>AGAP012068-PA gnl|CDD|64510 pfam00648, Peptidase_C2, Calpain family cysteine p... 433 e-122 gnl|CDD|64906 pfam01067, Calpain_III, Calpain large subunit, dom... 223 3e-059 gnl|CDD|70679 pfam07223, DUF1421, Protein of unknown function (D... 34 0.055 gnl|CDD|63925 pfam00036, efhand, EF hand. The EF-hands can be di... 33 0.077 gnl|CDD|68080 pfam04495, GRASP55_65, GRASP55/65 family. GRASP55 ... 32 0.14 gnl|CDD|65230 pfam01416, PseudoU_synth_1, tRNA pseudouridine syn... 31 0.23 gnl|CDD|66806 pfam03154, Atrophin-1, Atrophin-1 family. Atrophin... 30 0.66 ==> gnl|CDD|64510 pfam00648, Peptidase_C2, Calpain family cysteine protease.. Length = 303 Score = 433 bits (1116), Expect = e-122 Identities = 177/308 (57%), Positives = 222/308 (72%), Gaps = 12/308 (3%) Query: 151 LFEDPEFPASASSLMYSKRPD-----RHYEWLRPHEICDGPEFFVEGFSRFDVQQGELGD 205 LF DP FPA SL Y R EW RPHEIC+ P+F + G +R D+ QG LGD Sbjct: 1 LFVDPSFPADPKSLGYKPLGPYSSKTRGIEWKRPHEICENPQFIIGGATRTDICQGALGD 60 Query: 206 CWLLAACANLTQDHKMFLRVVPEDNSFEDGYAGVFHFRFWQYGKWVDVVIDDRLPTYRGQ 265 CWLLAA A+LT + ++ RVVP D SF++ YAG+FHF+FWQYG+WVDVV+DDRLPT G+ Sbjct: 61 CWLLAAIASLTLNEELLFRVVPHDQSFQENYAGIFHFQFWQYGEWVDVVVDDRLPTKDGE 120 Query: 266 LIYMRSSEQNEFWSALLEKAYAKLHGSYESLRGGTTCEAMEDFTGGVAEMYDLKDQTPP- 324 L+++ S+E+NEFWSALLEKAYAKLHG YE+L GG+T EAMEDFTGGVAE Y+LK Sbjct: 121 LVFVHSAERNEFWSALLEKAYAKLHGCYEALSGGSTTEAMEDFTGGVAEWYELKQAPSDL 180 Query: 325 NLFEIIEKGFKRNSMFGCSI-EADPHVLEAETPEGLIRGHAYSITKIQLVDIETPGRSGK 383 NLF+II K +R S+ GCSI P +EA T +GL++GHAYS+T ++ V+ R K Sbjct: 181 NLFKIIAKALERGSLMGCSIDITSPVDMEARTFKGLVKGHAYSVTGVKEVN----YRGEK 236 Query: 384 IPLIRLRNPWGNEAEWNGPWSDKSPEWRYIPDEQKQELGLNFDHDGEFWMSYRDFTRYFD 443 LIRLRNPWG + EW G WSD SPEWR+I +++ L L F+ DGEFWMS+ DF R+F Sbjct: 237 QKLIRLRNPWG-QVEWTGAWSDGSPEWRFIDPDERARLQLQFEEDGEFWMSFEDFLRHFS 295 Query: 444 RMEICNLS 451 R+EICNL+ Sbjct: 296 RLEICNLT 303 ==> gnl|CDD|64906 pfam01067, Calpain_III, Calpain large subunit, domain III. The function of the domain III and I are currently unknown. Domain II is a cysteine protease and domain IV is a calcium binding domain. Calpains are believed to participate in intracellular signaling pathways mediated by calcium ions.. Length = 150 Score = 223 bits (570), Expect = 3e-059 Identities = 92/147 (62%), Positives = 113/147 (76%), Gaps = 2/147 (1%) Query: 466 SWEMSMFEGEWAVGTTAGGCRNYLDTFWHNPQYVIRLDDPDEDDEEGNCTVIIALLQKNR 525 WE ++ EGEW G+TAGGCRNY DTFW NPQY+I L++PD+DD++ C+V++AL+QK+R Sbjct: 1 KWEETIVEGEWTRGSTAGGCRNYPDTFWTNPQYIITLEEPDDDDDDSECSVLVALMQKDR 60 Query: 526 RSRRNMGVECLTIGFAVYRVTERDLAQKPLKMNFFKYNASAARSPAFINLREVSCRFKLP 