ID A0A1R1X9M1_9FUNG Unreviewed; 1804 AA.
AC A0A1R1X9M1;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE SubName: Full=Ankyrin repeat domain-containing protein 6 {ECO:0000313|EMBL:OMJ11312.1};
GN ORFNames=AYI70_g9802 {ECO:0000313|EMBL:OMJ11312.1};
OS Smittium culicis.
OC Eukaryota; Fungi; Fungi incertae sedis; Zoopagomycota; Kickxellomycotina;
OC Harpellomycetes; Harpellales; Legeriomycetaceae; Smittium.
OX NCBI_TaxID=133412 {ECO:0000313|EMBL:OMJ11312.1, ECO:0000313|Proteomes:UP000187283};
RN [1] {ECO:0000313|EMBL:OMJ11312.1, ECO:0000313|Proteomes:UP000187283}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=GSMNP {ECO:0000313|EMBL:OMJ11312.1,
RC ECO:0000313|Proteomes:UP000187283};
RA Mah S.A., Swanson W.J., Moy G.W., Vacquier V.D.;
RL Submitted (JAN-2017) 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:OMJ11312.1}.
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DR EMBL; LSSN01004558; OMJ11312.1; -; Genomic_DNA.
DR STRING; 133412.A0A1R1X9M1; -.
DR Proteomes; UP000187283; Unassembled WGS sequence.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR CDD; cd16489; mRING-CH-C4HC2H_ZNRF; 1.
DR Gene3D; 1.25.40.20; Ankyrin repeat-containing domain; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 2.
DR InterPro; IPR002110; Ankyrin_rpt.
DR InterPro; IPR036770; Ankyrin_rpt-contain_sf.
DR InterPro; IPR000306; Znf_FYVE.
DR InterPro; IPR017455; Znf_FYVE-rel.
DR InterPro; IPR011011; Znf_FYVE_PHD.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR24166:SF48; ANKYRIN REPEAT DOMAIN 29; 1.
DR PANTHER; PTHR24166; ROLLING PEBBLES, ISOFORM B; 1.
DR Pfam; PF12796; Ank_2; 1.
DR Pfam; PF01363; FYVE; 1.
DR Pfam; PF13639; zf-RING_2; 1.
DR SMART; SM00248; ANK; 4.
DR SMART; SM00064; FYVE; 1.
DR SUPFAM; SSF48403; Ankyrin repeat; 1.
DR SUPFAM; SSF57903; FYVE/PHD zinc finger; 1.
DR SUPFAM; SSF57850; RING/U-box; 1.
DR PROSITE; PS50297; ANK_REP_REGION; 2.
DR PROSITE; PS50088; ANK_REPEAT; 3.
DR PROSITE; PS50178; ZF_FYVE; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 4: Predicted;
KW ANK repeat {ECO:0000256|ARBA:ARBA00023043, ECO:0000256|PROSITE-
KW ProRule:PRU00023}; Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000187283};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00175}.
