ID Q66HP7_RAT Unreviewed; 715 AA. AC Q66HP7; DT 11-OCT-2004, integrated into UniProtKB/TrEMBL. DT 11-OCT-2004, sequence version 1. DT 27-MAR-2024, entry version 128. DE SubName: Full=YME1-like 1 (S. cerevisiae) {ECO:0000313|EMBL:AAH81751.1}; GN Name=Yme1l1 {ECO:0000313|EMBL:AAH81751.1, ECO:0000313|RGD:620764}; OS Rattus norvegicus (Rat). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae; OC Murinae; Rattus. OX NCBI_TaxID=10116 {ECO:0000313|EMBL:AAH81751.1}; RN [1] {ECO:0000313|EMBL:AAH81751.1} RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Kidney {ECO:0000313|EMBL:AAH81751.1}; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RA Gerhard D.S., Wagner L., Feingold E.A., Shenmen C.M., Grouse L.H., RA Schuler G., Klein S.L., Old S., Rasooly R., Good P., Guyer M., Peck A.M., RA Derge J.G., Lipman D., Collins F.S., Jang W., Sherry S., Feolo M., RA Misquitta L., Lee E., Rotmistrovsky K., Greenhut S.F., Schaefer C.F., RA Buetow K., Bonner T.I., Haussler D., Kent J., Kiekhaus M., Furey T., RA Brent M., Prange C., Schreiber K., Shapiro N., Bhat N.K., Hopkins R.F., RA Hsie F., Driscoll T., Soares M.B., Casavant T.L., Scheetz T.E., RA Brown-stein M.J., Usdin T.B., Toshiyuki S., Carninci P., Piao Y., RA Dudekula D.B., Ko M.S., Kawakami K., Suzuki Y., Sugano S., Gruber C.E., RA Smith M.R., Simmons B., Moore T., Waterman R., Johnson S.L., Ruan Y., RA Wei C.L., Mathavan S., Gunaratne P.H., Wu J., Garcia A.M., Hulyk S.W., RA Fuh E., Yuan Y., Sneed A., Kowis C., Hodgson A., Muzny D.M., McPherson J., RA Gibbs R.A., Fahey J., Helton E., Ketteman M., Madan A., Rodrigues S., RA Sanchez A., Whiting M., Madari A., Young A.C., Wetherby K.D., Granite S.J., RA Kwong P.N., Brinkley C.P., Pearson R.L., Bouffard G.G., Blakesly R.W., RA Green E.D., Dickson M.C., Rodriguez A.C., Grimwood J., Schmutz J., RA Myers R.M., Butterfield Y.S., Griffith M., Griffith O.L., Krzywinski M.I., RA Liao N., Morin R., Morrin R., Palmquist D., Petrescu A.S., Skalska U., RA Smailus D.E., Stott J.M., Schnerch A., Schein J.E., Jones S.J., Holt R.A., RA Baross A., Marra M.A., Clifton S., Makowski K.A., Bosak S., Malek J.; RT "The status, quality, and expansion of the NIH full-length cDNA project: RT the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|ARBA:ARBA00001947}; CC -!- SIMILARITY: In the C-terminal section; belongs to the peptidase M41 CC family. {ECO:0000256|ARBA:ARBA00010044}. CC -!