ZCHC7_BOVIN
ID ZCHC7_BOVIN Reviewed; 546 AA.
AC Q2KIN0;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 14-APR-2009, sequence version 2.
DT 25-MAY-2022, entry version 80.
DE RecName: Full=Zinc finger CCHC domain-containing protein 7;
DE AltName: Full=TRAMP-like complex RNA-binding factor ZCCHC7;
GN Name=ZCCHC7;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Testis;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBUNIT: Component of a nucleolar TRAMP-like complex, an ATP-dependent
CC exosome regulatory complex consisting of a helicase (MTREX), an
CC oligadenylate polymerase (TENT4B or TENT4A), and a substrate specific
CC RNA-binding factor (ZCCHC7 or ZCCHC8). Several TRAMP-like complexes
CC exist with specific compositions and are associated with nuclear, or
CC nucleolar RNA exosomes (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000250}.
CC -!- CAUTION: It is uncertain whether Met-1 or Met-2 is the initiator.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAI12579.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; BC112578; AAI12579.1; ALT_INIT; mRNA.
DR RefSeq; NP_001039565.1; NM_001046100.2.
DR AlphaFoldDB; Q2KIN0; -.
DR STRING; 9913.ENSBTAP00000028791; -.
DR PaxDb; Q2KIN0; -.
DR GeneID; 511821; -.
DR KEGG; bta:511821; -.
DR CTD; 84186; -.
DR eggNOG; KOG4400; Eukaryota.
DR InParanoid; Q2KIN0; -.
DR Proteomes; UP000009136; Unplaced.
DR GO; GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell.
DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR InterPro; IPR001878; Znf_CCHC.
DR InterPro; IPR036875; Znf_CCHC_sf.
DR Pfam; PF00098; zf-CCHC; 1.
DR SMART; SM00343; ZnF_C2HC; 4.
DR SUPFAM; SSF57756; SSF57756; 2.
DR PROSITE; PS50158; ZF_CCHC; 2.
PE 2: Evidence at transcript level;
KW Isopeptide bond; Metal-binding; Nucleus; Reference proteome; Repeat;
KW Ubl conjugation; Zinc; Zinc-finger.
FT CHAIN 1..546
FT /note="Zinc finger CCHC domain-containing protein 7"
FT /id="PRO_0000370240"
FT ZN_FING 241..258
FT /note="CCHC-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00047"
FT ZN_FING 263..280
FT /note="CCHC-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00047"
FT ZN_FING 304..321
FT /note="CCHC-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00047"
FT ZN_FING 348..365
FT /note="CCHC-type 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00047"
FT REGION 52..71
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 402..546
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 402..478
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 501..539
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CROSSLNK 131
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q8N3Z6"
FT CROSSLNK 139
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q8N3Z6"
FT CROSSLNK 141
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q8N3Z6"
FT CROSSLNK 239
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q8N3Z6"
FT CROSSLNK 254
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q8N3Z6"
FT CROSSLNK 339
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q8N3Z6"
FT CROSSLNK 413
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q8N3Z6"
FT CROSSLNK 435
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q8N3Z6"
FT CROSSLNK 488
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q8N3Z6"
FT CROSSLNK 491
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q8N3Z6"
FT CROSSLNK 494
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q8N3Z6"
FT CROSSLNK 538
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q8N3Z6"
SQ SEQUENCE 546 AA; 63575 MW; D0E9390652B87483 CRC64;
MMFGGYETIE AYEDELYREE SSSELSVDSE VEFQLYSQVH YAQDLDNVIR EEEHEDRNSG
NSESFSSKPN QKNLIVLSDS EVIQLSDGSE VITLSDEDSI YRCERKNFRV HAKEKTQGSP
ASLHSNDLAD KKCKRDIEKS KPGERSGTIQ EVMIIEVSSS EEEESTISES DNVESWMLLG
CEVDDKDDDI LLNIVGCEKS VNEGEDDVNW FISDKDIEAQ IGNKRSSGRW THRYYTANKN
VTCRNCDKCG HLSKNCPFPQ KVRPCCLCSE RGHLQYACPA RFCLGCSLPM SSTHRCLERA
SWRKRCDRCD MIGHYADACP EIWRQYHLTT KPGPPKKPKT PSGQSTLVYC YNCGQEGHYG
HECTERRMFN QTFPTSPFIY YYDDKYKIRE RDQRIKRKVK ELQKNGDLPR KFKRPHMEAA
DKRPRDIRTS HASWKNNRWP QEKKETQKET MSRNMREREK HRKAARCHED DEDFPRGPRV
HSTPGTSKTQ KPHKPFHHSS HYLKPREDRL SKEGKRGKHK KKESCVGEDS NDNLFLIKQR
KKKSKL
