ID A0A163KN89_ABSGL Unreviewed; 1102 AA.
AC A0A163KN89;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 27-MAR-2024, entry version 36.
DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:SAM09443.1};
GN Name=ABSGL_15119.1 scaffold 15162 {ECO:0000313|EMBL:SAM09443.1};
OS Absidia glauca (Pin mould).
OC Eukaryota; Fungi; Fungi incertae sedis; Mucoromycota; Mucoromycotina;
OC Mucoromycetes; Mucorales; Cunninghamellaceae; Absidia.
OX NCBI_TaxID=4829 {ECO:0000313|EMBL:SAM09443.1};
RN [1] {ECO:0000313|EMBL:SAM09443.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 101.48 {ECO:0000313|EMBL:SAM09443.1};
RA Evans L.H., Alamgir A., Owens N., Weber N.D., Virtaneva K., Barbian K.,
RA Babar A., Rosenke K.;
RL Submitted (APR-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
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DR EMBL; LT555008; SAM09443.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A163KN89; -.
DR STRING; 4829.A0A163KN89; -.
DR InParanoid; A0A163KN89; -.
DR OrthoDB; 228305at2759; -.
DR Proteomes; UP000078561; Unassembled WGS sequence.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0000175; F:3'-5'-RNA exonuclease activity; IEA:InterPro.
DR GO; GO:0004301; F:epoxide hydrolase activity; IEA:UniProt.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-UniRule.
DR CDD; cd06133; ERI-1_3'hExo_like; 1.
DR Gene3D; 3.30.70.330; -; 1.
DR Gene3D; 3.40.50.1820; alpha/beta hydrolase; 1.
DR Gene3D; 3.30.420.10; Ribonuclease H-like superfamily/Ribonuclease H; 1.
DR Gene3D; 4.10.1060.10; Zinc finger, RanBP2-type; 5.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR000073; AB_hydrolase_1.
DR InterPro; IPR000639; Epox_hydrolase-like.
DR InterPro; IPR047201; ERI-1_3'hExo-like.
DR InterPro; IPR013520; Exonuclease_RNaseT/DNA_pol3.
DR InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
DR InterPro; IPR035979; RBD_domain_sf.
DR InterPro; IPR012337; RNaseH-like_sf.
DR InterPro; IPR036397; RNaseH_sf.
DR InterPro; IPR000504; RRM_dom.
DR InterPro; IPR001876; Znf_RanBP2.
DR InterPro; IPR036443; Znf_RanBP2_sf.
DR PANTHER; PTHR43329:SF4; BIFUNCTIONAL EPOXIDE HYDROLASE 2; 1.
DR PANTHER; PTHR43329; EPOXIDE HYDROLASE; 1.
DR Pfam; PF00561; Abhydrolase_1; 1.
DR Pfam; PF00929; RNase_T; 1.
DR Pfam; PF00076; RRM_1; 1.
DR Pfam; PF00641; zf-RanBP; 4.
DR PRINTS; PR00412; EPOXHYDRLASE.
DR SMART; SM00479; EXOIII; 1.
DR SMART; SM00360; RRM; 1.
DR SMART; SM00547; ZnF_RBZ; 5.
DR SUPFAM; SSF53474; alpha/beta-Hydrolases; 1.
DR SUPFAM; SSF90209; Ran binding protein zinc finger-like; 5.
DR SUPFAM; SSF53098; Ribonuclease H-like; 1.
DR SUPFAM; SSF54928; RNA-binding domain, RBD; 1.
DR PROSITE; PS50102; RRM; 1.
DR PROSITE; PS01358; ZF_RANBP2_1; 4.
DR PROSITE; PS50199; ZF_RANBP2_2; 5.
PE 4: Predicted;
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000078561};
KW RNA-binding {ECO:0000256|PROSITE-ProRule:PRU00176};
KW Zinc {ECO:0000256|PROSITE-ProRule:PRU00322};
KW Zinc-finger {ECO:0000256|PROSITE-ProRule:PRU00322}.
FT DOMAIN 640..718
FT /note="RRM"
FT /evidence="ECO:0000259|PROSITE:PS50102"
FT DOMAIN 741..770
FT /note="RanBP2-type"
FT /evidence="ECO:0000259|PROSITE:PS50199"
FT DOMAIN 847..878
FT /note="RanBP2-type"
FT /evidence="ECO:0000259|PROSITE:PS50199"
FT DOMAIN 913..941
FT /note="RanBP2-type"
FT /evidence="ECO:0000259|PROSITE:PS50199"
FT DOMAIN 1006..1035
FT /note="RanBP2-type"
FT /evidence="ECO:0000259|PROSITE:PS50199"
FT DOMAIN 1061..1092
FT /note="RanBP2-type"
FT /evidence="ECO:0000259|PROSITE:PS50199"
FT REGION 324..373
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 775..844
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 882..907
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 347..363
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 817..844
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 882..898
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1102 AA; 121396 MW; FA818D0C77EFE331 CRC64;
MAIDKNDPST FNHNYVTANG IRMHYVDENA SSDKPLLLLH GWPDLWLGWR EQIPFLVDLG
YRVIVPTLRG FGETDAPYSP DEYGMGTISK DMVGLLDHLQ LPTVTVLSHD WGGFVAWRFA
QLYPERVVNV ASFCTPYGSV LKQYIPLEKV VEFLPNFKYQ LHLRSPEAEK EMDENIAPFF
GRVFRPIKDS VGPLIDPETG MMVAGRPVIQ KHDALSQKVF DYYVDAYTKR GARGGLNWYK
QSWNNYDQCK HLEDIVTQPA LMVIATEDRA LPPAMSEKMH EFIPKLEKHT VAGAGHWVLW
ERPDECNDIL KTWLGKVYPV NSSPKLRVDS DQEEENVTIN KKPLLDSPRY DQTTASNTNG
NDNDNDNDDQ HDAMTMNYAP TIEQDTPLSP YAADCASVET IVPYPYLVLI NMEVTCDENP
TNPAAVQVSK ENAEIIQLSF AIVNSSDMKV VDEQVIHVKP ERTPLTQFCT QITGITSDTL
ASAGTLQDAV EILDSAIQTE ILDRQLEFCF VTHGGWLLRI QLSREARDKK LALPGYLAHP
RMFDLKQELQ RWQGHHPETH LRTTSLKELC DTFQLPLVGH GDSYSGDSDN DKKINDSDID
ILATTISVIR YLTKFRYNDV FVHPIDTASD LQQFNNEESL TVHLAGLPYE VTQGELEAWF
SSNGLRPARM WMMQMTEQTK PSLSGFVVFT QHEDAVNALL LNGRSFVDRV IEVSPSSDRV
VEAAAAILLP FPLQAKARQV RPGDWNCPNC SFHNFASRRH CFKCNAENPS HTSSAIATGG
APTGPAGASG AELMANTPNG TPSSNSGLPP PPPSSSSTLS SSTQPQAYTS TVAHHTPGSH
HQSTPFTSGD WICASATCGF LNYSSRAQCL KCGSYRPNNT GNVPPATPSS QNAGFTSHHQ
YHPPRPHHPA NFRPGDWFCS CGFQNFASRM SCLRCLAPNP ASTPSQPPTF GTAVGSSDGS
VASLGSYGYD NGAANASYGG NAYTSSYGTP PAGNTMAPGT GGHGFRIGDW YCPNCNSHNF
ASRFQCLKCH TTKPYTQAQS NPATTYSGAA TGGYRGPPPM KSGDWVCRNA VCGFHNFAKR
TYCGKCNTPN PDSSPYGATA DY
//
