Mitochondrial ATP-dependent zinc metallopeptidase, putative [Q4Q1E9] | |
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Systematic Name | LmjF.36.2710 [Leishmania major] |
Gene Name | LMJF_36_2710 |
Molecular Weight | 62188 Da |
Protein Sequence Size | 571 |
Function | |
Charge | -6.5 |
Isoelectric Point | 5.4 pH |
Description | Mitochondrial ATP-dependent zinc metallopeptidase, putative (Metallo-peptidase, clan ma(E), family m41). |
Subcellular Location | membrane; Mitochondrion[Predict] |
E. C. Number | N.A. |
Sequence | >tr|Q4Q1E9|Q4Q1E9_LEIMA Mitochondrial ATP-dependent zinc metallopeptidase, putative (Metallo- peptidase, clan ma(E), family m41) - Leishmania major. SYGQPQQQPLPSDLGTKERPIVVVSAPQKASWATRFWMFLLFGIALSCFISLVEEFNDRF QEGQPANKSGFARSGISGLFGSVDVKPVNLDNLEVTFDSIRGCDEAKKELEEIVEFLKDP EKFYNLGGRLPKGALLTGPPGCGKTMLAKAIAKEAGVSFFYATGSEFDEMFVGVGARRVR ELFAAAKANSPALIFIDEVDALGGRRSRSDHSTSRMTLNQLLAEMDGFDSDEAVIVLAAT NTPETLDKALTRPGRLDTTITVDPPDMKGRAEVAQVYLDKIKTDSTVNAMDIARGTTGFT GAELSNLVNLAAIRAAVLNKAKVTSEEIEYAKDRVMMGAESKKIVPEEERRVTAFHEGGH ALSAILLKDEGADPVHKATIVPRGNGIMGLVQQQPDRDKYSQSKRQCLARLKVCVAGRVG EEILLGPDDITTGAGSDFQQATNMARHMVRQFGFSDAMGFVDYGTPDTAEGAYISDETKL KIEKEVHRLVEQAYIETKELLLSHRAELENIANNLLKYETLSGKDLEKIIKGEAIPERPP RLSQAAESKAAPPRGGNSDQANGRRTVPIS |
DNA Sequence | >LmjF36.2710 |||mitochondrial ATP-dependent zinc metallopeptidase, putative|Leishmania major|chr 36|||Manual ATGTCGTATG GGCAGCCACA ACAGCAGCCA CTCCCAAGTG ATCTGGGGAC CAAGGAAAGACCGATTGTGG TCGTGTCAGC ACCGCAGAAG GCTTCCTGGG CCACCCGCTT CTGGATGTTCTTGCTCTTCG GGATTGCTCT TAGCTGCTTC ATCAGCCTGG TCGAGGAGTT CAACGATCGCTTTCAGGAGG GCCAGCCCGC AAACAAGTCA GGATTTGCGC GCTCTGGCAT ATCTGGCCTGTTCGGCTCTG TCGACGTGAA GCCGGTGAAT CTGGACAACT TGGAGGTCAC ATTTGACAGCATCCGCGGAT GCGATGAGGC GAAAAAAGAG CTGGAGGAGA TTGTTGAGTT TCTAAAGGACCCCGAGAAGT TCTACAATTT GGGTGGGCGG CTGCCAAAAG GAGCGCTGCT CACCGGTCCGCCAGGGTGCG GGAAAACCAT GCTGGCAAAG GCGATTGCCA AAGAGGCTGG CGTGAGCTTTTTCTACGCCA CCGGAAGCGA GTTCGATGAG ATGTTTGTTG GCGTTGGCGC CCGCCGCGTTCGCGAACTTT TCGCGGCCGC AAAGGCCAAC TCACCAGCTT TGATTTTCAT CGACGAGGTAGACGCATTAG GCGGTCGCCG CTCTCGTTCT GACCACAGCA CCTCTCGCAT GACGTTGAACCAGCTCCTGG CAGAGATGGA CGGCTTCGAC TCCGATGAGG CCGTTATTGT CCTCGCCGCCACGAACACCC CTGAAACGCT GGACAAGGCA CTCACGCGCC CCGGTCGCCT GGACACCACCATCACCGTTG ACCCTCCGGA TATGAAAGGG CGCGCGGAGG TAGCTCAGGT GTACCTTGACAAAATCAAGA CAGACAGCAC GGTCAATGCA ATGGATATCG CACGCGGAAC AACTGGTTTCACAGGTGCCG AGCTTAGCAA CTTGGTGAAT CTGGCAGCCA TCAGGGCCGC GGTGCTGAACAAGGCGAAAG TGACCAGCGA AGAGATAGAG TACGCTAAGG ACCGCGTCAT GATGGGTGCCGAGAGCAAGA AGATTGTGCC GGAGGAGGAG CGTCGCGTGA CTGCGTTCCA CGAGGGCGGCCACGCTTTGA GCGCTATCTT GCTGAAGGAT GAGGGTGCCG ATCCTGTCCA CAAGGCAACCATTGTTCCCC GCGGCAACGG CATTATGGGA CTCGTCCAGC AACAGCCGGA CAGGGATAAGTACAGTCAAA GCAAGCGCCA GTGCCTGGCT CGCCTGAAGG TGTGTGTGGC GGGACGAGTCGGCGAAGAGA TTCTTTTAGG CCCTGACGAT ATTACCACCG GCGCAGGCTC CGATTTTCAGCAGGCCACCA ACATGGCCCG CCACATGGTG CGACAGTTCG GGTTCAGCGA CGCTATGGGCTTCGTAGACT ATGGTACACC CGACACCGCC GAAGGCGCCT ACATTTCAGA TGAGACGAAGCTCAAGATCG AAAAAGAGGT ACATCGCCTC GTTGAGCAGG CCTACATCGA GACCAAGGAGCTTCTTCTGA GCCACCGCGC CGAGTTGGAG AATATCGCCA ACAACCTGCT CAAGTATGAAACGCTCAGTG GCAAGGATCT TGAGAAGATT ATAAAGGGCG AGGCTATCCC AGAGCGTCCTCCGCGCCTGT CACAGGCTGC AGAGAGCAAG GCCGCGCCGC CACGAGGCGG GAACAGCGACCAGGCAAACG GTCGGAGAAC TGTTCCAATC TCATAG |
Mitochondrial ATP-dependent zinc metallopeptidase, putative Q4Q1E9] | |
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Metabolite Information | cell cycle; protein catabolism; proteolysis |
Molecular Function | |
Biochemical Pathway | |
Regulatory Pathway | |
KEGG Pathways | K03798 |
