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Conserved domains on  [gi|1327788988|ref|XP_023366244|]
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A-kinase anchor protein 2 isoform X3 [Otolemur garnettii]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
MYO6_MIU_linker super family cl46503
MIU-linker domain found in unconventional myosin-VI; Myosins are actin-based motor molecules ...
 15-117 3.34e-42

MIU-linker domain found in unconventional myosin-VI; Myosins are actin-based motor molecules with ATPase activity. Unconventional myosins function in intracellular movements. Myosin-VI, also called unconventional myosin-6 (MYO6), is a reverse-direction motor protein that moves towards the minus-end of actin filaments. It is required for the structural integrity of the Golgi apparatus via the p53-dependent pro-survival pathway. It appears to be involved in a very early step of clathrin-mediated endocytosis in polarized epithelial cells. It modulates RNA polymerase II-dependent transcription. As part of the DISP complex, Myosin-VI may regulate the association of septins with actin and thereby regulate the actin cytoskeleton. Myosin-VI is encoded by the MYO6 gene, the human homologue of the gene responsible for deafness in Snell's waltzer mice. It is mutated in autosomal dominant nonsyndromic hearing loss. This model corresponds to a conserved region of myosin-VI, which consist of three helices: MIU (Motif Interacting with Ubiquitin), a common linker helix (linker-alpha1) and an isoform-specific helix (linker-alpha2).


The actual alignment was detected with superfamily member pfam03285:

Pssm-ID: 480843  Cd Length: 301  Bit Score: 156.83  E-value: 3.34e-42
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327788988   15 AEKRKRQTEIEGKRQQLDEQILLLQHSKSKVLREKWLLQGIPAGTAEEEEARRRQSEEDEFRVKQLEDNIQRLEQEIQML 94
Cdd:pfam03285    1 AEKRKRQTEIENKRRQLEDDRRQLQHLKSKALRERWLLEGPPSSASEEDEARRRQEEEDEQKKKLLEEIIRRLEEEIELL 80

                           90       100
                   ....*....|....*....|...
gi 1327788988   95 ESEESQISAKEQIILEKLKETEK 117
Cdd:pfam03285   81 EEESSISAKKENLAEKLLEITVE 103
 
Name Accession Description Interval E-value
Paralemmin pfam03285
Paralemmin;
15-117 3.34e-42

Paralemmin;


Pssm-ID: 460875  Cd Length: 301  Bit Score: 156.83  E-value: 3.34e-42
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327788988   15 AEKRKRQTEIEGKRQQLDEQILLLQHSKSKVLREKWLLQGIPAGTAEEEEARRRQSEEDEFRVKQLEDNIQRLEQEIQML 94
Cdd:pfam03285    1 AEKRKRQTEIENKRRQLEDDRRQLQHLKSKALRERWLLEGPPSSASEEDEARRRQEEEDEQKKKLLEEIIRRLEEEIELL 80

                           90       100
                   ....*....|....*....|...
gi 1327788988   95 ESEESQISAKEQIILEKLKETEK 117
Cdd:pfam03285   81 EEESSISAKKENLAEKLLEITVE 103
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
9-117 9.39e-05

Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 46.30  E-value: 9.39e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327788988    9 ERLQAIAEKRKRQTEIEGKRQQLDEQilLLQHSKSkvlREKWLLQGIPAGTAEEEEARRRQSEEDEFRVKQLEDNIQRLE 88
Cdd:COG4717    385 EELRAALEQAEEYQELKEELEELEEQ--LEELLGE---LEELLEALDEEELEEELEELEEELEELEEELEELREELAELE 459

                           90       100       110
                   ....*....|....*....|....*....|.
gi 1327788988   89 QEIQMLESEE--SQISAKEQIILEKLKETEK 117
Cdd:COG4717    460 AELEQLEEDGelAELLQELEELKAELRELAE 490
PRK12704 PRK12704
phosphodiesterase; Provisional
 17-124 2.10e-03

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 42.07  E-value: 2.10e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327788988   17 KRKRQTEIEGKRQQLdEQILLLQHSKSKVLREKWLLQgipagtAEEEEARRRQSEEDEFRVK--QLEDNIQRLEQEIQML 94
Cdd:PRK12704    26 KKIAEAKIKEAEEEA-KRILEEAKKEAEAIKKEALLE------AKEEIHKLRNEFEKELRERrnELQKLEKRLLQKEENL 98

