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Conserved domains on  [gi|1034638397|ref|XP_016863220|]
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mitochondria-eating protein isoform X2 [Homo sapiens]

Protein Classification

MIEAP domain-containing protein( domain architecture ID 11240381)

MIEAP domain-containing protein

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
MIEAP pfam16026
Mitochondria-eating protein; This domain is found at the C-terminus of mitochondria-eating ...
 178-368 1.44e-86

Mitochondria-eating protein; This domain is found at the C-terminus of mitochondria-eating proteins. This family of proteins regulate mitochondrial quality. They have a role in the degradation of damaged mitochondrial proteins and in the degradation of damaged mitochondria.


:

Pssm-ID: 464982  Cd Length: 198  Bit Score: 261.80  E-value: 1.44e-86
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638397 178 RKAALLSRFSDSYSQARLDAQCLLRRCI-DKAETVQRIIYIATVEAFHVAKMAFRHFKIHVRKSLTPSYVGSN----DFE 252
Cdd:pfam16026   1 RPSKLVERFSELYSNERLDAFEALDRLIdLEEELVQKILFSILVEAFRFCKEALRQLKLRVRKTLSPPHTGPEtrkeSLE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638397 253 NAVLDYVICHLDLYDSQSSVNDVIRAMNVNPKISFPPVVDFCLLSDFIQEICCIAFAMQALEPPLDIAYGADGEVFNDCK 332
Cdd:pfam16026  81 DAVSDYIRRHADLYDLQASVNEVICQMNVNPLISFPPLVECKLLRSYIRECVRLAWLMQIQDPPLDLAFEFDGELFDPEK 160

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 1034638397 333 YRRSYDSDFTAPLVLYHVWPALME--NDCVIMKGEAVT 368
Cdd:pfam16026 161 HRRSYDSDFTGDLVDYYVWPALMEheNGPVLSKGVVVT 198
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
1-131 3.83e-08

Uncharacterized protein, contains DUF3084 domain [Function unknown];


:

Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 54.91  E-value: 3.83e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638397   1 MQQLDSNLNSTRSQCNQVQDDLVETEKNLEESKNRsaisLLAAEEEINQLKKQLKSLQAQEDARHRNTDQRSSENRRSEP 80
Cdd:COG4372    40 LDKLQEELEQLREELEQAREELEQLEEELEQARSE----LEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQE 115

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1034638397  81 wSLEERKREQwNSLKQNADQ------QDTEAMSDYKKQLRNLKEEIAVLSAEKSALQ 131
Cdd:COG4372   116 -ELEELQKER-QDLEQQRKQleaqiaELQSEIAEREEELKELEEQLESLQEELAALE 170
 
Name Accession Description Interval E-value
MIEAP pfam16026
Mitochondria-eating protein; This domain is found at the C-terminus of mitochondria-eating ...
 178-368 1.44e-86

Mitochondria-eating protein; This domain is found at the C-terminus of mitochondria-eating proteins. This family of proteins regulate mitochondrial quality. They have a role in the degradation of damaged mitochondrial proteins and in the degradation of damaged mitochondria.


Pssm-ID: 464982  Cd Length: 198  Bit Score: 261.80  E-value: 1.44e-86
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638397 178 RKAALLSRFSDSYSQARLDAQCLLRRCI-DKAETVQRIIYIATVEAFHVAKMAFRHFKIHVRKSLTPSYVGSN----DFE 252
Cdd:pfam16026   1 RPSKLVERFSELYSNERLDAFEALDRLIdLEEELVQKILFSILVEAFRFCKEALRQLKLRVRKTLSPPHTGPEtrkeSLE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638397 253 NAVLDYVICHLDLYDSQSSVNDVIRAMNVNPKISFPPVVDFCLLSDFIQEICCIAFAMQALEPPLDIAYGADGEVFNDCK 332
Cdd:pfam16026  81 DAVSDYIRRHADLYDLQASVNEVICQMNVNPLISFPPLVECKLLRSYIRECVRLAWLMQIQDPPLDLAFEFDGELFDPEK 160

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 1034638397 333 YRRSYDSDFTAPLVLYHVWPALME--NDCVIMKGEAVT 368
Cdd:pfam16026 161 HRRSYDSDFTGDLVDYYVWPALMEheNGPVLSKGVVVT 198
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
1-131 3.83e-08