Orthologs | ||||
Homologs | GI | Percent Identity | Evalue | Score |
Homo sapiens | YME1-like 1 isoform 1 [Homo sapiens] | 50 | 1e-126 | 451 |
DEG Information | ||||
DEG Protein | DEG Organism | Percent Identity | Evalue | Bit Score |
hflB ATP-dependent zinc-metallo protease | Salmonella typhimurium | 42% | 1e-110 | 394 |
Post Translational Modification | ||||
PTM Type | PTM Sub Type | Score | Modification Site | Prosite ID |
PDOC00572 | AAA-protein family signature | 235-253; | PS00674 | |
PDOC00017 | ATP/GTP-binding site motif A (P-loop) | 139-146; | PS00017 | |
PDOC00595 | Formate--tetrahydrofolate ligase signatures | 68-71; | PS00722 | |
Acylation | N-myristoylation site | 44-49; 64-69; 79-84; 103-108; 134-139; 142-147; 204-209; 302-307; 465-470; 472-477; | PS00008 | |
Amidation | Amidation site | 204-207; 563-566; | PS00009 | |
Glycosylation | N-glycosylation site | 68-71; | PS00001 | |
Phosphorylation | cAMP- and cGMP-dependent protein kinase phosphorylation site | 351-354; | PS00004 | |
Phosphorylation | Casein kinase II phosphorylation site | 52-55; 164-167; 166-169; 208-211; 301-304; 325-328; 523-526; | PS00006 | |
Phosphorylation | Protein kinase C phosphorylation site | 100-102; 214-216; 342-344; 404-406; 504-506; 523-525; | PS00005 | |
Phosphorylation | Tyrosine kinase phosphorylation site | 119-125; 323-331; 489-495; | PS00007 |
Mitochondrial ATP-dependent zinc metallopeptidase, putative [Q4Q1E9] | ||
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Model Information | ||
Template PDB ID | 2dhrF | |
Percent Identity | 45% | |
Target Region | 93-541 | |
Template Region | 150-443 |
Domain Information | ||
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Domains | Start | End |
Active Site Information | ||
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Residue | Active Site Number | Functional Part |
Co-Factor | |
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Metal | Description |
Ligands | |||||
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CAS number | Name | Mol. Weight | Mol. Formula | Smile Notation | PDB Reference |
58-64-0 | ADENOSINE-5'-DIPHOSPHATE | 427.201 | C10 H15 N5 O10 P2 | O=P(O)(O)OP(=O)(O)OCC3OC(n2cnc1c(ncnc12)N)C(O)C3O | 2dhr |
Mutational Information | ||
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Residue | Feature | Description |
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Modeled Protein | Template Structure |
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+----------<<< P R O C H E C K S U M = M A R Y >>>----------+ | = | | /var/www/html/Services/SAVES_3/jobs/800610/Q4Q1E9.pdb 2.0 448 = residues | | = | *| Ramachandran plot: 88.0% core 9.7% allow 1.8% gener 0.5% = disall | | = | *| All Ramachandrans: 22 labelled residues (out of 446) = | +| Chi1-chi2 plots: 1 labelled residues (out of 263) = | | = | | Main-chain params: 6 better 0 inside 0 worse = | | Side-chain params: 5 better 0 inside 0 worse = | | = | *| Residue properties: Max.deviation: 4.0 Bad contacts: = 12 | *| Bond len/angle: 5.8 Morris et al class: 1 = 1 3 | +| 2 cis-peptides = | | G-factors Dihedrals: -0.04 Covalent: -0.18 Overall: = -0.08 | | = | | M/c bond lengths: 99.4% within limits 0.6% highlighted = | | M/c bond angles: 94.0% within limits 6.0% highlighted = | | Planar groups: 100.0% within limits 0.0% highlighted = | | = | = +------------------------------------------------------------------------= ----+ + May be worth investigating further. * Worth investigating further. |
Overlapped Structure | Procheck Summary |