                           90       100       110
                   ....*....|....*....|....*....|
gi 1327788988   95 ESEESQISAKEQIILEKLKETEKSFKDFQK 124
Cdd:PRK12704    99 DRKLELLEKREEELEKKEKELEQKQQELEK 128
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 2-124 7.61e-03

chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 40.43  E-value: 7.61e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327788988    2 AEAELHkERLQAIAEKRKRQTEIEGKRQQLDEQILLLQHSKSKVLREKWLLQGIPAGTAEEEEARRRQSEEDEFRVKQLE 81
Cdd:TIGR02168  237 LREELE-ELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLE 315

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|...
gi 1327788988   82 DNIQRLEQEIQMLESEESQISAKEQIILEKLKETEKSFKDFQK 124
Cdd:TIGR02168  316 RQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEA 358
 
Name Accession Description Interval E-value
Paralemmin pfam03285
Paralemmin;
15-117 3.34e-42

Paralemmin;


Pssm-ID: 460875  Cd Length: 301  Bit Score: 156.83  E-value: 3.34e-42
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327788988   15 AEKRKRQTEIEGKRQQLDEQILLLQHSKSKVLREKWLLQGIPAGTAEEEEARRRQSEEDEFRVKQLEDNIQRLEQEIQML 94
Cdd:pfam03285    1 AEKRKRQTEIENKRRQLEDDRRQLQHLKSKALRERWLLEGPPSSASEEDEARRRQEEEDEQKKKLLEEIIRRLEEEIELL 80

                           90       100
                   ....*....|....*....|...
gi 1327788988   95 ESEESQISAKEQIILEKLKETEK 117
Cdd:pfam03285   81 EEESSISAKKENLAEKLLEITVE 103
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
9-117 9.39e-05

Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 46.30  E-value: 9.39e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327788988    9 ERLQAIAEKRKRQTEIEGKRQQLDEQilLLQHSKSkvlREKWLLQGIPAGTAEEEEARRRQSEEDEFRVKQLEDNIQRLE 88
Cdd:COG4717    385 EELRAALEQAEEYQELKEELEELEEQ--LEELLGE---LEELLEALDEEELEEELEELEEELEELEEELEELREELAELE 459

                           90       100       110
                   ....*....|....*....|....*....|.
gi 1327788988   89 QEIQMLESEE--SQISAKEQIILEKLKETEK 117
Cdd:COG4717    460 AELEQLEEDGelAELLQELEELKAELRELAE 490
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
8-114 1.00e-04

Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 46.45  E-value: 1.00e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327788988    8 KERLQA-IAEKRKRQTEIEGKRQQLDEQILLLQHSKSKVLREKWLLQGIPAGTAEEEEARRRQSEEDEF----RVKQLED 82
Cdd:COG4913    340 LEQLEReIERLERELEERERRRARLEALLAALGLPLPASAEEFAALRAEAAALLEALEEELEALEEALAeaeaALRDLRR 419

                           90       100       110
                   ....*....|....*....|....*....|..
gi 1327788988   83 NIQRLEQEIQMLESEESQISAKEQIILEKLKE 114
Cdd:COG4913    420 ELRELEAEIASLERRKSNIPARLLALRDALAE 451
ARGLU pfam15346
Arginine and glutamate-rich 1; ARGLU, arginine and glutamate-rich 1 protein family, is ...
 1-111 2.47e-04

Arginine and glutamate-rich 1; ARGLU, arginine and glutamate-rich 1 protein family, is required for the oestrogen-dependent expression of ESR1 target genes. It functions in cooperation with MED1. The family of proteins is found in eukaryotes.