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 54.91  E-value: 3.83e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638397   1 MQQLDSNLNSTRSQCNQVQDDLVETEKNLEESKNRsaisLLAAEEEINQLKKQLKSLQAQEDARHRNTDQRSSENRRSEP 80
Cdd:COG4372    40 LDKLQEELEQLREELEQAREELEQLEEELEQARSE----LEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQE 115

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1034638397  81 wSLEERKREQwNSLKQNADQ------QDTEAMSDYKKQLRNLKEEIAVLSAEKSALQ 131
Cdd:COG4372   116 -ELEELQKER-QDLEQQRKQleaqiaELQSEIAEREEELKELEEQLESLQEELAALE 170
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
8-131 9.61e-05

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 44.67  E-value: 9.61e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638397   8 LNSTRSQCNQVQDDLVETEKNLEEsknrsaisLLAAEEEINQLKKQLKSLQ---AQEDARHRNTDQRSSEnRRSEPWSLE 84
Cdd:PRK03918  209 INEISSELPELREELEKLEKEVKE--------LEELKEEIEELEKELESLEgskRKLEEKIRELEERIEE-LKKEIEELE 279

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1034638397  85 ERKREQwNSLKQNADQQDT--EAMSDYKKQLRNLKEEIAVLSAEKSALQ 131
Cdd:PRK03918  280 EKVKEL-KELKEKAEEYIKlsEFYEEYLDELREIEKRLSRLEEEINGIE 327
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 6-131 3.48e-04

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: 43.12  E-value: 3.48e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638397    6 SNLNSTRSQCNQVQDDLVETEKNLE--ESKNRSAISLLAAEEEINQLKKQL--KSLQAQEDARHRNTDQRSSENRRSEPW 81
Cdd:TIGR02168  179 RKLERTRENLDRLEDILNELERQLKslERQAEKAERYKELKAELRELELALlvLRLEELREELEELQEELKEAEEELEEL 258

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|
gi 1034638397   82 SLEERKREQWNSLKQNADQQDTEAMSDYKKQLRNLKEEIAVLSAEKSALQ 131
Cdd:TIGR02168  259 TAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILR 308
Cast pfam10174
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ...
 44-128 1.15e-03

RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.


Pssm-ID: 431111 [Multi-domain]  Cd Length: 766  Bit Score: 41.35  E-value: 1.15e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638397  44 EEEINQLKKQLKSLQaqEDARHRNTDQRSSENRRSEPWSLEERKREQwnslKQNADQQDTEAMSDYKKQLRNLKEEIAVL 123
Cdd:pfam10174 414 DKQLAGLKERVKSLQ--TDSSNTDTALTTLEEALSEKERIIERLKEQ----REREDRERLEELESLKKENKDLKEKVSAL 487


                  ....*
gi 1034638397 124 SAEKS 128
Cdd:pfam10174 488 QPELT 492
 
Name Accession Description Interval E-value
MIEAP pfam16026
Mitochondria-eating protein; This domain is found at the C-terminus of mitochondria-eating ...
 178-368 1.44e-86

Mitochondria-eating protein; This domain is found at the C-terminus of mitochondria-eating proteins. This family of proteins regulate mitochondrial quality. They have a role in the degradation of damaged mitochondrial proteins and in the degradation of damaged mitochondria.


Pssm-ID: 464982  Cd Length: 198  Bit Score: 261.80  E-value: 1.44e-86
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638397 178 RKAALLSRFSDSYSQARLDAQCLLRRCI-DKAETVQRIIYIATVEAFHVAKMAFRHFKIHVRKSLTPSYVGSN----DFE 252
Cdd:pfam16026   1 RPSKLVERFSELYSNERLDAFEALDRLIdLEEELVQKILFSILVEAFRFCKEALRQLKLRVRKTLSPPHTGPEtrkeSLE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638397 253 NAVLDYVICHLDLYDSQSSVNDVIRAMNVNPKISFPPVVDFCLLSDFIQEICCIAFAMQALEPPLDIAYGADGEVFNDCK 332
Cdd:pfam16026  81 DAVSDYIRRHADLYDLQASVNEVICQMNVNPLISFPPLVECKLLRSYIRECVRLAWLMQIQDPPLDLAFEFDGELFDPEK 160

