ID A0A094EYQ0_9PEZI Unreviewed; 1298 AA.
AC A0A094EYQ0;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 44.
DE RecName: Full=RING-type domain-containing protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=V499_03683 {ECO:0000313|EMBL:KFY76770.1};
OS Pseudogymnoascus sp. VKM F-103.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Leotiomycetes incertae sedis; Pseudeurotiaceae; Pseudogymnoascus.
OX NCBI_TaxID=1420912 {ECO:0000313|EMBL:KFY76770.1, ECO:0000313|Proteomes:UP000029295};
RN [1] {ECO:0000313|EMBL:KFY76770.1, ECO:0000313|Proteomes:UP000029295}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=VKM F-103 {ECO:0000313|EMBL:KFY76770.1,
RC ECO:0000313|Proteomes:UP000029295};
RA Leushkin E.V., Logacheva M.D., Penin A.A., Sutormin R.A., Gerasimov E.S.,
RA Kochkina G.A., Ivanushkina N.E., Vasilenko O.V., Kondrashov A.S.,
RA Ozerskaya S.M.;
RT "Population genomics of a fungus Geomyces pannorum provides evidence of
RT horizontal gene transfer but not of sexual reproduction.";
RL Submitted (JUL-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000256|ARBA:ARBA00004477}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004477}. Membrane
CC {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: Belongs to the EBP family. {ECO:0000256|ARBA:ARBA00008337}.
CC -!- SIMILARITY: Belongs to the SH3RF family.
CC {ECO:0000256|ARBA:ARBA00008649}.
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:KFY76770.1}.
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DR EMBL; JPKB01000558; KFY76770.1; -; Genomic_DNA.
DR HOGENOM; CLU_005224_1_0_1; -.
DR Proteomes; UP000029295; Unassembled WGS sequence.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0047750; F:cholestenol delta-isomerase activity; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016125; P:sterol metabolic process; IEA:InterPro.
DR CDD; cd02249; ZZ; 1.
DR Gene3D; 3.30.60.90; -; 1.
DR Gene3D; 2.30.30.40; SH3 Domains; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR007905; EBP.
DR InterPro; IPR033118; EXPERA.
DR InterPro; IPR036028; SH3-like_dom_sf.
DR InterPro; IPR001452; SH3_domain.
DR InterPro; IPR018957; Znf_C3HC4_RING-type.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR InterPro; IPR017907; Znf_RING_CS.
DR InterPro; IPR043145; Znf_ZZ_sf.
DR PANTHER; PTHR14207:SF1; EMOPAMIL-BINDING PROTEIN-LIKE; 1.
DR PANTHER; PTHR14207; STEROL ISOMERASE; 1.
DR Pfam; PF05241; EBP; 1.
DR Pfam; PF00097; zf-C3HC4; 1.
DR SMART; SM00184; RING; 1.
DR SMART; SM00326; SH3; 1.
DR SUPFAM; SSF57850; RING/U-box; 3.
DR SUPFAM; SSF50044; SH3-domain; 1.
DR PROSITE; PS51751; EXPERA; 1.
DR PROSITE; PS50002; SH3; 1.
DR PROSITE; PS00518; ZF_RING_1; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 3: Inferred from homology;
KW Endoplasmic reticulum {ECO:0000256|ARBA:ARBA00022824};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|PROSITE-
KW ProRule:PRU01087}; Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW SH3 domain {ECO:0000256|ARBA:ARBA00022443, ECO:0000256|PROSITE-
KW ProRule:PRU00192};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|PROSITE-
KW ProRule:PRU01087};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989, ECO:0000256|PROSITE-
KW ProRule:PRU01087}; Ubl conjugation {ECO:0000256|ARBA:ARBA00022843};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00175}.
FT TRANSMEM 20..40
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 47..65
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 130..152
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 159..178
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 198..220
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 47..216
FT /note="EXPERA"
FT /evidence="ECO:0000259|PROSITE:PS51751"
FT DOMAIN 306..362
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT DOMAIN 1234..1296
FT /note="SH3"
FT /evidence="ECO:0000259|PROSITE:PS50002"
FT REGION 388..586
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 624..862
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 388..429
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 444..466
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 467..481
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 482..514
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 527..562
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 563..578
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 624..654
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 677..703
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 720..783
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 840..862
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1298 AA; 144050 MW; 9D86079F153781EC CRC64;
MSSQPPTTIA ELLADRTTVL SFSLVLALIV SAYVLSLATL RRGTSGALRF LFIWHAFDAL
IHFIFEGSFL YNALFTYVSL PSFASAAPNW LGYTDRLYGS NFGGPENHLA ALWRVYAQAD
SRWGGADATV VSIELLTVLL AGPVAAYVAI LIARGDARAS IWMIALAVAE LYGGFMTFAP
EWLTGSPSLD TSNWIFTWVY LFFFNTLWVW IPMYAIYVSY KDICNAFNVR TEVIVASEEK
LKKEESTTIR IRAAKWRLMA MSPTSTRISF YLHKVEAATS TSSEDSDTIT MEAANQGLDL
ERELTCSICT EVLYQPLTLL DCLHTFCGAC LKEWFAFQLN SARASGASSS SSSNPVTCPS
CRAVVRATKN NATVTTLLEM FLAANPDKGR TAEEKEDVKK KYSPGDDVMP KSEEREKTMR
ERMAEDDDGR LIQQVQMASL REVGVELPEE RRERRRRREE RARASGRTSS RTASREPSSD
PAGSGQDRDR RRAEEDSGSE SRRRREERRE ERASASASSP TTLHPESTRA LERRRRRSEE
AAARRSQDDS RRRNDDANRT AVRQIEHQSS LRSLISSSDV DSREMEEEIL RQIREEGLLD
GIDLENIDVN QEDQISERIA EAFRRRQRER AEQVVAPEPR NRSPSDRSEH RSATSSRTRQ
STTTAPPMAT ARRLPHSRSL SAASQADEAT RASPRTSATR LEPQSSDEGR RRRRTASGGH
RSTRSATSPA PSSSPVTRPA ARSATDLTER STSSHIAPTR PLMSVETRST TEPVPTSSNV
ADVVELATGR RRPPTLPPRS QLAGEAEIAA SPVELQSSHT RTASQAPAYP PPPVPVATTP
QDSQPGLSPA AALSHHSTAT ERASALQAVS RPTSSESTAS QRVSLPRFPE PSIQCNRCHK
SHIEYELHYS CSICARGEWN LCLGCYRSGR GCEHWFGFGY AAWAKWEKAR TAGHIPPNAE
KPHMLFAERY LPPRITPGGA EGRRTLTTED PARRLQSGAF CASCQEWANE CYWRCDSCNE
GDWGFCNNCV NQGRCCTHPL LPLLYKPDNR DGEPMSPTHD HQTPRTATLL TGPGVVELGS
FKPLSFRVEC DACHYPIQPT QTRFHCFQCT SALPGREAGD YDLCTTCYHS MVNKKRISNE
NGHQGWRRCL QGHRMVIVGF EDARGGQRRV VVQDRVGGRG LFEEPAKTQD AVDAGLQQWS
WAEGTRARLV TNNVSSTAPT GNPAMAREFP PDGGVGMRAV ALWSWYPKEG EGANELLFPR
GAEVREVVDV NGDWFHGSFM GAKGLFPAPY VRVLDSAS
//
