ID A0A498MST7_LABRO Unreviewed; 1158 AA.
AC A0A498MST7;
DT 05-JUN-2019, integrated into UniProtKB/TrEMBL.
DT 05-JUN-2019, sequence version 1.
DT 27-MAR-2024, entry version 14.
DE SubName: Full=Zinc finger protein 407 {ECO:0000313|EMBL:RXN22953.1};
GN ORFNames=ROHU_006544 {ECO:0000313|EMBL:RXN22953.1};
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:RXN22953.1, ECO:0000313|Proteomes:UP000290572};
RN [1] {ECO:0000313|EMBL:RXN22953.1, ECO:0000313|Proteomes:UP000290572}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DASCIFA01 {ECO:0000313|EMBL:RXN22953.1};
RC TISSUE=Testis {ECO:0000313|EMBL:RXN22953.1};
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 -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
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:RXN22953.1}.
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DR EMBL; QBIY01012573; RXN22953.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A498MST7; -.
DR STRING; 84645.A0A498MST7; -.
DR Proteomes; UP000290572; Unassembled WGS sequence.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR Gene3D; 3.30.160.60; Classic Zinc Finger; 11.
DR InterPro; IPR003604; Matrin/U1-like-C_Znf_C2H2.
DR InterPro; IPR036236; Znf_C2H2_sf.
DR InterPro; IPR013087; Znf_C2H2_type.
DR PANTHER; PTHR24403:SF67; ENHANCER OF VARIEGATION 3-9-RELATED; 1.
DR PANTHER; PTHR24403; ZINC FINGER PROTEIN; 1.
DR Pfam; PF13894; zf-C2H2_4; 1.
DR Pfam; PF12874; zf-met; 1.
DR SMART; SM00355; ZnF_C2H2; 17.
DR SMART; SM00451; ZnF_U1; 5.
DR SUPFAM; SSF57667; beta-beta-alpha zinc fingers; 5.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 5.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 5.
PE 4: Predicted;
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000290572};
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 546..575
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS50157"
FT DOMAIN 705..732
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS50157"
FT DOMAIN 733..762
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS50157"
FT DOMAIN 763..790
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS50157"
FT DOMAIN 791..818
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS50157"
FT REGION 113..143
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 350..419
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 479..510
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 357..376
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 392..419
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 485..500
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1158 AA; 129762 MW; B760DD8149C6904B CRC64;
MTRPTESKAQ HQCDRCTFTA NNSVMLAQHI KTHHPVEHRF HCRACHYYTT TIEAMEVHLS
EEVHQQVAKE KNISPIFKDC VEKILVILSD LREEGDMNES DTREQCSKEA EEVQEMENVL
PEPAGAVRKG SPHKRKRGRP KTSNVTVCSH CGLVASNATN LSVHIRRRHS RLYSFVCKLC
NYYCVTKGDM DRHCETKKHI NKMQAAGSEG SGVVLLDAEQ PIQAKKNEAE LGDKVSVIET
TIDEVDKNNS TVPCKKSKYD LSNICTQCDF VAHSTPSLAL HVRRKHTKDF EFVCLACSYY
TVTRREMFRH MATEKHKQKR ECYLKKQNQS FNNGQADLTD MTTKSTFEDP ETIAGSEVVR
DSSTLTSSST TTTDEENSAK VGEENCANED GAKQSAVKNT SKDNEESSTN PAESNVSDMV
QSLTMVKDAM LEDMDEENVF DDDEMTDLGD DSPSTEKHLR AIQFDACIFS LKTLAERKQT
SHDEEQTTGA LNQQSMKKPK TPVVPETKTT KPMPRIRCED CGFLADGLSG LNVHISMKHP
SKEKHFHCLL CGKSFYTESN LQQHLSSAAH VRNEHGSIED LPEGGASFKC VRCSEPCQTE
QELFVHIKEK HEELLREVNK YVLEDTEQIN RERQENQGNV CKYCGKVCKS SNSMAFLAHI
RTHTGSKPFM CKICNFATAQ LGDARNHVKR HLGMREYKCH ICGKFECELC ERSFSEKWAL
NNHMKLHTGD KPYKCAWPSC HYAFLTLSAM KDHHRTHTGE KSFLCDLCGF AGGTRHALTK
HRRQHTGERP FKCQLCNFAS TTQSHLTRHK RVHTGEKPYR CPWCDYRSNC AENIRKHILH
TGKHEGVKMY NCPKCSYATN APMDFRNHLK ETHPDIENPD LAYLHAGIVS KSFECRLKGQ
GASFVQAESV FTPDESELGS EAVQQVIIIQ GYSGGEVAID HALEESAAAT LQTLAMSSQL
AEVLHITEDG QLITSGREVS TVTGGQTTQY VLVESSGETV EDARQEGEEA VHSVSESSSA
LDALLCAVTE LGQQGGPREG EITTTTVSEH MPEENCEGQT SQTQRQSEGQ VYEERAEVGV
VAQVMSSTHE HPSEEMQEVL QFAASQLMMK EGLTQVIVND EGTHYIVTQL DDSTLHVEGT
VEDPSGEEAI VYSEINPE
//