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 1034638397 333 YRRSYDSDFTAPLVLYHVWPALME--NDCVIMKGEAVT 368
Cdd:pfam16026 161 HRRSYDSDFTGDLVDYYVWPALMEheNGPVLSKGVVVT 198
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
1-131 3.83e-08

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 54.91  E-value: 3.83e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638397   1 MQQLDSNLNSTRSQCNQVQDDLVETEKNLEESKNRsaisLLAAEEEINQLKKQLKSLQAQEDARHRNTDQRSSENRRSEP 80
Cdd:COG4372    40 LDKLQEELEQLREELEQAREELEQLEEELEQARSE----LEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQE 115

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1034638397  81 wSLEERKREQwNSLKQNADQ------QDTEAMSDYKKQLRNLKEEIAVLSAEKSALQ 131
Cdd:COG4372   116 -ELEELQKER-QDLEQQRKQleaqiaELQSEIAEREEELKELEEQLESLQEELAALE 170
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 1-131 6.78e-05

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: 44.75  E-value: 6.78e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638397   1 MQQLDSNLNSTRSQCNQVQDDLVETEKNLEESKNR-SAIS--LLAAEEEINQLKKQLKSLQAQEDARHR------NTDQR 71
Cdd:COG4942    36 IAELEKELAALKKEEKALLKQLAALERRIAALARRiRALEqeLAALEAELAELEKEIAELRAELEAQKEelaellRALYR 115

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1034638397  72 SSENRR------SEPWSLEERKREQWNSLKQnADQQDTEAMSDYKKQLRNLKEEIAVLSAEKSALQ 131
Cdd:COG4942   116 LGRQPPlalllsPEDFLDAVRRLQYLKYLAP-ARREQAEELRADLAELAALRAELEAERAELEALL 180
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
8-131 9.61e-05

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 44.67  E-value: 9.61e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638397   8 LNSTRSQCNQVQDDLVETEKNLEEsknrsaisLLAAEEEINQLKKQLKSLQ---AQEDARHRNTDQRSSEnRRSEPWSLE 84
Cdd:PRK03918  209 INEISSELPELREELEKLEKEVKE--------LEELKEEIEELEKELESLEgskRKLEEKIRELEERIEE-LKKEIEELE 279

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1034638397  85 ERKREQwNSLKQNADQQDT--EAMSDYKKQLRNLKEEIAVLSAEKSALQ 131
Cdd:PRK03918  280 EKVKEL-KELKEKAEEYIKlsEFYEEYLDELREIEKRLSRLEEEINGIE 327
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
4-131 3.26e-04

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 42.58  E-value: 3.26e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638397   4 LDSNLNSTRSQCNQVQDDLVETEKNLEESKNRsaisLLAAEEEINQLKKQLKSLQAQEDARHRNTDQRSSEnrrsepwsl 83
Cdd:COG4372    29 LSEQLRKALFELDKLQEELEQLREELEQAREE----LEQLEEELEQARSELEQLEEELEELNEQLQAAQAE--------- 95

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1034638397  84 EERKREQWNSLKQNADQQDTEaMSDYKKQLRNLKEEIAVLSAEKSALQ 131
Cdd:COG4372    96 LAQAQEELESLQEEAEELQEE-LEELQKERQDLEQQRKQLEAQIAELQ 142
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 6-131 3.48e-04

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: 43.12  E-value: 3.48e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638397    6 SNLNSTRSQCNQVQDDLVETEKNLE--ESKNRSAISLLAAEEEINQLKKQL--KSLQAQEDARHRNTDQRSSENRRSEPW 81
Cdd:TIGR02168  179 RKLERTRENLDRLEDILNELERQLKslERQAEKAERYKELKAELRELELALlvLRLEELREELEELQEELKEAEEELEEL 258

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|
gi 1034638397   82 SLEERKREQWNSLKQNADQQDTEAMSDYKKQLRNLKEEIAVLSAEKSALQ 131
Cdd:TIGR02168  259 TAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILR 308
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 1-131 8.18e-04