585 R R MG + LTIGFAVY+V + L +FF N S ARS FINLREVS RF+LP Sbjct: 61 RRERRMGEDMLTIGFAVYKVPDEL--NVHLSRDFFLTNQSRARSSTFINLREVSLRFRLP 118 Query: 586 PGTYVIVPSTFEPNEEGEFIIRVFSET 612 PG YV+VPSTFEPNEEGEFI+RVFSE Sbjct: 119 PGEYVVVPSTFEPNEEGEFILRVFSEK 145 ==> gnl|CDD|70679 pfam07223, DUF1421, Protein of unknown function (DUF1421). This family represents a conserved region approximately 350 residues long within a number of plant proteins of unknown function.. Length = 331 Score = 33.6 bits (76), Expect = 0.055 Identities = 30/116 (25%), Positives = 36/116 (31%), Gaps = 27/116 (23%) Query: 6 QSPPA-SQWPTVPTPGSSGYSSLNPSISGQSLSYGFNPNVMP---ALPDSGAGYP----- 56 Q+PP Q+P P P SGY+ Q SY N N P P S Sbjct: 129 QAPPQQPQYPQQP-PPPSGYNPEEQPAQTQ--SYPPNQNWPPQPQPPPGSSPSQQTYNPP 185 Query: 57 ---PAGNQLP--YPTMGFAGFGSPMDYT----------MPNLPPPVPDALLRGAEP 97 P+ P GF S Y + PP P +GA P Sbjct: 186 PPQPSMYDGPGGRSNSGFPSGYSMEAYGYGGAPPPQAGRMSYKPPHPSQQGQGAYP 241 ==> gnl|CDD|63925 pfam00036, efhand, EF hand. The EF-hands can be divided into two classes: signaling proteins and buffering/transport proteins. The first group is the largest and includes the most well-known members of the family such as calmodulin, troponin C and S100B. These proteins typically undergo a calcium-dependent conformational change which opens a target binding site. The latter group is represented by calbindin D9k and do not undergo calcium dependent conformational changes.. Length = 29 Score = 32.9 bits (76), Expect = 0.077 Identities = 9/28 (32%), Positives = 14/28 (50%) Query: 691 CRAMVAMLDVDHTGKLGFEEFQQLLTDI 718 + D D GK+ FEEF++ L + Sbjct: 2 LKEAFKEFDKDGDGKISFEEFKEALKKL 29 ==> gnl|CDD|68080 pfam04495, GRASP55_65, GRASP55/65 family. GRASP55 (Golgi reassembly stacking protein of 55 kDa) and GRASP65 (a 65 kDa) protein are highly homologous. GRASP55 is a component of the Golgi stacking machinery. GRASP65, an N-ethylmaleimide- sensitive membrane protein required for the stacking of Golgi cisternae in a cell-free system.. Length = 321 Score = 32.0 bits (72), Expect = 0.14 Identities = 19/99 (19%), Positives = 26/99 (26%), Gaps = 4/99 (4%) Query: 1 PAAFAQSPPASQWPTVPTPGSSGYSSLNPSISGQSLSYGFNPNVMPALPDSGAG--YPPA 58 PAA P+ P + SS+ P PP Sbjct: 153 PAATNFPDPSPLLSPFSAPPAP--SSVLQLGGPTPPYPPPLVQQGSYAPPVEPETQLPPP 210 Query: 59 GNQLPYPTMGFAGFGSPMDYTMPNLPPPVPDALLRGAEP 97 + L + A GS + P P P A+P Sbjct: 211 SSLLGHGLSSSANAGSSNEIPPPAPQPTPPYVQSPSAQP 249 ==> gnl|CDD|65230 pfam01416, PseudoU_synth_1, tRNA pseudouridine synthase. Involved in the formation of pseudouridine at