ID A0A024TDR3_9STRA Unreviewed; 895 AA.
AC A0A024TDR3;
DT 09-JUL-2014, integrated into UniProtKB/TrEMBL.
DT 09-JUL-2014, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE RecName: Full=RING-type domain-containing protein {ECO:0000259|PROSITE:PS50089};
GN ORFNames=H310_13993 {ECO:0000313|EMBL:ETV91452.1};
OS Aphanomyces invadans.
OC Eukaryota; Sar; Stramenopiles; Oomycota; Saprolegniales; Saprolegniaceae;
OC Aphanomyces.
OX NCBI_TaxID=157072 {ECO:0000313|EMBL:ETV91452.1};
RN [1] {ECO:0000313|EMBL:ETV91452.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NJM9701 {ECO:0000313|EMBL:ETV91452.1};
RG The Broad Institute Genomics Platform;
RA Russ C., Tyler B., van West P., Dieguez-Uribeondo J., Young S.K., Zeng Q.,
RA Gargeya S., Fitzgerald M., Abouelleil A., Alvarado L., Chapman S.B.,
RA Gainer-Dewar J., Goldberg J., Griggs A., Gujja S., Hansen M., Howarth C.,
RA Imamovic A., Ireland A., Larimer J., McCowan C., Murphy C., Pearson M.,
RA Poon T.W., Priest M., Roberts A., Saif S., Shea T., Sykes S., Wortman J.,
RA Nusbaum C., Birren B.;
RT "The Genome Sequence of Aphanomyces invadans NJM9701.";
RL Submitted (DEC-2013) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; KI914010; ETV91452.1; -; Genomic_DNA.
DR RefSeq; XP_008879904.1; XM_008881682.1.
DR AlphaFoldDB; A0A024TDR3; -.
DR EnsemblFungi; H310_13993-t26_2; H310_13993-t26_2-p1; H310_13993.
DR EnsemblProtists; ETV91452; ETV91452; H310_13993.
DR GeneID; 20091043; -.
DR VEuPathDB; FungiDB:H310_13993; -.
DR OrthoDB; 54226at2759; -.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0140658; F:ATP-dependent chromatin remodeler activity; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR CDD; cd18793; SF2_C_SNF; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR Gene3D; 3.40.50.10810; Tandem AAA-ATPase domain; 1.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR038718; SNF2-like_sf.
DR InterPro; IPR049730; SNF2/RAD54-like_C.
DR InterPro; IPR000330; SNF2_N.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR017907; Znf_RING_CS.
DR PANTHER; PTHR45865:SF1; E3 UBIQUITIN-PROTEIN LIGASE SHPRH; 1.
DR PANTHER; PTHR45865; E3 UBIQUITIN-PROTEIN LIGASE SHPRH FAMILY MEMBER; 1.
DR Pfam; PF00176; SNF2-rel_dom; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR PROSITE; PS00518; ZF_RING_1; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00175}.
FT DOMAIN 674..716
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
SQ SEQUENCE 895 AA; 101451 MW; F62CFC7C8284FF84 CRC64;
MVASEAHANR QGDEACLHRM KDMATHFAQT TWSSSIFNAT TPINESHRIV IILMKDLAKE
WHRRQSELSE RGRSVSTLYH VSWSRICVDE VQEILGKSSL AAQMMQQLNA PIRWGLSGTP
VSKVADIAGV AQFLQLAPYD SSTWWLQHDI AVALELVQPI LDQIVWRTSS QHVSRSLQLP
SQTILPTTFV QLSAIEFAAY RPHFERYIKD IRRRIASFKG NTSLITLHEL RQLLHHPAVL
NLCKGASHVS LLTKCTTSID SSAGFIAHMA TRQREQCSLA LSQWLGVCLS CPKQLEIAYK
TWQDLATEIS VPWQVQLKVL SALSALHHVS PVRYRHQIHR AILDSPCQRR LPVTLWQRIF
VYLHEDFSDQ QLRVLIAQQH PLLAAFQDKA TAFWTAHAAP WSQHNFQSQV EASFDLERRI
QLPAMVAILN DFTNMRLSEA KSRVGIFERP TLWHYLRNKT TESIDVGEIR MVTMDLLGQY
MEQFSASLKL LHDVMHADWR RELQMVLRGY RDCNHATRRL DRTLVVGREE RWQRRDHAHG
QGRGQISLGS RCVVCTLRNR IDLALSFLVT EGKTLTLMVI FFTLEAPPEM LGLFNDCIAH
LEHMVSLATL LDNWLRVSCE AQNCMAYAGD DPSAAAFKRV KVAHEKFQLA NCYRQYTSTI
ASLDETASPA TNCCDFCGTA MTRSATSLLL CCHRFCAACI AKAASNEMAT HRCLVCFKSQ
PFALAKAPPL PPSLLACGSK MDVILQDLTA IAPHEKCVVF SQFPEVLELV MTELTKRHVR
SVQLRSGNQI SLRHAFETDT DVRVLLLPLK KYNHGLNLVE ATHVFLIEPS LQPALHAQAI
ARVKRLNQTR PTFVHRYAVR DTVEEAVDAA VTHDNHRLTK GDIYRIFAHD AFLST
//