- SIMILARITY: In the N-terminal section; belongs to the AAA ATPase CC family. {ECO:0000256|ARBA:ARBA00010550}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; BC081751; AAH81751.1; -; mRNA. DR RefSeq; NP_446134.2; NM_053682.2. DR AlphaFoldDB; Q66HP7; -. DR MEROPS; M41.026; -. DR GeneID; 114217; -. DR KEGG; rno:114217; -. DR CTD; 10730; -. DR RGD; 620764; Yme1l1. DR OrthoDB; 9585at2759; -. DR GO; GO:0005743; C:mitochondrial inner membrane; IEA:UniProtKB-KW. DR GO; GO:0005524; F:ATP binding; IEA:InterPro. DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro. DR GO; GO:0004176; F:ATP-dependent peptidase activity; IEA:InterPro. DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro. DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW. DR CDD; cd19501; RecA-like_FtsH; 1. DR Gene3D; 1.10.8.60; -; 1. DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1. DR Gene3D; 1.20.58.760; Peptidase M41; 1. DR HAMAP; MF_01458; FtsH; 1. DR InterPro; IPR003593; AAA+_ATPase. DR InterPro; IPR041569; AAA_lid_3. DR InterPro; IPR003959; ATPase_AAA_core. DR InterPro; IPR003960; ATPase_AAA_CS. DR InterPro; IPR005936; FtsH. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR000642; Peptidase_M41. DR InterPro; IPR037219; Peptidase_M41-like. DR NCBIfam; TIGR01241; FtsH_fam; 1. DR PANTHER; PTHR23076:SF37; ATP-DEPENDENT ZINC METALLOPROTEASE YME1L1; 1. DR PANTHER; PTHR23076; METALLOPROTEASE M41 FTSH; 1. DR Pfam; PF00004; AAA; 1. DR Pfam; PF17862; AAA_lid_3; 1. DR Pfam; PF01434; Peptidase_M41; 1. DR SMART; SM00382; AAA; 1. DR SUPFAM; SSF140990; FtsH protease domain-like; 1. DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1. DR PROSITE; PS00674; AAA; 1. DR Genevisible; Q66HP7; RN. PE 2: Evidence at transcript level; KW Hydrolase {ECO:0000256|ARBA:ARBA00022801}; KW Membrane {ECO:0000256|ARBA:ARBA00022792}; KW Metalloprotease {ECO:0000256|ARBA:ARBA00023049}; KW Mitochondrion {ECO:0000256|ARBA:ARBA00023128}; KW Mitochondrion inner membrane {ECO:0000256|ARBA:ARBA00022792}; KW Protease {ECO:0000256|ARBA:ARBA00022670}. FT DOMAIN 313..450 FT /note="AAA+ ATPase" FT /evidence="ECO:0000259|SMART:SM00382" FT REGION 31..54 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" SQ SEQUENCE 715 AA; 79812 MW; 4140E6183783C9CD CRC64; MFSLSSTVQP QVTVPLSHLI NAFHSPKNIS VSVNTSASPK QHRDTVAEHE APSSEPVLNL RDLGLSELKI GQTDKLVENL LPGFYKDKRV SSCWHTSHIS AQSFFENKYG HLDMFSTLRS SSLYRQHPKT LQSICSDLQN FPVFIQSRGF KTLKSRTRRL QSTSERLAEA QNIAPSFVKG FLLRDRGTDL ESLDKLMKTK NIPEVHQDAF KTGFAEGFLK AQALTQKTND SLRRTRLILF VLLLFGIYGL LKNPFLSVRF RTTTGLDSAV DPVQMKNVTF EHVKGVEEAK QELQEVVEFL KNPQKFTVLG GKLPKGILLV GPPGTGKTLL ARAVAGEADV PFYYASGSEF DEMFVGVGAS RIRNLFREAK ANAPCVIFID ELDSVGGKRI ESPMHPYSRQ TINQLLAEMD GFKPNEGVII IGATNFPEAL DNALIRPGRF DMQVTVPRPD VKGRTEILKW YLNKIKFDKS VDPEIIARGT VGFSGAELEN LVNQAALKAA VDGKEMVTMK ELEFSKDKIL MGPERRSVEI DNKNKTITAY HESGHAIIAY YTKDAMPINK ATIMPRGPTL GHVSLLPEND RWNETRAQLL AQMDVSMGGR VAEELIFGTD HITTGASSDF DNATKIAKRM VTKFGMSEKL GVMTYSDTGK LSPETQSAIE QEIRILLRES YERAKHILKT HAKEHKNLAE ALLTYETLDA KEIQIVLEGK KLEVR //