| Basic Information | |
|---|---|
| Species | Malus domestica |
| Cazyme ID | MDP0000283457 |
| Family | AA1 |
| Protein Properties | Length: 1039 Molecular Weight: 113856 Isoelectric Point: 6.6965 |
| Chromosome | Chromosome/Scaffold: 006372339 Start: 43668 End: 54021 |
| Description | TCP-1/cpn60 chaperonin family protein |
| View CDS | |
| External Links |
|---|
| NCBI Taxonomy |
| CAZyDB |
| Signature Domain Download full data set without filtering | |||
|---|---|---|---|
| Family | Start | End | Evalue |
| AA1 | 49 | 498 | 0 |
| KGILINGQFPGPDIHSVTNDNLIINVFNSLDEPFLLSWNGIQQRRNSFEDGVYGTTCPIPPGKNFTYILQVKDQIGSFYYFPSLAFHKAAGGFGGIRILS RPRIPVPFPDPAGDYTVLIGDWYKANHTTLKAHLDRGKKLPFPDGILINGRGPGGFSLNFEQGKTYRLRISNIGLQNSLNFRIQNHKMKLVEVEGTHTLQ TTYSSLDVHVGQSYSVLVTADQPGQDYYLVASSRFTSPILTTTGTVHYANSAGKVSGPPPGGPTIQVDWSLNQARSIRTNLTASGPRPNPQGSYHYGLIN LTKTYVLQNSAGQVNGKQRYGVNSVSFVPADTPLKLADYFKIGGVFRVGSISDRPTGGGLYLDTSVLGADYRAFVEIVFQNNEDIIQSWHLDGYSFFVVG MDGGQWTTASRNAYNLRDAVSRCTTQVYPKSWTAIYIPLDNVGMWNLRTE | |||
| Full Sequence |
|---|
| Protein Sequence Length: 1039 Download |
| MPLNGAEGAI WALLCLAALF SIAVAEDPYR FFEWNVTYGD IYPLGVRQKG ILINGQFPGP 60 DIHSVTNDNL IINVFNSLDE PFLLSWNGIQ QRRNSFEDGV YGTTCPIPPG KNFTYILQVK 120 DQIGSFYYFP SLAFHKAAGG FGGIRILSRP RIPVPFPDPA GDYTVLIGDW YKANHTTLKA 180 HLDRGKKLPF PDGILINGRG PGGFSLNFEQ GKTYRLRISN IGLQNSLNFR IQNHKMKLVE 240 VEGTHTLQTT YSSLDVHVGQ SYSVLVTADQ PGQDYYLVAS SRFTSPILTT TGTVHYANSA 300 GKVSGPPPGG PTIQVDWSLN QARSIRTNLT ASGPRPNPQG SYHYGLINLT KTYVLQNSAG 360 QVNGKQRYGV NSVSFVPADT PLKLADYFKI GGVFRVGSIS DRPTGGGLYL DTSVLGADYR 420 AFVEIVFQNN EDIIQSWHLD GYSFFVVGMD GGQWTTASRN AYNLRDAVSR CTTQVYPKSW 480 TAIYIPLDNV GMWNLRTEFW ARQYLGQQLY LRVERIFKDE ASEEKGERAR LASFVGAMAI 540 ADLVKTTLGP KGMDKILQST GRGHEVTVTN DGATILKSLH IDNAAAKVLV ESDISKVQDD 600 EVGDGTTSVV VLAGELLREA EKLVASKIHP MTIISGYRMA AECARNALLQ KVVDNKADSE 660 KFKSDLMKIA MTTLSSKILS QDKEHFAQLA VDAVMRLKGS TNLEAIQIIK KPGGSLIDSF 720 LDEGFILDKK IGLGQPKRIE NANILVANTA MDTDKVKIYG ARVRVDSMAK VAEIEGAEKD 780 KMREKVQKII GHGINCFVNR QLIYNFPEEL FADAGILAIE HADFDGIERL ALVTGGEIAS 840 TFDNPESVKL GHCKLIEEIM IGEDKLIHFS GVELGQACTI VLRGASHHVL DEAERSLHDA 900 LCVLSQTVND SRVLLGGGWP EMIMAKEVDE LARKTPGKKS HAIEAFSRAL LAIPTIIADN 960 AGLDSAELIA KLRAEHQKEG CTSGIDVISG TVGDMAERGI SEAFKVKQAV LLSATEAAEM 1020 ILRVDEIITC APRKREDRM 1080 |
| Functional Domains Download unfiltered results here | ||||||||
|---|---|---|---|---|---|---|---|---|
| Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
| cd03336 | TCP1_beta | 0 | 516 | 1034 | 519 | + TCP-1 (CTT or eukaryotic type II) chaperonin family, beta subunit. Chaperonins are involved in productive folding of proteins. They share a common general morphology, a double toroid of 2 stacked rings. In contrast to bacterial group I chaperonins (GroEL), each ring of the eukaryotic cytosolic chaperonin (CTT) consists of eight different, but homologous subunits. Their common function is to sequester nonnative proteins inside their central cavity and promote folding by using energy derived from ATP hydrolysis. The best studied in vivo substrates of CTT are actin and tubulin. | ||
