ID A0A2U4BF28_TURTR Unreviewed; 863 AA.
AC A0A2U4BF28;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 24-JAN-2024, entry version 23.
DE SubName: Full=Zinc finger protein 658 isoform X1 {ECO:0000313|RefSeq:XP_019791801.1, ECO:0000313|RefSeq:XP_019791802.1};
GN Name=ZNF658 {ECO:0000313|RefSeq:XP_019791801.1,
GN ECO:0000313|RefSeq:XP_019791802.1, ECO:0000313|RefSeq:XP_019791803.1};
OS Tursiops truncatus (Atlantic bottle-nosed dolphin) (Delphinus truncatus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Whippomorpha; Cetacea; Odontoceti;
OC Delphinidae; Tursiops.
OX NCBI_TaxID=9739 {ECO:0000313|Proteomes:UP000245320, ECO:0000313|RefSeq:XP_019791802.1};
RN [1] {ECO:0000313|RefSeq:XP_019791801.1, ECO:0000313|RefSeq:XP_019791802.1}
RP IDENTIFICATION.
RC TISSUE=Spleen {ECO:0000313|RefSeq:XP_019791801.1,
RC ECO:0000313|RefSeq:XP_019791802.1};
RG RefSeq;
RL Submitted (SEP-2023) to UniProtKB.
CC -!- SIMILARITY: Belongs to the krueppel C2H2-type zinc-finger protein
CC family. {ECO:0000256|ARBA:ARBA00006991}.
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DR RefSeq; XP_019791800.1; XM_019936241.1.
DR RefSeq; XP_019791801.1; XM_019936242.2.
DR RefSeq; XP_019791802.1; XM_019936243.2.
DR RefSeq; XP_019791803.1; XM_019936244.2.
DR GeneID; 101336681; -.
DR OrthoDB; 5250617at2759; -.
DR Proteomes; UP000245320; Chromosome 6.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006355; P:regulation of DNA-templated transcription; IEA:InterPro.
DR CDD; cd07765; KRAB_A-box; 1.
DR Gene3D; 6.10.140.140; -; 1.
DR Gene3D; 3.30.160.60; Classic Zinc Finger; 18.
DR InterPro; IPR001909; KRAB.
DR InterPro; IPR036051; KRAB_dom_sf.
DR InterPro; IPR036236; Znf_C2H2_sf.
DR InterPro; IPR013087; Znf_C2H2_type.
DR PANTHER; PTHR24381; ZINC FINGER PROTEIN; 1.
DR PANTHER; PTHR24381:SF390; ZINC FINGER PROTEIN OZF; 1.
DR Pfam; PF01352; KRAB; 1.
DR Pfam; PF00096; zf-C2H2; 15.
DR SMART; SM00349; KRAB; 1.
DR SMART; SM00355; ZnF_C2H2; 16.
DR SUPFAM; SSF57667; beta-beta-alpha zinc fingers; 9.
DR SUPFAM; SSF109640; KRAB domain (Kruppel-associated box); 1.
DR PROSITE; PS50805; KRAB; 1.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 12.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 16.
PE 3: Inferred from homology;
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000245320};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00042}.
FT DOMAIN 8..84
FT /note="KRAB"
FT /evidence="ECO:0000259|PROSITE:PS50805"
FT DOMAIN 406..433
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS50157"
FT DOMAIN 434..461
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS50157"
FT DOMAIN 462..489
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS50157"
FT DOMAIN 490..517
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS50157"
FT DOMAIN 518..545
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS50157"
FT DOMAIN 546..573
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS50157"
FT DOMAIN 574..601
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS50157"
FT DOMAIN 602..629
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS50157"
FT DOMAIN 630..657
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS50157"
FT DOMAIN 658..685
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS50157"
FT DOMAIN 686..713
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS50157"
FT DOMAIN 714..741
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS50157"
FT DOMAIN 742..769
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS50157"
FT DOMAIN 770..797
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS50157"
FT DOMAIN 798..825
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS50157"
FT DOMAIN 826..854
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS50157"
SQ SEQUENCE 863 AA; 99803 MW; 4F886846A83C8C63 CRC64;
MNTAQGSVSF EDVTVEFTQD EWQYVGPALR TLYKDVMLEN YSHLVSLVVT FAGYCIIKPQ
VIFKLEHGEE PWPSEEEFLN QKYPGCYRVD VHIEENQERQ EKPLWQVVFT DNKILSKEEQ
KALEKPFYFS ITPDFSGKMP SKRDSCRMNL PVVSELILSD RNYSRNKTDY INVCEKLQLD
IQREKTHTGE QCYKYNENMK ALSYVKDHHK FQTLEQSFEC NEYGKVLHDK TICVTAKSSV
KGEESCKDNE FRGNCVKAAL FNHMRTGTRK KCFDLNECGK SCEYNEVHMA LAHYECNESG
NNFSGNSPLT QPQRTVTGQG AFESSKCEEN LSQSSGRIVH QKTQTRDTFC VYNGFTNTIY
QKLDFTVHQR IHKEEKFYQC DKYEKSSYQN SALSVHQQCD TGEKSFELTE CRKSFYQKAH
LIQHQRTHPG EKPYECEECG KSFCSYSHPI HYPGTHMGVN LYECNECGKT SADNSTLRAH
QRIHTEEKPF KCNDCERSFA HNSARRAHQR IHTGEKPYEC NDCEKTFAHN STLRAHQKIH
TGVKLYKCNE CGKTFSQKTR LSTHQRIHTG EKPYGCSECG KTFSQKSYLS GHERIHKGEK
PYECNECGKT FVYKAALIVH QRIHTGEKPY ECNECGKTFS QRTHLYAHQR THTGEKPYEC
KECGKTFADN SALRAHQRIH KGEKPYECSE CGKTFSKTSH LRAHLRTRTG EKPYECNECG
KTFSQKSYVS AHQRIHTGEK PYECNICGKP FAHNSTLRVH QRIHTGVKSY KCNECGKTFS
QKSHLSAHQR IHTGEKPYEC NECGKAFAQN STLGVHLRIH TGERPYKCYE CGKTFVRKAA
LRVHHTRMHS REKTLACNEF GMC
//