ID A0A3Q4H5B9_NEOBR Unreviewed; 1502 AA.
AC A0A3Q4H5B9;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE SubName: Full=Zinc finger protein 335-like {ECO:0000313|Ensembl:ENSNBRP00000011587.1};
GN Name=ZNF335 {ECO:0000313|Ensembl:ENSNBRP00000011587.1};
OS Neolamprologus brichardi (Fairy cichlid) (Lamprologus brichardi).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Cichlomorphae; Cichliformes; Cichlidae; African cichlids;
OC Pseudocrenilabrinae; Lamprologini; Neolamprologus.
OX NCBI_TaxID=32507 {ECO:0000313|Ensembl:ENSNBRP00000011587.1, ECO:0000313|Proteomes:UP000261580};
RN [1] {ECO:0000313|Ensembl:ENSNBRP00000011587.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
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DR STRING; 32507.ENSNBRP00000011587; -.
DR Ensembl; ENSNBRT00000011917.1; ENSNBRP00000011587.1; ENSNBRG00000008985.1.
DR GeneTree; ENSGT00940000158508; -.
DR OMA; HKRAHVG; -.
DR Proteomes; UP000261580; Unplaced.
DR Bgee; ENSNBRG00000008985; Expressed in blood and 7 other cell types or tissues.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR Gene3D; 3.30.160.60; Classic Zinc Finger; 6.
DR InterPro; IPR036236; Znf_C2H2_sf.
DR InterPro; IPR013087; Znf_C2H2_type.
DR PANTHER; PTHR24403; ZINC FINGER PROTEIN; 1.
DR PANTHER; PTHR24403:SF36; ZINC FINGER PROTEIN 335; 1.
DR Pfam; PF00096; zf-C2H2; 2.
DR SMART; SM00355; ZnF_C2H2; 13.
DR SUPFAM; SSF57667; beta-beta-alpha zinc fingers; 6.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 6.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 9.
PE 4: Predicted;
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000261580};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|PROSITE-ProRule:PRU00042}.
FT DOMAIN 724..751
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS50157"
FT DOMAIN 754..781
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS50157"
FT DOMAIN 782..809
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS50157"
FT DOMAIN 816..843
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS50157"
FT DOMAIN 844..866
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS50157"
FT DOMAIN 874..901
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS50157"
FT DOMAIN 902..929
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS50157"
FT DOMAIN 1184..1211
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS50157"
FT DOMAIN 1240..1267
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS50157"
FT REGION 1..57
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 208..316
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 328..358
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 370..513
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 539..694
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 233..277
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 285..301
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 332..347
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 397..435
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 453..484
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 560..587
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 588..611
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 627..656
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 678..694
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1502 AA; 165646 MW; 674765167A61AA9D CRC64;
MDLEENEVES SSDAGPSGME EPSESGMGME SSEAMSADSS DAAAPHAQAP ESDCHVGQSS
EGLVVFIPET SSSTDVRVSS VHLPDSSSVA QSTSVSSVST VTQSVLVSES AQVLVHSSAV
SEGAMMVSDS TASTSSDLGS AIDKIIESTI GPDIMNCIAV TSAEDGGAET TQYLILQGPD
DAPMVAQMSS SALSNRIAIE ALAEGPTSTC LDQRDLQGNV EPDQPDDQPG HSGYLEDSSS
QPDQPQHSHP SQYMDCSADG PDQTEESSSS YVECSGEEPD QTRSRSGFPD YSGNNSDQDL
PGYVGCSGAD SNPTSRSHYV VECSAGYPGR AADEGERPHH SRSYIDSSAD HRTQTSRQYA
AEYGGECVVA ADSEQPGCSR YQAEDDDEDD DQNQDPDQPQ HSQQQPQHSC YMESSNGPEA
SLYTDDSSSS DHPLADTAGS GGLPEALEGS ESQPGPFISS SGTYTSNAEP ELAQHCSPSK
EEPQGSQDEA GLGRDMETST VAEGSGERPP NLAELEEMME VVIVQQFKCK MCPYKSASKD
TLINHMRDKH FKPAKRKRGR PPKSETLARQ KAEREEAAKM KAAESQQAAE EEEDDIVDDG
AIDDPEDSDY NPADEDSKGR PPAILKKSAT PTSSSSSPQG NESEEASSSG LDNSAPTVTD
GDAPEAAISQ SDSENKDPSS NQRTEVEYFP RKRGRPSRRF LRKKYKKYMN RRHYKSLKPL
LRPHNCYICG SRFLTLEDLR FHIDSHEGND PELFKCLQCN YRCKRWSSLK EHMFNHEGTK
PFKCEECDYT SVYKKDVIRH SAVHNKELQV PKASEFPCPV CHRVYPMQKR LTQHLKTHSS
EKPHMCDKCG KSFKKRYTFK MHLLTHIQSL DDNFKCEFCD YTCDNKKLLL NHQLSHTNDR
PFKCDYCKYS TSKEEFLVSH LAIKHTEKPF SCDMCHFMTK HRKNLRLHVQ CRHAEAFEEW
SLAHPEEPVK TRRRPFFTLQ QIEELKQQHE DTQSLQNTIV TVDSATLQAM QGMENASVSQ
DALGNTTIIY EQSDLSAQNA LDLLLNMSNA REVAVLKSDG KALEKGTWST VTAASGQAQK
ILTFHVSENG ETVLQEAYEA ATSETGELTH IAIEGYEGGG DFSVVEQAAE SQALEVSGSE
SLKSDKYYLT SALADGVLQQ VELSSEAPAS PSAVGSPSLT TKRFSCRICM ESFHGRSDME
NHKRAHVDAN TFKCPDCDFT STSWPEVKTH MGQHSYLRPH KCPNCSFASK NKKDLRRHMM
THTNEKPFSC KLCGQFNRNG HLKFHMERLH NQDNPARKSR TTASQQTIIV NSDEEALATL
QLQGHQAVIT PERLQALGQE HIIVAQEQAL SDQEEGAYIQ QITTIDGQTV QHLMTGDNQV
TEVQYIISQD GVQHLLPQEY VVVADGNHIQ MPDGQIIQYE HDRTIVQEQQ IAVSHDGQIQ
YLPVSSDQQI VNAEDLEAAA HSAVTDAAMT QTQTVYTEAT PEQLEELQQQ GIHYDVITFS
NE
//