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 41.85  E-value: 8.18e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638397   1 MQQLDSNLNSTRSQCNQVQDDLVETEKNLEESKNRSAISLLAAEEEINQLKKQLKSLQAQ-----EDARHRNTDQRSSEN 75
Cdd:COG1196   286 AQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEEleeaeEELEEAEAELAEAEE 365

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1034638397  76 RRSEpwslEERKREQWNSLKQNADQQDTEAMSD---YKKQLRNLKEEIAVLSAEKSALQ 131
Cdd:COG1196   366 ALLE----AEAELAEAEEELEELAEELLEALRAaaeLAAQLEELEEAEEALLERLERLE 420
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
1-104 9.47e-04

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 41.04  E-value: 9.47e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638397   1 MQQLDSNLNSTRSQCNQVQ---DDLVETEKNLEESKNRSAISLLAAEEEINQLKKQLKSLQAQEDARHRNTDQRSSENRR 77
Cdd:COG4372   103 LESLQEEAEELQEELEELQkerQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAE 182

                          90       100
                  ....*....|....*....|....*..
gi 1034638397  78 SEPWSLEERKREQWNSLKQNADQQDTE 104
Cdd:COG4372   183 QALDELLKEANRNAEKEEELAEAEKLI 209
Cast pfam10174
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ...
 44-128 1.15e-03

RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.


Pssm-ID: 431111 [Multi-domain]  Cd Length: 766  Bit Score: 41.35  E-value: 1.15e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638397  44 EEEINQLKKQLKSLQaqEDARHRNTDQRSSENRRSEPWSLEERKREQwnslKQNADQQDTEAMSDYKKQLRNLKEEIAVL 123
Cdd:pfam10174 414 DKQLAGLKERVKSLQ--TDSSNTDTALTTLEEALSEKERIIERLKEQ----REREDRERLEELESLKKENKDLKEKVSAL 487


                  ....*
gi 1034638397 124 SAEKS 128
Cdd:pfam10174 488 QPELT 492
GAS pfam13851
Growth-arrest specific micro-tubule binding; This family is the highly conserved central ...
 45-131 1.27e-03

Growth-arrest specific micro-tubule binding; This family is the highly conserved central region of a number of metazoan proteins referred to as growth-arrest proteins. In mouse, Gas8 is predominantly a testicular protein, whose expression is developmentally regulated during puberty and spermatogenesis. In humans, it is absent in infertile males who lack the ability to generate gametes. The localization of Gas8 in the motility apparatus of post-meiotic gametocytes and mature spermatozoa, together with the detection of Gas8 also in cilia at the apical surfaces of epithelial cells lining the pulmonary bronchi and Fallopian tubes suggests that the Gas8 protein may have a role in the functioning of motile cellular appendages. Gas8 is a microtubule-binding protein localized to regions of dynein regulation in mammalian cells.


Pssm-ID: 464001 [Multi-domain]  Cd Length: 200  Bit Score: 39.89  E-value: 1.27e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638397  45 EEINQLKKQLKSLQAQEDARHRNTDQRSSENRR-SEPwsLEERKREQwNSLKQNADQQDTEamsdyKKQLRNLKEEIAVL 123
Cdd:pfam13851  26 ELIKSLKEEIAELKKKEERNEKLMSEIQQENKRlTEP--LQKAQEEV-EELRKQLENYEKD-----KQSLKNLKARLKVL 97


                  ....*...
gi 1034638397 124 SAEKSALQ 131
Cdd:pfam13851  98 EKELKDLK 105
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
2-132 1.67e-03

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 40.67  E-value: 1.67e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638397    2 QQLDSNLNSTRSQCNQVQDDLVETEKNLEESKNRsaisLLAAE-EEINQLKKQLKSLQAQEDARHRNTDQRSSENRR--- 77
Cdd:COG4913    298 EELRAELARLEAELERLEARLDALREELDELEAQ----IRGNGgDRLEQLEREIERLERELEERERRRARLEALLAAlgl 373

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638397   78 SEPWSLEE--RKREQWNSLKQNADQQDTEAMSDY---KKQLRNLKEEIAVLSAEKSALQG 132
Cdd:COG4913    374 PLPASAEEfaALRAEAAALLEALEEELEALEEALaeaEAALRDLRRELRELEAEIASLER 433
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
 26-118 3.09e-03

