ID A0A094GIX4_9PEZI Unreviewed; 1292 AA.
AC A0A094GIX4;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 08-NOV-2023, entry version 45.
DE RecName: Full=SH3 domain-containing protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=V498_02939 {ECO:0000313|EMBL:KFY96050.1};
OS Pseudogymnoascus sp. VKM F-4517 (FW-2822).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Leotiomycetes incertae sedis; Pseudeurotiaceae; Pseudogymnoascus.
OX NCBI_TaxID=1420911 {ECO:0000313|EMBL:KFY96050.1, ECO:0000313|Proteomes:UP000029270};
RN [1] {ECO:0000313|EMBL:KFY96050.1, ECO:0000313|Proteomes:UP000029270}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=VKM F-4517 (FW-2822) {ECO:0000313|Proteomes:UP000029270};
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:KFY96050.1}.
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DR EMBL; JPKA01000486; KFY96050.1; -; Genomic_DNA.
DR HOGENOM; CLU_005224_1_0_1; -.
DR Proteomes; UP000029270; 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:0009966; P:regulation of signal transduction; IEA:UniProt.
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; SM00326; SH3; 1.
DR SUPFAM; SSF57850; RING/U-box; 2.
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 52..71
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 305..361
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT DOMAIN 1228..1290
FT /note="SH3"
FT /evidence="ECO:0000259|PROSITE:PS50002"
FT REGION 388..411
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 441..774
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 779..798
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 806..838
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1041..1060
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 443..465
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 481..509
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 522..556
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 557..572
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 573..595
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 605..648
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 649..664
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 671..694
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 695..713
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 714..774
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1292 AA; 143615 MW; CBF85134739CD317 CRC64;
MSSQPPTTIA DLLSDRTTVL SFSLVLALIV SAYVLSLATL RRGTSSPLRF LFIWHAFDAL
IHFIFEGSYL YNALFTYVSL PSFASAAPNW LGYTDRLYGS NFGGPENHLA ALWRVYAQAD
SRWGGADATV VSIELLTVLL AGPVAAYIAV LIARGDARAS IWMVALAVAE LYGGFMTFAP
EWLTGSQSLD TSNWVFTWVY LFFFNTLWVW IPIYAIYVSY KDISNAFDVR TEVIVASEEK
QKKEESKKSR ANGERSPISA MLQLLFKAKL NNNSYTRRPV AAYGYERLEH LVSAPTFTKL
KSLRICTEVL YQPLTLLDCL HTFCGACLKE WFAFQLNSAR ASGASSSSSS SSSPVTCPSC
RAVVRATKNN ATVTTLLEMF LAANPDKGRT VEEKEEVKKK YTPGDDVMPK AEEREKTLRE
RMADDDDGRL IQQVQMASLR EVGVELPEER RERRRRREER ARASGRTSSR TASRDASNDP
AGSGPERERR RAEDDSGSES RRRREERAAA SASSPTTLHP ESTRALERRR RRSEEAARRS
QDESRRRNDD ANRTAVRQIE HQSSLRSLIS SSDVDSREME EEILRQIREE GLLDGIDLEN
IDVNQEDQIS ERIAEAFRRR QRERAEQVDV PEPRNRSPSD RSEHRSGTSS RTRQSTTTQP
PMATARRLPH SRSLSAASQA DEATRASPRT SATRLEPHSS DEGRRRRRTA SGGDRSTRSA
TSPAPSSSPV TRPAARSATD LTERSTSSHI FPTRPLMSVD TRSTTEPVPT SSTVADVVEL
ATSRRRPPTL PPRSQVAGEA EIAASPVELQ SSHSRTASQA PAYPPPPVPA VATQQDSQPG
LIPAATLSHH STATERAGAL QAVSRPTSSE STASQRVSLP RFPEPSIQCN RCHKQHIEYE
LHYSCTICAR GEWNVCLGCY RSGRGCEHWF GFGYAAWAKW EKARVAGHIP LNAEKPHMLF
AERYLPPRIT PGGAEGRRTL TTEDPARRLQ SGAFCANCLE WANECYWRCD SCNEGDWGFC
NNCVNQGRCC THTLLPLLHK PDNRDAEPMS PSHDHQTPRS ATLLTGPGVV ELGSFKPLSF
RVECDACHYP IQPTQTRFHC FQCTSALPGR EAGDYDLCTT CYHSMVNKKR ISNENGHLGW
RRCLQGHRMI IVGFEDARGG QRRVVVQDRV GGRGLFEEPA KTQDAVDAGL QQWSWAEGTR
ARLVANNVAS TAPTGNPAMT REFPPDGGVG MRAVALWSWY PKEGEGANEL LFPRGAEVRE
VVDVNGDWFH GSFMGTKGLF PAPYVRVLDS AS
//