FT REPEAT 185..217
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 218..250
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 251..271
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT DOMAIN 862..899
FT /note="FYVE-type"
FT /evidence="ECO:0000259|PROSITE:PS50178"
FT DOMAIN 1762..1802
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT REGION 595..641
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 744..816
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1338..1358
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1390..1410
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1527..1561
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1593..1653
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1341..1358
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1527..1552
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1597..1632
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1633..1653
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1804 AA; 200675 MW; AAED402188A0B06F CRC64;
MSLNATKKAI SEDFLHFYDD GISLERNSTT TSLQKDHISE LQIEESVRLA QSLLNDSHFD
LNFPDFVAPL TPNSTHPYYG DVKKKYDPLN LYLYEHDQIQ SFDLPYSTPL KMPSIANTIP
IISKNISETS SNISLQGYPK FSEIQSKFLI AVETGSTSVV KKMILIAKEN FNNADKLISF
QSGINKVTPL MLATTKGHAR VVSELLIAGA PVDSLDSENE SALLKASYLG NLEIVSVLLK
HHANPSFSDK DGWTSLHNAA SFGHLDIVKL LAKNKNVDIS AQSLQGHTPL SHTKVADFLL
KTGKAKVVLK NKFGENAYDI AAAGMFVDLC FLIEEAERLN WLKKQATSMV KEPWDPLKAH
TSHLIVIHEN ERSKGHFSKV LDEDITNHLS SVSAAFYHPI SVFLGFKSNN NTTSEENNTI
NSESKLSRIR YPKDFSAFNL ISGIDPPRWS NIIGEPCTPD QVTLPHLEES ESSSNSWFWL
TDWCLLSKSQ YTRSPGIENN VSNNNEGWKY CKSGFNYANG NWKDSLDEIY LNDFDDMSLD
ISCVRRRKWV RIMRRQIDLS SFEHHKTKSL NNNNQDSPLN EFKRKSFESI PAANTHLYNP
SQSHTPGSPS YEYPSSNLDK SSSSEFKSAL DNSSDSSFSS NYSDVNDKNI NIYHFDNQSS
QEPILSSTKI SINSPIKDAH IDDVPNSVEN SSNVIISRNV KNTKQSNPNR LIEDISANDQ
MLNEELDDSV SAIGSNASDI SKLSNKSRVY EHNSSNNPIE AQKPTSSTEK VSKPRNLLSG
DNVSANSSSV KFSMSVDSPQ LPNNSLSEYS DSNSRSNKNL SFKQILAQDL KHIEYKFKEA
TRSLSSSIYI RQYMPEQAWQ PDSSAPSCIN CDRKFKLFFR RHHCRRCGLV FCDICSRDRE
WLASRLYSLE NFGSDSSIPL ISSSKSINGV LFIDEITKSL ISLLELPNGH ENIATNQNSP
ILDNISLDIN TEMLQKIFNS SSNENKPQSL YLIQQHRVCI PCKRAINRVD GSTKNRDVND
IPDVLKRLFG LLAAMKPNEQ LDRIDYNILN NDVLNATIIK PNSDENNSGN LNEVLEKEFN
SLLNLNGIVM EVPLSHTEDA ALMLVKMNLP ALLEHSVPEI NWFQDALNIY TQLASSIQDS
SDISKHNLTN DLLSLSNLKI ENIQSIDHNS KLKSTDKNID SSNAISIKKL KSDNINHINF
TNNNSSGSPI QPNVAYDYWY ATNNDITSSS PIPDAPGNSA GLYLNESYGL LDKFYREMNK
VLIQSVIKIG CSDESSIHKT SKKFKLSEFS VECPVCNKLW TDVLDSIGRS PGEGWQEIQE
RHISECLVDM QLELGGTAKE GSAENENSSD IVPSSNVAMN ISNNSNQALS ANDSNPSSSR
PVLGLLDMLN ESSKTGSSSG KGKLVSTNTS SFNSNTNDFA KDRLISLTRK ISDNEHASNI
ISEDILSINH HGFDDSKDMN SVAGKAMSLP KDLGDKQNPN SMFPIWESEE RNDNNDPIII
ENSFLGSSQS ISNDNIGIVQ NSSMRPSDIN IGNSKRKNTL PSNISKSYTP SEMIGDDVSG
KRRDNYEEKN LKSITFNLFN QIGNLAGVIG LIPPSETEKK PNHESRSEND FDTALPDLGK
KYYKKHEGSS ASKNRYMDNS GAQPASSSSN RIDTGENTYG FFNKLVFQKI GISRDNTEHS
SNELSYQSGE ITNAYASAGS SIYSANFRSA ENLQFGSRAG AVTGAGSSSS DALNRKKSKS
KSKVRFVSYK LSEDSPLLNQ ECSICFDEFE CGDSVARLSC FCTFHSGCIK EWFKRNPNCP
VHGI
//