Pssm-ID: 405931 [Multi-domain]  Cd Length: 151  Bit Score: 42.35  E-value: 2.47e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327788988    1 MAEAELHKERLQAIAEKRKRQTEIEGKRQQLDEqiLLLQHSKskvlrekwllqgipagtaEEEEARRRQSEEdefRVKQL 80
Cdd:pfam15346   53 QVLEELEREREAELEEERRKEEEERKKREELER--ILEENNR------------------KIEEAQRKEAEE---RLAML 109

                           90       100       110
                   ....*....|....*....|....*....|..
gi 1327788988   81 EDnIQRLEQEIQMLESEESQISAKEQ-IILEK 111
Cdd:pfam15346  110 EE-QRRMKEERQRREKEEEEREKREQqKILNK 140
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
1-124 2.80e-04

Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 44.76  E-value: 2.80e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327788988    1 MAEAELHKERLQAIAEKRKRQTEIEGKRQQLDEQILLLQHSKSKVLREKWLLQGIPAGTAEEEEARRRQSEEDEFRVKQL 80
Cdd:COG4717    118 LEKLEKLLQLLPLYQELEALEAELAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDL 197

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....
gi 1327788988   81 EDNIQRLEQEIQMLESEESQISAKEQIILEKLKETEKSFKDFQK 124
Cdd:COG4717    198 AEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAAL 241
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 2-124 3.17e-04

Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 44.93  E-value: 3.17e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327788988    2 AEAELHKERLQAIAEKRKRQTEIEGKRQQLDEQILLLQHSKSKVLREKWLLQGIPAGTAEEEEAR----------RRQSE 71
Cdd:COG1196    317 RLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELeelaeelleaLRAAA 396

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1327788988   72 EDEFRVKQLEDNIQRLEQEIQMLESEESQISAKEQIILEKLKETEKSFKDFQK 124
Cdd:COG1196    397 ELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAE 449
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 5-104 4.81e-04

Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 43.60  E-value: 4.81e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327788988    5 ELHKERLQAIAEKRKRQTEIEGKRQQLDEQILLLQHSKSKVLREKWLLQGIPAGTAEEEEARRRQSEEDEFRVKQLEDNI 84
Cdd:COG4942    143 YLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEA 222

                           90       100
                   ....*....|....*....|
gi 1327788988   85 QRLEQEIQMLESEESQISAK 104
Cdd:COG4942    223 EELEALIARLEAEAAAAAER 242
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
 3-123 8.81e-04

Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.


Pssm-ID: 375164 [Multi-domain]  Cd Length: 722  Bit Score: 43.19  E-value: 8.81e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327788988    3 EAELHKERLQAIAEKRKRQTEIEGKRQQLDEQillLQHSKSKVLREKWLLQGIPAGTAEE-----EEARRRQSEEDEFRV 77
Cdd:pfam17380  469 EEERKRKKLELEKEKRDRKRAEEQRRKILEKE---LEERKQAMIEEERKRKLLEKEMEERqkaiyEEERRREAEEERRKQ 545

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*...
gi 1327788988   78 KQLEDNiQRLEQEIQMLESEESQISA--KEQIILEKLKETEKSFKDFQ 123
Cdd:pfam17380  546 QEMEER-RRIQEQMRKATEERSRLEAmeREREMMRQIVESEKARAEYE 592
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 2-95 9.39e-04

Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 43.39  E-value: 9.39e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327788988    2 AEAELHKERLQAIAEKRKRQTEIEGKRQQLDEQILLLQHSKSKVLREKWLLQGIPAGTAEEEEARRRQSEEDEFRVKQLE 81
Cdd:COG1196    687 RLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELE 766

                           90
                   ....*....|....
gi 1327788988   82 DNIQRLEQEIQMLE 95
Cdd:COG1196    767 RELERLEREIEALG 780
PRK12704 PRK12704
phosphodiesterase; Provisional
 17-124 2.10e-03

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 42.07  E-value: 2.10e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327788988   17 KRKRQTEIEGKRQQLdEQILLLQHSKSKVLREKWLLQgipagtAEEEEARRRQSEEDEFRVK--QLEDNIQRLEQEIQML 94
Cdd:PRK12704    26 KKIAEAKIKEAEEEA-KRILEEAKKEAEAIKKEALLE------AKEEIHKLRNEFEKELRERrnELQKLEKRLLQKEENL 98

                           90       100       110
                   ....*....|....*....|....*....|
gi 1327788988   95 ESEESQISAKEQIILEKLKETEKSFKDFQK 124
Cdd:PRK12704    99 DRKLELLEKREEELEKKEKELEQKQQELEK 128
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 2-124 3.47e-03

Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 41.46  E-value: 3.47e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327788988    2 AEAELHKERLQ------AIAEKRKRQTEIEGKRQQLDEQILLLQHSKSKVLREKwllqgipAGTAEEEEARRRQSEEDEF 75
Cdd:COG1196    265 LEAELEELRLEleelelELEEAQAEEYELLAELARLEQDIARLEERRRELEERL-------EELEEELAELEEELEELEE 337

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*....
gi 1327788988   76 RVKQLEDNIQRLEQEIQMLESEESQISAKEQIILEKLKETEKSFKDFQK 124
Cdd:COG1196    338 ELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAE 386
PspA_IM30 pfam04012
PspA/IM30 family; This family includes PspA a protein that suppresses sigma54-dependent ...
 4-108 6.41e-03

PspA/IM30 family; This family includes PspA a protein that suppresses sigma54-dependent transcription. The PspA protein, a negative regulator of the Escherichia coli phage shock psp operon, is produced when virulence factors are exported through secretins in many Gram-negative pathogenic bacteria and its homolog in plants, VIPP1, plays a critical role in thylakoid biogenesis, essential for photosynthesis. Activation of transcription by the enhancer-dependent bacterial sigma(54) containing RNA polymerase occurs through ATP hydrolysis-driven protein conformational changes enabled by activator proteins that belong to the large AAA(+) mechanochemical protein family. It has been shown that PspA directly and specifically acts upon and binds to the AAA(+) domain of the PspF transcription activator.


Pssm-ID: 461130 [Multi-domain]  Cd Length: 215  Bit Score: 39.28  E-value: 6.41e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327788988    4 AELHKERLQAIAEKR------KRQTEIEGKRQQLDEQILLLQHSK--SKVLREKWLLQGIPAGTAEEEEARRRQSEEDEF 75
Cdd:pfam04012   39 VKARQALAQTIARQKqlerrlEQQTEQAKKLEEKAQAALTKGNEElaREALAEKKSLEKQAEALETQLAQQRSAVEQLRK 118

                           90       100       110
                   ....*....|....*....|....*....|...
gi 1327788988   76 RVKQLEDNIQRLEQEIQMLESEESQISAKEQII 108
Cdd:pfam04012  119 QLAALETKIQQLKAKKNLLKARLKAAKAQEAVQ 151
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 2-124 7.61e-03

chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 40.43  E-value: 7.61e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327788988    2 AEAELHkERLQAIAEKRKRQTEIEGKRQQLDEQILLLQHSKSKVLREKWLLQGIPAGTAEEEEARRRQSEEDEFRVKQLE 81
Cdd:TIGR02168  237 LREELE-ELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLE 315

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|...
gi 1327788988   82 DNIQRLEQEIQMLESEESQISAKEQIILEKLKETEKSFKDFQK 124
Cdd:TIGR02168  316 RQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEA 358
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
4-116 8.15e-03

Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 40.28  E-value: 8.15e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327788988    4 AELHKERLQA---IAEKRKRQTEIEGKRQQLDEQILLLQhsksKVLREKWLLQGIPAgtAEEE----EARRRQSEEDEFR 76
Cdd:COG4913    613 AALEAELAELeeeLAEAEERLEALEAELDALQERREALQ----RLAEYSWDEIDVAS--AEREiaelEAELERLDASSDD 686

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|
gi 1327788988   77 VKQLEDNIQRLEQEIQMLESEESQISAKEQIILEKLKETE 116
Cdd:COG4913    687 LAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAE 726
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
3-124 8.45e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 40.05  E-value: 8.45e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327788988    3 EAELHKERlqaIAEKRKRQTEIEGKRQQLDEQILLLQH------SKSKVLREKwlLQGIPAGTAEEEEARRRQSEEDEFR 76
Cdd:PRK03918   232 ELEELKEE---IEELEKELESLEGSKRKLEEKIRELEErieelkKEIEELEEK--VKELKELKEKAEEYIKLSEFYEEYL 306

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|
gi 1327788988   77 VK--QLEDNIQRLEQEIQMLESEESQISAKEqiilEKLKETEKSFKDFQK 124
Cdd:PRK03918   307 DElrEIEKRLSRLEEEINGIEERIKELEEKE----ERLEELKKKLKELEK 352
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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