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Database: UniProt
Entry: I1BYK9_RHIO9
LinkDB: I1BYK9_RHIO9
Original site: I1BYK9_RHIO9 
ID   I1BYK9_RHIO9            Unreviewed;       732 AA.
AC   I1BYK9;
DT   13-JUN-2012, integrated into UniProtKB/TrEMBL.
DT   13-JUN-2012, sequence version 1.
DT   27-MAR-2024, entry version 57.
DE   SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:EIE81289.1};
GN   ORFNames=RO3G_05994 {ECO:0000313|EMBL:EIE81289.1};
OS   Rhizopus delemar (strain RA 99-880 / ATCC MYA-4621 / FGSC 9543 / NRRL
OS   43880) (Mucormycosis agent) (Rhizopus arrhizus var. delemar).
OC   Eukaryota; Fungi; Fungi incertae sedis; Mucoromycota; Mucoromycotina;
OC   Mucoromycetes; Mucorales; Mucorineae; Rhizopodaceae; Rhizopus.
OX   NCBI_TaxID=246409 {ECO:0000313|EMBL:EIE81289.1, ECO:0000313|Proteomes:UP000009138};
RN   [1] {ECO:0000313|EMBL:EIE81289.1, ECO:0000313|Proteomes:UP000009138}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RA 99-880 / ATCC MYA-4621 / FGSC 9543 / NRRL 43880
RC   {ECO:0000313|Proteomes:UP000009138};
RX   PubMed=19578406; DOI=10.1371/journal.pgen.1000549;
RA   Ma L.-J., Ibrahim A.S., Skory C., Grabherr M.G., Burger G., Butler M.,
RA   Elias M., Idnurm A., Lang B.F., Sone T., Abe A., Calvo S.E.,
RA   Corrochano L.M., Engels R., Fu J., Hansberg W., Kim J.-M., Kodira C.D.,
RA   Koehrsen M.J., Liu B., Miranda-Saavedra D., O'Leary S.,
RA   Ortiz-Castellanos L., Poulter R., Rodriguez-Romero J., Ruiz-Herrera J.,
RA   Shen Y.-Q., Zeng Q., Galagan J., Birren B.W., Cuomo C.A., Wickes B.L.;
RT   "Genomic analysis of the basal lineage fungus Rhizopus oryzae reveals a
RT   whole-genome duplication.";
RL   PLoS Genet. 5:E1000549-E1000549(2009).
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DR   EMBL; CH476735; EIE81289.1; -; Genomic_DNA.
DR   AlphaFoldDB; I1BYK9; -.
DR   STRING; 246409.I1BYK9; -.
DR   MEROPS; M67.005; -.
DR   VEuPathDB; FungiDB:RO3G_05994; -.
DR   eggNOG; KOG1279; Eukaryota.
DR   eggNOG; KOG1555; Eukaryota.
DR   InParanoid; I1BYK9; -.
DR   OMA; FQSDFIA; -.
DR   OrthoDB; 2786778at2759; -.
DR   Proteomes; UP000009138; Unassembled WGS sequence.
DR   GO; GO:0008237; F:metallopeptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   CDD; cd08067; MPN_2A_DUB; 1.
DR   CDD; cd00167; SANT; 1.
DR   Gene3D; 3.40.140.10; Cytidine Deaminase, domain 2; 1.
DR   Gene3D; 1.10.10.60; Homeodomain-like; 1.
DR   Gene3D; 1.10.10.10; Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain; 1.
DR   InterPro; IPR009057; Homeobox-like_sf.
DR   InterPro; IPR000555; JAMM/MPN+_dom.
DR   InterPro; IPR037518; MPN.
DR   InterPro; IPR017930; Myb_dom.
DR   InterPro; IPR001005; SANT/Myb.
DR   InterPro; IPR017884; SANT_dom.
DR   InterPro; IPR007526; SWIRM.
DR   InterPro; IPR036388; WH-like_DNA-bd_sf.
