ID A0A0J7NN49_LASNI Unreviewed; 784 AA.
AC A0A0J7NN49;
DT 14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT 14-OCT-2015, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE SubName: Full=Putative zinc finger protein 729 {ECO:0000313|EMBL:KMQ93940.1};
GN ORFNames=RF55_5931 {ECO:0000313|EMBL:KMQ93940.1};
OS Lasius niger (Black garden ant).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Formicoidea;
OC Formicidae; Formicinae; Lasius; Lasius.
OX NCBI_TaxID=67767 {ECO:0000313|EMBL:KMQ93940.1, ECO:0000313|Proteomes:UP000036403};
RN [1] {ECO:0000313|EMBL:KMQ93940.1, ECO:0000313|Proteomes:UP000036403}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC TISSUE=Whole {ECO:0000313|EMBL:KMQ93940.1};
RA Konorov E.A., Nikitin M.A., Kirill M.V., Chang P.;
RT "Lasius niger genome sequencing.";
RL Submitted (APR-2015) to the EMBL/GenBank/DDBJ databases.
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:KMQ93940.1}.
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DR EMBL; LBMM01003123; KMQ93940.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0J7NN49; -.
DR STRING; 67767.A0A0J7NN49; -.
DR PaxDb; 67767-A0A0J7NN49; -.
DR OrthoDB; 3374558at2759; -.
DR Proteomes; UP000036403; Unassembled WGS sequence.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR GO; GO:0090304; P:nucleic acid metabolic process; IEA:UniProt.
DR Gene3D; 3.30.160.60; Classic Zinc Finger; 14.
DR Gene3D; 3.30.420.10; Ribonuclease H-like superfamily/Ribonuclease H; 1.
DR InterPro; IPR012337; RNaseH-like_sf.
DR InterPro; IPR036397; RNaseH_sf.
DR InterPro; IPR036236; Znf_C2H2_sf.
DR InterPro; IPR013087; Znf_C2H2_type.
DR PANTHER; PTHR24394:SF29; GM08392P; 1.
DR PANTHER; PTHR24394; ZINC FINGER PROTEIN; 1.
DR Pfam; PF00096; zf-C2H2; 13.
DR Pfam; PF12874; zf-met; 1.
DR SMART; SM00355; ZnF_C2H2; 15.
DR SUPFAM; SSF57667; beta-beta-alpha zinc fingers; 9.
DR SUPFAM; SSF53098; Ribonuclease H-like; 1.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 15.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 15.
PE 4: Predicted;
KW Metal-binding {ECO:0000256|PROSITE-ProRule:PRU00042};
KW Reference proteome {ECO:0000313|Proteomes:UP000036403};
KW Zinc {ECO:0000256|PROSITE-ProRule:PRU00042};
KW Zinc-finger {ECO:0000256|PROSITE-ProRule:PRU00042}.
FT DOMAIN 256..283
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS50157"
FT DOMAIN 284..312
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS50157"
FT DOMAIN 401..428
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS50157"
FT DOMAIN 429..456
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS50157"
FT DOMAIN 457..484
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS50157"
FT DOMAIN 503..530
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS50157"
FT DOMAIN 531..558
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS50157"
FT DOMAIN 559..586
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS50157"
FT DOMAIN 587..614
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS50157"
FT DOMAIN 615..643
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS50157"
FT DOMAIN 644..671
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS50157"
FT DOMAIN 672..699
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS50157"
FT DOMAIN 700..728
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS50157"
FT DOMAIN 729..756
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS50157"
FT DOMAIN 757..784
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS50157"
FT REGION 303..368
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 303..322
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 323..342
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 784 AA; 90905 MW; 9EBC82B71BC1C62E CRC64;
MTVEPTFHFK YFFVYENQPS KFVVLRALCN NTAKEVARNL LDILAIIGAP RVLQSGNGRK
FAEQVVHELR SLWNDSLILH GDVPKCEVSC RDFKSLLESW MRKNPTRTWC EGLNFIQILH
NSTHRCQNGK IPCDVLFGRD VRENFQSLGI EKDTENLWTE EEWIEHLSHR ENKDIVTMTK
DTQRTSDSTN YCEENDNVQD ARSQKAFSRN DDINGFSFVN VKNESFTSNL RATDSTTRGE
IEIGKNELKT ENTQFLKCKY CQKQYMKLGH LKNHMRTHKA QRVLRCKLCS KTFSVPRLYA
KHMKQSHGQD KLADKEEEIP VSRNTRSNAA DAVTTASNVE RSEIRTAHNE LSDPETTNED
CDASLDDTKN SYSKTAKISG HIGRRKSSAE SRSVSKIQST LQCTYCEQKF SFPSVLERHI
RSHTNERPYV CDVCNKSFKQ LGHLSQHSLT HHDYRSFQCT VCGVKFDSLD SLKQHAHSHK
GDATSTTTTM TTTSKIRDVY RLFECDNCKK VFTTKSVLER HIFTHTQERQ YDCKVCGKRF
KQAGHVKSHM LVHTGERRFQ CTVCSKRFSL SNSLKKHMYV HNGEKPYQCD VCGARFLEKR
NLNGHLLTHT NERPYCCKIC GKRYTLADTL RRHVSAAHED GRTYQCEICA KMFKQLAHLS
VHKKVHNDER PFQCHLCEKN FKHKNVLKSH LAIHANVRPF ECDVCKATFV RKTNLQTHIS
SAHMNERPYA CTICSKRFKQ ISHLNGHVVV HSNLMPYKCD YCDRRCNRLD NLKKHMRLHT
KNKE
//
