ID A0A094CHX4_9PEZI Unreviewed; 1572 AA.
AC A0A094CHX4;
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:0000259|PROSITE:PS50089};
GN ORFNames=V493_06813 {ECO:0000313|EMBL:KFY22152.1};
OS Pseudogymnoascus sp. VKM F-4281 (FW-2241).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Leotiomycetes incertae sedis; Pseudeurotiaceae; Pseudogymnoascus.
OX NCBI_TaxID=1420906 {ECO:0000313|EMBL:KFY22152.1, ECO:0000313|Proteomes:UP000029327};
RN [1] {ECO:0000313|EMBL:KFY22152.1, ECO:0000313|Proteomes:UP000029327}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=VKM F-4281 (FW-2241) {ECO:0000313|Proteomes:UP000029327};
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 -!- 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:KFY22152.1}.
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DR EMBL; JPJV01002468; KFY22152.1; -; Genomic_DNA.
DR STRING; 1420906.A0A094CHX4; -.
DR HOGENOM; CLU_001287_1_1_1; -.
DR OrthoDB; 5491867at2759; -.
DR Proteomes; UP000029327; Unassembled WGS sequence.
DR GO; GO:0005768; C:endosome; IEA:UniProt.
DR GO; GO:0099023; C:vesicle tethering complex; IEA:UniProt.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006886; P:intracellular protein transport; IEA:UniProtKB-UniRule.
DR GO; GO:0016192; P:vesicle-mediated transport; IEA:InterPro.
DR CDD; cd16688; RING-H2_Vps11; 1.
DR CDD; cd03399; SPFH_flotillin; 1.
DR Gene3D; 3.30.479.30; Band 7 domain; 1.
DR Gene3D; 1.25.40.10; Tetratricopeptide repeat domain; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR001107; Band_7.
DR InterPro; IPR036013; Band_7/SPFH_dom_sf.
DR InterPro; IPR000547; Clathrin_H-chain/VPS_repeat.
DR InterPro; IPR011047; Quinoprotein_ADH-like_supfam.
DR InterPro; IPR011990; TPR-like_helical_dom_sf.
DR InterPro; IPR024763; VPS11_C.
DR InterPro; IPR011011; Znf_FYVE_PHD.
DR InterPro; IPR001965; Znf_PHD.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR23323; VACUOLAR PROTEIN SORTING-ASSOCIATED PROTEIN; 1.
DR PANTHER; PTHR23323:SF24; VACUOLAR PROTEIN SORTING-ASSOCIATED PROTEIN 11 HOMOLOG; 1.
DR Pfam; PF01145; Band_7; 1.
DR Pfam; PF00637; Clathrin; 1.
DR Pfam; PF12451; VPS11_C; 1.
DR SMART; SM00249; PHD; 1.
DR SMART; SM00184; RING; 1.
DR SUPFAM; SSF48371; ARM repeat; 1.
DR SUPFAM; SSF117892; Band 7/SPFH domain; 1.
DR SUPFAM; SSF57903; FYVE/PHD zinc finger; 1.
DR SUPFAM; SSF50998; Quinoprotein alcohol dehydrogenase-like; 1.
DR PROSITE; PS50236; CHCR; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 4: Predicted;
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000029327};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00175}.
FT DOMAIN 1478..1520
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
SQ SEQUENCE 1572 AA; 173754 MW; 300DAAAC9653294A CRC64;
MVFYTIAQPD EYLAITGAGV RTVKIAKKGF IWPMQKCMRF TIQPRDYPMN LRAMTKEKLQ
FELPVVFTVG PDLNQRGDNS IVHGEASAED REDRGDALMK YSMLLAGAAT TGGHAHIESI
VKGIIEGETR VLVSSMTMEE IFTEREQFKR RIYHNIQSEL DQFGLKIYNA NVKELTDAPN
SNYFASLSRK AHEGASNQAR VDVAEAQWHG NVGEAERQGR QNREIAKIHA ETAVQKTERD
TEKSQAEALL ATRKAAFDRD VNIAKIEASR AVEVKDEQLR KDVESLRAAT EIERLRASDV
VKATILRESQ QQASDARAYE TQTKASADFF LAQKAAEARA YETNTKTAAD ADREKQTAQA
KAFETQAKAD ADKFRVTRAA EATYLSESKK AEAEAYKLKV IAESSFHAEA KKADAEAYRV
KVAAEAAYIK TTRAAEAAKI AREAEAVGLT AMAGAYSAMS DAFGGPAGLV QYLMLEKGVY
GELARANAQA VQNLNPKLTV WNTGSQAGSG EGGEGGADAG ASIRNVYQML PPLMTTIKEQ
TGVELPEWQV GRLGGKEGPA KAESVVVNGA KGQAVTVAAN RITTLVALLP SPHQNSQHAN
TMALTSWKSF DFFEATQINP PDPDIFASSE ISAITSGSDS LFVASPDGHV RIFSRGFRIQ
KTWRAHDVGS ITHMRQVEGT ALLVTIAEDL PREPVLKVWA LDKLVKKTGL PTCTSLLSIQ
NGRKPFPISA FAALGDLSQL AVGFANGAVT VVRGDLIHDR GTRQKTVFES EEPVTGVEFR
DVARLTTLYV STTARLLKLV ISGQGQGQPA RTIEDAGCGV GCMTVDERNG DVVVVRDDAI
YYYGIDGRGP CFAYDGPKSL VQCHEEYLAI ITPPPTTSSA KSNTLRRFGG SQAEDLFNTS
TFTVLDTELQ IVAHSESMVS QIQTLLNVWG DLYALTLEGK ILRYHEKSLE QRLEIFYQRN
LFIYAINLAQ KSGMDAQQQN VIFRKYGEHL YQKGDYDGAM QQYLKAIDST EPSQVIRKYL
DSQRIHNLIE YLEELHEHHK ATADHTTLLL NCYAKLKDID KLEKFIKSPG DLKFDLDTAI
SMCRQGGYYD QAAYLATKHG EHEIVVDILI EDSKKYSEAL KYICRLDPDS AYPNLMKYAR
VLLENCPKDT TKVFIDYYTG KYHPVLEVVA TETPLPEAGY AQNAAQAVQG LANRIPVPFR
NAPAAATPAT QVDINPTIHD VINLGDNSST TTIPTYIPPR PRTAFSSFVD HSNDFITFLE
ACLAKTDVAE SDKVDLYTTL FEMYLHKANE DDGHDREEWE AKAKTLIENK DIPIDTSNVL
LLSHLADFKD GSILVREQAG LRFDIFRSYT SAKDTRGAIK ALRKYGPDEP ALYPAALAYF
TSDSRILKEA GSELDAVLKK IDDDGLMAPL QVIQTLSANS VATMGLIKPY LQKTIERERR
DIESNQRVIS SYRTETEAKR REIEELSTKP VVFQATRCAR CGSPLDPPMV HFLCKHSFHQ
LCLNVPNEAE GEKWECPTCR PGNDTIRAIV RAQTEMASKH DVFADALERS NDRFGTVSEF
FGRGVLGVPG AE
//
