DR Gene3D; 4.10.60.10; Zinc finger, CCHC-type; 1.
DR InterPro; IPR001748; BUD31.
DR InterPro; IPR018230; BUD31/G10-rel_CS.
DR InterPro; IPR045348; CPSF4/Yth1.
DR InterPro; IPR000571; Znf_CCCH.
DR InterPro; IPR036855; Znf_CCCH_sf.
DR InterPro; IPR001878; Znf_CCHC.
DR InterPro; IPR036875; Znf_CCHC_sf.
DR PANTHER; PTHR23102:SF24; CLEAVAGE AND POLYADENYLATION SPECIFICITY FACTOR SUBUNIT 4; 1.
DR PANTHER; PTHR23102; CLEAVAGE AND POLYADENYLATION SPECIFICITY FACTOR SUBUNIT 4-RELATED; 1.
DR Pfam; PF01125; BUD31; 1.
DR Pfam; PF00642; zf-CCCH; 2.
DR Pfam; PF00098; zf-CCHC; 1.
DR PRINTS; PR00322; G10.
DR SMART; SM00343; ZnF_C2HC; 1.
DR SMART; SM00356; ZnF_C3H1; 4.
DR SUPFAM; SSF90229; CCCH zinc finger; 2.
DR SUPFAM; SSF57756; Retrovirus zinc finger-like domains; 1.
DR PROSITE; PS00997; G10_1; 1.
DR PROSITE; PS50103; ZF_C3H1; 4.
DR PROSITE; PS50158; ZF_CCHC; 1.
PE 1: Evidence at protein level;
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|PROSITE-
KW ProRule:PRU00723}; mRNA processing {ECO:0000256|RuleBase:RU369008};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242, ECO:0000256|RuleBase:RU369008};
KW Proteomics identification {ECO:0007829|PeptideAtlas:A0A498L5I4};
KW Reference proteome {ECO:0000313|Proteomes:UP000290572};
KW Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|RuleBase:RU369008};
KW RNA-binding {ECO:0000256|RuleBase:RU369008};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|PROSITE-ProRule:PRU00723};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00723}.
FT DOMAIN 147..174
FT /note="C3H1-type"
FT /evidence="ECO:0000259|PROSITE:PS50103"
FT DOMAIN 175..202
FT /note="C3H1-type"
FT /evidence="ECO:0000259|PROSITE:PS50103"
FT DOMAIN 203..230
FT /note="C3H1-type"
FT /evidence="ECO:0000259|PROSITE:PS50103"
FT DOMAIN 232..254
FT /note="C3H1-type"
FT /evidence="ECO:0000259|PROSITE:PS50103"
FT DOMAIN 330..345
FT /note="CCHC-type"
FT /evidence="ECO:0000259|PROSITE:PS50158"
FT ZN_FING 147..174
FT /note="C3H1-type"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00723"
FT ZN_FING 175..202
FT /note="C3H1-type"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00723"
FT ZN_FING 203..230
FT /note="C3H1-type"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00723"
FT ZN_FING 232..254
FT /note="C3H1-type"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00723"
FT REGION 258..287
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 264..287
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 354 AA; 41069 MW; A6F52E3D3F4B5D8E CRC64;
MPKVKRSRKP PPDGWELIEP TLDELDQKMR EAETEPHEGK RKVESLWPIF RLHHQRSRYI
FDLFYKRKAI SRELYEYCIK EGYADKNLIA KWKKQGYENL CCLRCIQTRD TNFGTNCICR
VPKGKLEVTL QLSLLTGGMC PFRHISGEKT VVCKHWLRGL CKKGDQCEFL HEYDMTKMPE
CYFYSKFGEC SNKECPFLHI DPESKIKDCP WYDRGFCKHG PDCRHRHTRR VICVNYLVGF
CPEGKSCKFM HPRFELPMGA TEQPPLPQQA QSQQKQQNTQ PTNRSSQSLI QLTNTNVNSN
QRMPNAVGIV HSNNNMGGPR GPRPLDQVTC YKCGEKGHYA NKCTKGHLAF LSGQ
//
