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Conserved domains on  [gi|33991487|gb|AAH14153|]
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ATR interacting protein [Homo sapiens]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Tropomyosin_1 super family cl38368
Tropomyosin like; This family is a set of eukaryotic tropomyosins. Within the yeast Tpm1 and ...
 113-212 1.13e-07

Tropomyosin like; This family is a set of eukaryotic tropomyosins. Within the yeast Tpm1 and Tpm2, biochemical and sequence analyses indicate that Tpm2p spans four actin monomers along a filament, whereas Tpm1p spans five. Despite its shorter length, Tpm2p can compete with Tpm1p for binding to F-actin. Over-expression of Tpm2p in vivo alters the axial budding of haploids to a bipolar pattern, and this can be partially suppressed by co-over-expression of Tpm1p. This suggests distinct functions for the two tropomyosins, and indicates that the ratio between them is important for correct morphogenesis. The family also contains higher eukaryote Tpm3 members.


The actual alignment was detected with superfamily member pfam12718:

Pssm-ID: 403808 [Multi-domain]  Cd Length: 142  Bit Score: 51.54  E-value: 1.13e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33991487   113 ELEVLQAQYKELKEKMKVMEEEVLIKNGEIKILRDSLHQTES---VLEEQRRSHFLLEQEKTQALSDKEKeFSKKLQSLQ 189
Cdd:pfam12718   8 EAENAQERAEELEEKVKELEQENLEKEQEIKSLTHKNQQLEEeveKLEEQLKEAKEKAEESEKLKTNNEN-LTRKIQLLE 86

                          90       100
                  ....*....|....*....|....
gi 33991487   190 SELQFKDAEMNELRTKL-QTSERA 212
Cdd:pfam12718  87 EELEESDKRLKETTEKLrETDVKA 110
 
Name Accession Description Interval E-value
Tropomyosin_1 pfam12718
Tropomyosin like; This family is a set of eukaryotic tropomyosins. Within the yeast Tpm1 and ...
 113-212 1.13e-07

Tropomyosin like; This family is a set of eukaryotic tropomyosins. Within the yeast Tpm1 and Tpm2, biochemical and sequence analyses indicate that Tpm2p spans four actin monomers along a filament, whereas Tpm1p spans five. Despite its shorter length, Tpm2p can compete with Tpm1p for binding to F-actin. Over-expression of Tpm2p in vivo alters the axial budding of haploids to a bipolar pattern, and this can be partially suppressed by co-over-expression of Tpm1p. This suggests distinct functions for the two tropomyosins, and indicates that the ratio between them is important for correct morphogenesis. The family also contains higher eukaryote Tpm3 members.


Pssm-ID: 403808 [Multi-domain]  Cd Length: 142  Bit Score: 51.54  E-value: 1.13e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33991487   113 ELEVLQAQYKELKEKMKVMEEEVLIKNGEIKILRDSLHQTES---VLEEQRRSHFLLEQEKTQALSDKEKeFSKKLQSLQ 189
Cdd:pfam12718   8 EAENAQERAEELEEKVKELEQENLEKEQEIKSLTHKNQQLEEeveKLEEQLKEAKEKAEESEKLKTNNEN-LTRKIQLLE 86

                          90       100
                  ....*....|....*....|....
gi 33991487   190 SELQFKDAEMNELRTKL-QTSERA 212
Cdd:pfam12718  87 EELEESDKRLKETTEKLrETDVKA 110
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
113-212 2.15e-05

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 47.59  E-value: 2.15e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33991487 113 ELEVLQAQYKELKEKMKVMEEEVLIKNGEIKILRDSLHQTESVLEEQRRSHFLLEQEKtQALSDKEKEFSKKLQSLQSEL 192
Cdd:COG4372  46 ELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEEL-ESLQEEAEELQEELEELQKER 124

                        90       100
                ....*....|....*....|
gi 33991487 193 QFKDAEMNELRTKLQTSERA 212
Cdd:COG4372 125 QDLEQQRKQLEAQIAELQSE 144
PRK12704 PRK12704
phosphodiesterase; Provisional
 113-212 2.35e-05

