(data stored in ACNUC30567 zone)

HOGENOM: CANAW_1_PE1014

ID   CANAW_1_PE1014                       STANDARD;      PRT;   622 AA.
AC   CANAW_1_PE1014; Q5AI20;
DT   00-JAN-0000 (Rel. 1, Created)
DT   00-JAN-0000 (Rel. 2, Last sequence update)
DT   00-JAN-0000 (Rel. 3, Last annotation update)
DE   SubName: Full=RNAse L inhibitor-type ATP binding cassette protein;
DE   (CANAW_1.PE1014).
GN   Name=RLI1; ORFNames=CaO19.10552, CaO19.3034;
OS   CANDIDA ALBICANS WO-1.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomyceta; Saccharomycotina;
OC   Saccharomycetes; Saccharomycetales; mitosporic Saccharomycetales; Candida.
OX   NCBI_TaxID=294748;
RN   [0]
RP   -.;
RG   -.;
RL   -.;
CC   -!- SEQ. DATA ORIGIN: Translated from the HOGENOM CDS CANAW_1.PE1014.
CC       Candida albicans WO-1 chromosome 1 supercont1.1 genomic scaffold, whole
CC       genome shotgun sequence.
CC   -!- ANNOTATIONS ORIGIN:Q5AI20_CANAL
CC   -!- SIMILARITY: Belongs to the ABC transporter superfamily.
CC   -!- CAUTION: The sequence shown here is derived from an
CC       EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is
CC       preliminary data.
CC   -!- GENE_FAMILY: HOG000222803 [ FAMILY / ALN / TREE ]
DR   UniProtKB/Swiss-Prot; Q5AI20; -.
DR   EMBL; AACQ01000017; EAL02454.1; -; Genomic_DNA.
DR   EMBL; AACQ01000015; EAL02734.1; -; Genomic_DNA.
DR   RefSeq; XP_721261.1; XM_716168.1.
DR   RefSeq; XP_721532.1; XM_716439.1.
DR   ProteinModelPortal; Q5AI20; -.
DR   STRING; Q5AI20; -.
DR   GeneID; 3636888; -.
DR   GeneID; 3637076; -.
DR   KEGG; cal:CaO19.10552; -.
DR   KEGG; cal:CaO19.3034; -.
DR   CGD; CAL0001388; RLI1.
DR   OMA; AFVIEHD; -.
DR   PhylomeDB; Q5AI20; -.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016887; F:ATPase activity; IEA:InterPro.
DR   GO; GO:0009055; F:electron carrier activity; IEA:InterPro.
DR   GO; GO:0051536; F:iron-sulfur cluster binding; IEA:InterPro.
DR   InterPro; IPR001450; 4Fe4S-bd_dom.
DR   InterPro; IPR017896; 4Fe4S_Fe-S-bd.
DR   InterPro; IPR017900; 4Fe4S_Fe_S_CS.
DR   InterPro; IPR013283; ABC_E.
DR   InterPro; IPR003439; ABC_transporter-like.
DR   InterPro; IPR017871; ABC_transporter_CS.
DR   InterPro; IPR003593; ATPase_AAA+_core.
DR   InterPro; IPR007209; RNaseL-inhib_metal-bd_dom.
DR   Pfam; PF00005; ABC_tran; 2.
DR   Pfam; PF00037; Fer4; 1.
DR   Pfam; PF04068; RLI; 1.
DR   PRINTS; PR01868; ABCEFAMILY.
DR   SMART; SM00382; AAA; 2.
DR   PROSITE; PS00198; 4FE4S_FER_1; 1.
DR   PROSITE; PS51379; 4FE4S_FER_2; 1.
DR   PROSITE; PS00211; ABC_TRANSPORTER_1; 1.
DR   PROSITE; PS50893; ABC_TRANSPORTER_2; 2.
DR   HOGENOMDNA; CANAW_1.PE1014; -.
KW   EEQ42827.100008510fold_1320000031;
KW   ATP-binding cassette sub-family E member 1;
KW   ATP-binding; Nucleotide-binding.
SQ   SEQUENCE   622 AA;  UNKNOWN MW;  UNKNOWN CRC64;
     MSTKGKGKTK NGRGDTHAKN ERIAIVSADR CKPKKCKQEC RKSCPVVKTG KLCIEVTPAS
     KIAFISETLC IGCGICVKKC PFDAITIINL PTNLEGETTH RYSANSFKLH RLPTPRPGQV
     LGLVGTNGIG KSTALKILAG KQKPNLGRYD DPPDWEEILR HFRGSELQNY FTKVLEDNIK
     AIIKPQYVDN IPRALAKSKV KQVGAILESK NEKNDDYNYI LNVLELKNVL NREVENLSGG
     ELQRFALGMT CVQDANVYMF DEPSSYLDVK QRLRAAEIIR SLLNPTTYII CVEHDLSVLD
     YLSDFVCILY GAPSVYGVVT LPASVREGIN IFLDGHIPTE NLRFRTESLQ FRLADAADDL
     ILDKSNSLEY PSLQKTQGDF KLRVEAGDFT NSEILVMMGE NGTGKTTFCK LLAGAIAPDG
     GQEIPKLNVS MKPQKIAPKF TGTVRQLFFK KIRAAFLHPQ FQTDVVKPLK IEDIVDQEVQ
     TLSGGELQRV AIVLALGIPA DIYLIDEPSA YLDSEQRIIC SKVIRRFILH AKKTAFIVEH
     DFIMATYLAD RVIVFEGQPS KDAVARSPES LLTGCNRFLK NLNVTFRRDP NSYRPRINKL
     DSQMDKEQKA SGNYFFLENT EL
//

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