the anticodon stem and loop of transfer-RNAs Pseudouridine is an isomer of uridine (5-(beta-D-ribofuranosyl) uracil, and id the most abundant modified nucleoside found in all cellular RNAs. The TruA-like proteins also exhibit a conserved sequence with a strictly conserved aspartic acid, likely involved in catalysis.. Length = 101 Score = 31.4 bits (71), Expect = 0.23 Identities = 21/73 (28%), Positives = 29/73 (39%), Gaps = 8/73 (10%) Query: 662 EVDWVELKRILDHSFRDDNISSEGFSKDVCRAMVAMLDVDHTGKLGFEEFQQLLT----- 716 + L RI R IS GF+ RA+V +L G+ E+ ++LL Sbjct: 26 TILEKALSRIGGEKIR---ISGAGFTDKGVRAIVQVLLFVGPGERPPEDIKELLNAKLRD 82 Query: 717 DIAKWKAVFKLYD 729 DI A LY Sbjct: 83 DIGVLTAPAGLYL 95 ==> gnl|CDD|66806 pfam03154, Atrophin-1, Atrophin-1 family. Atrophin-1 is the protein product of the dentatorubral-pallidoluysian atrophy (DRPLA) gene. DRPLA OMIM:125370 is a progressive neurodegenerative disorder. It is caused by the expansion of a CAG repeat in the DRPLA gene on chromosome 12p. This results in an extended polyglutamine region in atrophin-1, that is thought to confer toxicity to the protein, possibly through altering its interactions with other proteins. The expansion of a CAG repeat is also the underlying defect in six other neurodegenerative disorders, including Huntington's disease. One interaction of expanded polyglutamine repeats that is thought to be pathogenic is that with the short glutamine repeat in the transcriptional coactivator CREB binding protein, CBP. This interaction draws CBP away from its usual nuclear location to the expanded polyglutamine repeat protein aggregates that are characteristic of the polyglutamine neurodegenerative disorders. This interferes with CBP-mediated transcription and causes cytotoxicity.. Length = 984 Score = 29.8 bits (66), Expect = 0.66 Identities = 20/86 (23%), Positives = 29/86 (33%), Gaps = 3/86 (3%) Query: 6 QSPPASQWPTVPTPGSSGYSSLNPSISGQSLSYGFNPNVMPALPDSGAGYPPAGNQLPYP 65 QSP A PG+ ++ PSI S + P P + P+ Sbjct: 210 QSPTAPPPDVPQQPGAQSVPAVAPSIQAASALHPQRPPSPHNPLSPFLFPPSLPSAQPHA 269 Query: 66 TMGFAGFGSPMDYTM---PNLPPPVP 88 G G P +++ P L P P Sbjct: 270 QPPLHGQGPPSPHSLQAGPLLQHPQP 295 Score = 29.4 bits (65), Expect = 0.87 Identities = 19/90 (21%), Positives = 26/90 (28%), Gaps = 4/90 (4%) Query: 1 PAAFAQSPPASQ----WPTVPTPGSSGYSSLNPSISGQSLSYGFNPNVMPALPDSGAGYP 56 P Q PP+ P + P + GQ+ P+ + P Sbjct: 271 PPLHGQGPPSPHSLQAGPLLQHPQPPQNFLPPQASQGQAPLGTSPAAAYPSQSALQSQQP 330 Query: 57 PAGNQLPYPTMGFAGFGSPMDYTMPNLPPP 86 P LP G P +P LP P Sbjct: 331 PREQPLPPAPSGMPHIKPPPTTPIPQLPAP 360