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: 39.72  E-value: 3.09e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638397  26 EKNLEESKNrsaisllAAEEEINQLKKQLKSLQAQEDARHRNTDQRSSENRRSEPWSLEERKREQWNSLKQNADQQDTEA 105
Cdd:pfam17380 498 EKELEERKQ-------AMIEEERKRKLLEKEMEERQKAIYEEERRREAEEERRKQQEMEERRRIQEQMRKATEERSRLEA 570

                          90
                  ....*....|...
gi 1034638397 106 MSDYKKQLRNLKE 118
Cdd:pfam17380 571 MEREREMMRQIVE 583
PRK01156 PRK01156
chromosome segregation protein; Provisional
 6-126 3.64e-03

chromosome segregation protein; Provisional


Pssm-ID: 100796 [Multi-domain]  Cd Length: 895  Bit Score: 39.50  E-value: 3.64e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638397   6 SNLNSTRSQCNQVQDDLVETEKNLEE----------SKNRSAISLLAAEEEINQLKKQLKSLQAQEDARHR-NTDQRSSE 74
Cdd:PRK01156  183 SNIDYLEEKLKSSNLELENIKKQIADdekshsitlkEIERLSIEYNNAMDDYNNLKSALNELSSLEDMKNRyESEIKTAE 262

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1034638397  75 NRRSEPW-------SLEERKREQWNSlKQNADQQDTEAMSDYKKQLRNLKEEIAVLSAE 126
Cdd:PRK01156  263 SDLSMELeknnyykELEERHMKIIND-PVYKNRNYINDYFKYKNDIENKKQILSNIDAE 320
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 2-131 4.15e-03

helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.


Pssm-ID: 275316 [Multi-domain]  Cd Length: 745  Bit Score: 39.62  E-value: 4.15e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638397   2 QQLDSNLNST-RSQCNQVQDDLVETEKNLeeSKNRSAISLLaaEEEINQLKKQLKSLQAQEDARHRNTDQRSSE----NR 76
Cdd:TIGR04523 302 NQKEQDWNKElKSELKNQEKKLEEIQNQI--SQNNKIISQL--NEQISQLKKELTNSESENSEKQRELEEKQNEieklKK 377

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1034638397  77 RSEPWSLEERKRE-QWNSLKQNADQQdteamsdyKKQLRNLKEEIAVLSAEKSALQ 131
Cdd:TIGR04523 378 ENQSYKQEIKNLEsQINDLESKIQNQ--------EKLNQQKDEQIKKLQQEKELLE 425
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 2-131 4.18e-03

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 39.53  E-value: 4.18e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638397   2 QQLDSNLNSTRSQCNQVQDDLVETEKNLEESKNRSAISLLAAEEEINQLKKQLKSLQAQEDARHRNTDQRSS-ENRRSEP 80
Cdd:COG1196   319 EELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEaLRAAAEL 398

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1034638397  81 WSLEERKREQWNSLKQNADQQDTEAMSDYKKQLRNLKEEIAVLSAEKSALQ 131
Cdd:COG1196   399 AAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAE 449
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
1-132 4.42e-03

Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 39.23  E-value: 4.42e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638397   1 MQQLDSNLNSTRSQCNQVQDDLVETEKNLEE-----SKNRSAISLLAAEEEINQLKKQLKSLQAQED-ARHRNTDQrsSE 74
Cdd:COG3206   214 AKLLLQQLSELESQLAEARAELAEAEARLAAlraqlGSGPDALPELLQSPVIQQLRAQLAELEAELAeLSARYTPN--HP 291

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1034638397  75 NRRsepwsleeRKREQWNSLKQNADQQDTEAMSDYKKQLRNLKEEIAVLSAEKSALQG 132
Cdd:COG3206   292 DVI--------ALRAQIAALRAQLQQEAQRILASLEAELEALQAREASLQAQLAQLEA 341
PRK11281 PRK11281
mechanosensitive channel MscK;
1-131 4.85e-03

mechanosensitive channel MscK;


