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Database: UniProt
Entry: A0A093TK87_PHACA
LinkDB: A0A093TK87_PHACA
Original site: A0A093TK87_PHACA 
ID   A0A093TK87_PHACA        Unreviewed;      1080 AA.
AC   A0A093TK87;
DT   26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT   26-NOV-2014, sequence version 1.
DT   27-MAR-2024, entry version 37.
DE   RecName: Full=ribonuclease III {ECO:0000256|ARBA:ARBA00012177};
DE            EC=3.1.26.3 {ECO:0000256|ARBA:ARBA00012177};
DE   Flags: Fragment;
GN   ORFNames=N336_03026 {ECO:0000313|EMBL:KFW94649.1};
OS   Phalacrocorax carbo (Great cormorant) (Pelecanus carbo).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Suliformes; Phalacrocoracidae;
OC   Phalacrocorax.
OX   NCBI_TaxID=9209 {ECO:0000313|EMBL:KFW94649.1, ECO:0000313|Proteomes:UP000053238};
RN   [1] {ECO:0000313|EMBL:KFW94649.1, ECO:0000313|Proteomes:UP000053238}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BGI_N336 {ECO:0000313|EMBL:KFW94649.1};
RA   Zhang G., Li C.;
RT   "Genome evolution of avian class.";
RL   Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Endonucleolytic cleavage to 5'-phosphomonoester.; EC=3.1.26.3;
CC         Evidence={ECO:0000256|ARBA:ARBA00000109};
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DR   EMBL; KL442824; KFW94649.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A093TK87; -.
DR   Proteomes; UP000053238; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0004525; F:ribonuclease III activity; IEA:InterPro.
DR   GO; GO:0003723; F:RNA binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0031054; P:pre-miRNA processing; IEA:InterPro.
DR   GO; GO:0006364; P:rRNA processing; IEA:InterPro.
DR   CDD; cd19877; DSRM_RNAse_III_meta_like; 1.
DR   CDD; cd00593; RIBOc; 2.
DR   Gene3D; 3.30.160.20; -; 1.
DR   Gene3D; 1.10.1520.10; Ribonuclease III domain; 2.
DR   HAMAP; MF_00104; RNase_III; 1.
DR   InterPro; IPR014720; dsRBD_dom.
DR   InterPro; IPR011907; RNase_III.
DR   InterPro; IPR000999; RNase_III_dom.
DR   InterPro; IPR044442; RNAse_III_DSRM__animal.
DR   InterPro; IPR036389; RNase_III_sf.
DR   PANTHER; PTHR11207:SF0; RIBONUCLEASE 3; 1.
DR   PANTHER; PTHR11207; RIBONUCLEASE III; 1.
DR   Pfam; PF00035; dsrm; 1.
DR   Pfam; PF14622; Ribonucleas_3_3; 1.
DR   Pfam; PF00636; Ribonuclease_3; 1.
DR   SMART; SM00358; DSRM; 1.
DR   SMART; SM00535; RIBOc; 2.
DR   SUPFAM; SSF54768; dsRNA-binding domain-like; 1.
DR   SUPFAM; SSF69065; RNase III domain-like; 2.
DR   PROSITE; PS50137; DS_RBD; 1.
DR   PROSITE; PS00517; RNASE_3_1; 2.
DR   PROSITE; PS50142; RNASE_3_2; 2.
PE   3: Inferred from homology;
KW   Endonuclease {ECO:0000256|ARBA:ARBA00022759};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Nuclease {ECO:0000256|ARBA:ARBA00022722};
KW   Reference proteome {ECO:0000313|Proteomes:UP000053238};
KW   RNA-binding {ECO:0000256|ARBA:ARBA00022884, ECO:0000256|PROSITE-
KW   ProRule:PRU00266}; Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        34..58
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          582..762
FT                   /note="RNase III"
FT                   /evidence="ECO:0000259|PROSITE:PS50142"
FT   DOMAIN          813..939
FT                   /note="RNase III"
FT                   /evidence="ECO:0000259|PROSITE:PS50142"
FT   DOMAIN          966..1040
FT                   /note="DRBM"
FT                   /evidence="ECO:0000259|PROSITE:PS50137"
FT   REGION          1..25
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          65..111
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          161..204
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        65..101
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        161..184
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        185..199
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:KFW94649.1"
FT   NON_TER         1080
FT                   /evidence="ECO:0000313|EMBL:KFW94649.1"
SQ   SEQUENCE   1080 AA;  126008 MW;  CEB153ECBEFD66A7 CRC64;
     RERERERHRH RESRRSPSPD RSYKKDYKRA GSKLFVFYYK TVTVKIITRI AFVCFVPLSR
     SPSRERKRPR WEEDRERWSE NQSSSKEKNY TAVKDKESEE NASEKNEEED EELLKPVWVR
     CTHSESYYSN DPMDQVGDST VVGTSKLRDL YEKFDEELGK RQAKAKAARP PWEPPKTKLD
     EDLESSSDSD CDSEDDSSCS SSSDSEVFDV IAEIKRKKAH PDRLHEELWY NDPGQMNDGP
     LCKCSAKARR TGIRHGIYPG EEPIKPCRPM TNNAGRLYHY RITVSPPTNF LTDRPTVIEY
     DDHEYIFEGF SMFAHAPLTN IPLCKVIRFN IDYTIHFIEE MMPENFCVRG LELFSSYLFK
     DILELYDWNL KGPSTDNDSI SCPRFHFMPR FVRFLPDGGK EVLSMHQILL YLLRCNKALV
     PEEEIANMLQ WEELEWQKYA EECKGMIVTS PGMKPSSVRI DQLDREQFNP DVITFPIIVH
     FGIRPAQLSY AGDPQYQKLW KSYVKLRHLL ANSPKVKQAD KQKLSQREEA LQKIRQKNTM
     RREVTVELSS QGFWKTGIRS DVCQHAMMLP VLTHHVRYHQ CLMHLDKLIG YTFRDRCLLQ
     LAMTHPSHHL NFGMNPDHAR NSLSNCGIRQ PKYGDRKVHH MHMRKKGINT LINIMSRLGQ
     DDPAPSRINH NERLEFLGDA VVEFLTSVHL YYLFPTLEEG GLATYRTAIV QNQHLAMLAK
     KLELDRFMLY AHGPDLCRES DLRHAMANCF EALIGAVYLE GSLEEAKQLF GRLLFNDKDL
     RDVWLNYPLH PLQLQESNTD RQLIETSPVL QKLTEFEDAI GVIFTHVRLL ARAFTLRTVG
     FNHLTLGHNQ RMEFLGDSIM QLVATEYLFI HFPDHHEGHL TLLRSSLVNN RTQAKVAEEL
     GMQEFAITND KTKRPVALRT KTLADLLESF IAALYIDKDL EYVHTFMNVC FFPRLKEFIL
     NQDWNDPKSQ LQQCCLTLRT EGKEPDIPLY KTLQTVGPSH ARTYTVAVYF KGERIGCGKG
     PSIQQAEMGA AMDALEKYNF PQMAHQKRFI ERKYRQELKE MRWEREHQER EPDETEEARK
//
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