DR   PANTHER; PTHR10410:SF39; DOMAIN-CONTAINING PROTEIN, PUTATIVE-RELATED; 1.
DR   PANTHER; PTHR10410; EUKARYOTIC TRANSLATION INITIATION FACTOR 3 -RELATED; 1.
DR   Pfam; PF01398; JAB; 1.
DR   Pfam; PF00249; Myb_DNA-binding; 1.
DR   Pfam; PF04433; SWIRM; 1.
DR   SMART; SM00717; SANT; 1.
DR   SUPFAM; SSF46689; Homeodomain-like; 2.
DR   SUPFAM; SSF102712; JAB1/MPN domain; 1.
DR   PROSITE; PS51294; HTH_MYB; 1.
DR   PROSITE; PS50249; MPN; 1.
DR   PROSITE; PS50090; MYB_LIKE; 1.
DR   PROSITE; PS51293; SANT; 1.
DR   PROSITE; PS50934; SWIRM; 1.
PE   4: Predicted;
KW   DNA-binding {ECO:0000256|ARBA:ARBA00023125};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00023049};
KW   Metalloprotease {ECO:0000256|ARBA:ARBA00023049};
KW   Protease {ECO:0000256|ARBA:ARBA00022670};
KW   Reference proteome {ECO:0000313|Proteomes:UP000009138}.
FT   DOMAIN          56..108
FT                   /note="SANT"
FT                   /evidence="ECO:0000259|PROSITE:PS51293"
FT   DOMAIN          58..108
FT                   /note="HTH myb-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51294"
FT   DOMAIN          58..104
FT                   /note="Myb-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50090"
FT   DOMAIN          290..388
FT                   /note="SWIRM"
FT                   /evidence="ECO:0000259|PROSITE:PS50934"
FT   DOMAIN          494..630
FT                   /note="MPN"
FT                   /evidence="ECO:0000259|PROSITE:PS50249"
FT   REGION          29..63
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          128..223
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        29..46
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        128..199
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        200..217
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   732 AA;  85558 MW;  62BB040ABD6D032C CRC64;
     MIDQEMDSES RQLIEQMLAE EEFYYGKNHS SIPKKKQSDF EPPKKKKGLS SASLPSHKTR
     WNKEEDDKLL EALDKFGYGH WKLIAEYVGT RNRLQCKNHA RHLALAEKIK VPVKQVEIKE
     TEIKETNENK QETYEVSNET RKETETLKED KQEAKTNGET IKDEREVKDK NQTEDYKQEA
     DENEHKVKDD QQGVDVEPKK ENDEDEDEED DLLDIGDTTI EENMIENGMS QEIKAEEDEE
     MTDVSQEEES TMHIAEEQKD TSVFQKETMS PVSQEEDVEN MNHDALETKE VIPETNTPFD
     RSYVSEEEKR QNPEWFKQKY SKTPDRYLKI RNHIIDCWYQ CKPRYLTKTQ ARKGLKDCGD
     VNAIGRVHSW LESVGAINVD CVTNAPRPPK RVPREMSFEE EDIFDASDLV VNYDGPRKRK
     VRNERGEWVD PKELEGRVIE HGVEIPQTIK PKRVKRMLFH QHYYTGDDFN RGYDPFRLVP
     TSYYNDIVLP PFEVEIVSDA LLVMDFHSHL AHTEIIGLMG GNFITKSGTK VLQVKSIFPC
     KSTSTGIQCE MDPASEMRAR EVFAEQGYNV VGWYHSHPTF EPHPSIRDIE NQTSYQTLFR
     EEESGDEPFI GVIVTPYDAE IQSDHSQFQY LHISKEWNES HSYRVPYACK RRVEQCEEVS
     DCILDQLKAL IDEYKDYEHK VDMTSPFGKS TRLEKLLDSL RTHLFIKAEQ EAQFIDKVKE
     LVEKEFMKPE KN
//
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