Pssm-ID: 236892 [Multi-domain]  Cd Length: 1113  Bit Score: 39.51  E-value: 4.85e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638397    1 MQQLDSNLNSTRSQCNQVQDDLVETEKNLEESKNR-----SAISllAAEEEINQLKKQLKSLQA-QEDARHRNTDQRSSE 74
Cdd:PRK11281   123 LRQLESRLAQTLDQLQNAQNDLAEYNSQLVSLQTQperaqAALY--ANSQRLQQIRNLLKGGKVgGKALRPSQRVLLQAE 200

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1034638397   75 nrrsepWSLEERKREQWNSLKQNADQ-QDTeamsdYKKQLRNLKEEIAVLSAEKSALQ 131
Cdd:PRK11281   201 ------QALLNAQNDLQRKSLEGNTQlQDL-----LQKQRDYLTARIQRLEHQLQLLQ 247
HMMR_N pfam15905
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of ...
 1-123 6.01e-03

Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of eukaryotic hyaluronan-mediated motility receptor proteins. The protein is functionally associated with BRCA1 and thus predicted to be a common, low-penetrance breast cancer candidate.


Pssm-ID: 464932 [Multi-domain]  Cd Length: 329  Bit Score: 38.64  E-value: 6.01e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638397   1 MQQLDSNLNSTRSQCNQVQDDLVETEKNLEESKNRSAiSLLAAEEEINQLKKQ-----LKSLQAQEDARHRNTDQRSSEN 75
Cdd:pfam15905 186 LQVTQKNLEHSKGKVAQLEEKLVSTEKEKIEEKSETE-KLLEYITELSCVSEQvekykLDIAQLEELLKEKNDEIESLKQ 264

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1034638397  76 RRSEPWSLEERKREQWNSLKQNADQQDTEAMSDYKKQLRNLKEEIAVL 123
Cdd:pfam15905 265 SLEEKEQELSKQIKDLNEKCKLLESEKEELLREYEEKEQTLNAELEEL 312
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 2-131 7.94e-03

Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 38.27  E-value: 7.94e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638397   2 QQLDSNLNSTRSQCNQVQDDLVETEKNLEEsknrsaisllaAEEEINQLKKQLKSLQAQ-EDARHRNTDQRSSENRRSEp 80
Cdd:COG3883    19 QAKQKELSELQAELEAAQAELDALQAELEE-----------LNEEYNELQAELEALQAEiDKLQAEIAEAEAEIEERRE- 86

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1034638397  81 wSLEERKREQ---------WNSLKQNADQQD--------TEAMSDYKKQLRNLKEEIAVLSAEKSALQ 131
Cdd:COG3883    87 -ELGERARALyrsggsvsyLDVLLGSESFSDfldrlsalSKIADADADLLEELKADKAELEAKKAELE 153
sbcc TIGR00618
exonuclease SbcC; All proteins in this family for which functions are known are part of an ...
 14-132 9.86e-03

exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]


Pssm-ID: 129705 [Multi-domain]  Cd Length: 1042  Bit Score: 38.41  E-value: 9.86e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638397   14 QCNQvQDDLVETE----KNLEESKNRSAISLLAAEEEINQLKKQLKSLQAQEDARHRNTDQRSSENRRSEPWSLEERKRE 89
Cdd:TIGR00618  304 QIEQ-QAQRIHTElqskMRSRAKLLMKRAAHVKQQSSIEEQRRLLQTLHSQEIHIRDAHEVATSIREISCQQHTLTQHIH 382

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|...
gi 1034638397   90 QWNSLKQnADQQDTEAMSDYKKQLRNLKEEIAVLSAEKSALQG 132
Cdd:TIGR00618  383 TLQQQKT-TLTQKLQSLCKELDILQREQATIDTRTSAFRDLQG 424
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
22-119 9.88e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 38.12  E-value: 9.88e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034638397  22 LVETEKNLEESKNRSAI---SLLAAEEEINQLKKQLKSLQAQEDARHRNTDQRSSENRRSEPWSLE---ERKREQwnsLK 95
Cdd:PRK03918  607 LKDAEKELEREEKELKKleeELDKAFEELAETEKRLEELRKELEELEKKYSEEEYEELREEYLELSrelAGLRAE---LE 683

                          90       100
                  ....*....|....*....|....
gi 1034638397  96 QNADQQDTeamsdYKKQLRNLKEE 119
Cdd:PRK03918  684 ELEKRREE-----IKKTLEKLKEE 702
 
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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