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Database: UniProt
Entry: A0A498MH74_LABRO
LinkDB: A0A498MH74_LABRO
Original site: A0A498MH74_LABRO 
ID   A0A498MH74_LABRO        Unreviewed;       935 AA.
AC   A0A498MH74;
DT   05-JUN-2019, integrated into UniProtKB/TrEMBL.
DT   05-JUN-2019, sequence version 1.
DT   24-JAN-2024, entry version 13.
DE   SubName: Full=Ankyrin repeat and MYND domain-containing 1 {ECO:0000313|EMBL:RXN20481.1};
GN   ORFNames=ROHU_025032 {ECO:0000313|EMBL:RXN20481.1}, ROHU_032737
GN   {ECO:0000313|EMBL:RXN06561.1};
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:RXN20481.1, ECO:0000313|Proteomes:UP000290572};
RN   [1] {ECO:0000313|EMBL:RXN20481.1, ECO:0000313|Proteomes:UP000290572}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DASCIFA01 {ECO:0000313|EMBL:RXN20481.1};
RC   TISSUE=Testis {ECO:0000313|EMBL:RXN20481.1};
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   -!- 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:RXN20481.1}.
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DR   EMBL; QBIY01013362; RXN06561.1; -; Genomic_DNA.
DR   EMBL; QBIY01012644; RXN20481.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A498MH74; -.
DR   STRING; 84645.A0A498MH74; -.
DR   Proteomes; UP000290572; Unassembled WGS sequence.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   Gene3D; 6.10.140.2220; -; 1.
DR   Gene3D; 1.25.40.20; Ankyrin repeat-containing domain; 3.
DR   Gene3D; 2.20.110.10; Histone H3 K4-specific methyltransferase SET7/9 N-terminal domain; 2.
DR   InterPro; IPR002110; Ankyrin_rpt.
DR   InterPro; IPR036770; Ankyrin_rpt-contain_sf.
DR   InterPro; IPR003409; MORN.
DR   InterPro; IPR002893; Znf_MYND.
DR   PANTHER; PTHR15897; ANKYRIN REPEAT AND MYND DOMAIN PROTEIN 1; 1.
DR   PANTHER; PTHR15897:SF2; ANKYRIN REPEAT AND MYND DOMAIN-CONTAINING PROTEIN 1; 1.
DR   Pfam; PF00023; Ank; 1.
DR   Pfam; PF12796; Ank_2; 1.
DR   Pfam; PF13637; Ank_4; 1.
DR   Pfam; PF02493; MORN; 4.
DR   Pfam; PF01753; zf-MYND; 1.
DR   SMART; SM00248; ANK; 5.
DR   SMART; SM00698; MORN; 3.
DR   SUPFAM; SSF48403; Ankyrin repeat; 2.
DR   SUPFAM; SSF82185; Histone H3 K4-specific methyltransferase SET7/9 N-terminal domain; 1.
DR   SUPFAM; SSF144232; HIT/MYND zinc finger-like; 1.
DR   PROSITE; PS50297; ANK_REP_REGION; 2.
DR   PROSITE; PS50088; ANK_REPEAT; 3.
DR   PROSITE; PS01360; ZF_MYND_1; 1.
DR   PROSITE; PS50865; ZF_MYND_2; 1.
PE   4: Predicted;
KW   ANK repeat {ECO:0000256|PROSITE-ProRule:PRU00023};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000290572};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833};
KW   Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW   ProRule:PRU00134}.
FT   REPEAT          272..304
FT                   /note="ANK"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT   REPEAT          609..644
FT                   /note="ANK"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT   REPEAT          687..720
FT                   /note="ANK"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT   DOMAIN          883..923
FT                   /note="MYND-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50865"
FT   REGION          334..382
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          844..867
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        343..382
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        847..867
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   935 AA;  105819 MW;  A27A16E2DE2003A7 CRC64;
     MKHGTGVFTW PNGEFYKGSF FKDYRHGKGM YSWPDGSKYT GKFYLNRKEG YGVQVFPDGS
     TFEGLYHADE RFGPGVMTYP DGRQDVGLWH RERLLRLCTT LESGFSLEDF PEHMRRLPRN
     HLKQPQLLLD VESSRETDQG LSEDKDRFIL PPDIESYSTD SDHLPIPRCL RRELDLHFFG
     TSDVSKEQQS PSTALPLQQR MNAHIQRHRS ETDALDWDVA AVLNMNRTQF GPKGPLELNS
     EKLIKEASHG ECRNVYRILR DEKVHPDVSD ARGHTALIAA TVNCHNDVIH ILLDNGADVN
     KLNDEGMSAL AVCHVLYYPL QSLHETLAER VTQNISPEPQ IKPLEDVSHE SSPDPMTETP
     KDESGQETFE TPTESDQADR SLEPENLNNL EKLEEQINED EIVPQPDQAE EPQPHFQINE
     DTDPNNEVVL QFECEEDKPI EEPHVIIMSR SIQVFDDKIP VGSVSWREKE AKTVVDTEEE
     MTDLEIEENL ERSIRSDDPT FDSARSMASF HIDVTEEILQ KSAEILCQTG TVTPADTQET
     VRKIALLKTE HRNRWTTIKL LLERGADPNA STVPMPVIFL AIKAAHVKGV RRLLECGART
     DIPLLPEQKG LYPLHIAAGL SGAEGPEITE LLLHALADPD VKAQDTHEVY EFDKDMFEPQ
     AFKNQHLIAS GPLAKFNEAH IEVPQEGGRT PLHVACQRDS DYANARDVVA LLLSHNANPN
     DVWSGHSPLS LAIASGNDLL EKLIKAGADI LMPVVVGEGR RSSEISFITS TNYAPLTRPV
     PLSHQNQRMA HTPYHALNKH ERQAYNARRQ LLDLMGDLLR QAAIRMEKER SQDVLGVSPA
     EKLLRTGSGA TPSQLSSPEE NNRTSFNKRI NQRVQRKPRF KYCYECGRSV GVQLLACTRC
     REVFYCSKTC KTKAWDERHR DECVRVPGKC FLYRV
//
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