| PTZ00212 | PTZ00212 | 0 | 515 | 1036 | 525 | + T-complex protein 1 subunit beta; Provisional | ||
| PLN02991 | PLN02991 | 0 | 13 | 513 | 501 | + oxidoreductase | ||
| TIGR02341 | chap_CCT_beta | 0 | 515 | 1035 | 521 | + T-complex protein 1, beta subunit. Members of this family, all eukaryotic, are part of the group II chaperonin complex called CCT (chaperonin containing TCP-1) or TRiC. The archaeal equivalent group II chaperonin is often called the thermosome. Both are somewhat related to the group I chaperonin of bacterial, GroEL/GroES. This family consists exclusively of the CCT beta chain (part of a paralogous family) from animals, plants, fungi, and other eukaryotes. | ||
| PLN02792 | PLN02792 | 0 | 18 | 513 | 499 | + oxidoreductase | ||
| Gene Ontology | |
|---|---|
| GO Term | Description |
| GO:0005507 | copper ion binding |
| GO:0005524 | ATP binding |
| GO:0016491 | oxidoreductase activity |
| GO:0044267 | cellular protein metabolic process |
| GO:0055114 | oxidation-reduction process |
| Annotations - NR Download unfiltered results here | |||||||
|---|---|---|---|---|---|---|---|
| Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
| RefSeq | NP_001050672.1 | 0 | 513 | 1039 | 1 | 525 | Os03g0619400 [Oryza sativa (japonica cultivar-group)] |
| RefSeq | NP_197589.1 | 0 | 513 | 1039 | 3 | 527 | chaperonin, putative [Arabidopsis thaliana] |
| RefSeq | XP_002285912.1 | 0 | 511 | 1039 | 1 | 527 | PREDICTED: hypothetical protein [Vitis vinifera] |
| RefSeq | XP_002326179.1 | 0 | 511 | 1039 | 1 | 527 | predicted protein [Populus trichocarpa] |
| RefSeq | XP_002510630.1 | 0 | 1 | 513 | 1 | 515 | multicopper oxidase, putative [Ricinus communis] |
| Annotations - PDB Download unfiltered results here | |||||||
|---|---|---|---|---|---|---|---|
| Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
| PDB | 4b2t_b | 0 | 516 | 1035 | 11 | 528 | G Chain G, An Unbiased Statistical Approach Solves The Crystal Structures Of The Group Ii Chaperonin Cct Tric |
| PDB | 4b2t_B | 0 | 516 | 1035 | 11 | 528 | G Chain G, An Unbiased Statistical Approach Solves The Crystal Structures Of The Group Ii Chaperonin Cct Tric |
| PDB | 4a13_P | 0 | 521 | 1033 | 3 | 513 | G Chain G, An Unbiased Statistical Approach Solves The Crystal Structures Of The Group Ii Chaperonin Cct Tric |
| PDB | 4a13_O | 0 | 521 | 1033 | 3 | 513 | G Chain G, An Unbiased Statistical Approach Solves The Crystal Structures Of The Group Ii Chaperonin Cct Tric |
| PDB | 4a13_N | 0 | 521 | 1033 | 3 | 513 | G Chain G, An Unbiased Statistical Approach Solves The Crystal Structures Of The Group Ii Chaperonin Cct Tric |