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 47.85  E-value: 2.35e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33991487  113 ELEVLQAQYKELKEKMKvMEEEVLIKNGEIKILRDSLHQTESVLEEQRRshfLLEQEKtQALSDKEKEFSKKLQSLQSEL 192
Cdd:PRK12704  56 KEALLEAKEEIHKLRNE-FEKELRERRNELQKLEKRLLQKEENLDRKLE---LLEKRE-EELEKKEKELEQKQQELEKKE 130

                         90       100
                 ....*....|....*....|....*
gi 33991487  193 QFKDAEMNELRTKLQ-----TSERA 212
Cdd:PRK12704 131 EELEELIEEQLQELErisglTAEEA 155
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 101-211 2.70e-05

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: 47.71  E-value: 2.70e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33991487   101 KNRETvpIKD-NFELEVLQAQYKELKEKMKVMEEEVLIKNGEIKILRDSLHQTESVLEEQRRSHFLLEQEKTQaLSDKEK 179
Cdd:TIGR04523 437 KNNSE--IKDlTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKE-LEEKVK 513

                          90       100       110
                  ....*....|....*....|....*....|..
gi 33991487   180 EFSKKLQSLQSELQFKDAEMNELRTKLQTSER 211
Cdd:TIGR04523 514 DLTKKISSLKEKIEKLESEKKEKESKISDLED 545
OmpH smart00935
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH ...
 115-208 3.80e-05

Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH among others. Skp (OmpH) has been characterized as a molecular chaperone that interacts with unfolded proteins as they emerge in the periplasm from the Sec translocation machinery.


Pssm-ID: 214922 [Multi-domain]  Cd Length: 140  Bit Score: 44.11  E-value: 3.80e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33991487    115 EVLQAQYKELKEKMKVMEEEvlikngeIKILRDSLHQTESVLEEQRRshflleQEKTQALSDKEKEFSKKLQSLQSELQF 194
Cdd:smart00935  21 KQLEKEFKKRQAELEKLEKE-------LQKLKEKLQKDAATLSEAAR------EKKEKELQKKVQEFQRKQQKLQQDLQK 87

                           90
                   ....*....|....*
gi 33991487    195 KDAE-MNELRTKLQT 208
Cdd:smart00935  88 RQQEeLQKILDKINK 102
Prefoldin_alpha cd00584
Prefoldin alpha subunit; Alpha subunits of prefoldin, a hexameric molecular chaperone complex, ...
 113-207 6.52e-05

Prefoldin alpha subunit; Alpha subunits of prefoldin, a hexameric molecular chaperone complex, found in both eukaryotes and archaea. Prefoldin binds and stabilizes newly synthesized polypeptides allowing them to fold correctly. The complex contains two alpha and four beta subunits, the two subunits being evolutionarily related. In archaea, there is usually only one gene for each subunit while in eukaryotes there two or more paralogous genes encoding each subunit adding heterogeneity to the structure of the hexamer. The structure of the complex consists of a double beta barrel assembly with six protruding coiled-coils.


Pssm-ID: 467468 [Multi-domain]  Cd Length: 121  Bit Score: 42.98  E-value: 6.52e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33991487 113 ELEVLQAQYKELKEKMKVMEE---EVLIKNGEIKILRDSLHQTESVLeeqrrSH----FLLEQEKTQA---LSDKEKEFS 182
Cdd:cd00584  21 QLEEEQAEIDEAKEALEELKKegsEVLVPLGGNAYVRAEVVDIDKVI-----VHlglgYYAERDPDGAieiLEKKEDELD 95

                        90       100
                ....*....|....*....|....*
gi 33991487 183 KKLQSLQSELQFKDAEMNELRTKLQ 207
Cdd:cd00584  96 KRIEELQAELAELEDEYDQLEQQAQ 120
 
Name Accession Description Interval E-value
Tropomyosin_1 pfam12718
Tropomyosin like; This family is a set of eukaryotic tropomyosins. Within the yeast Tpm1 and ...
 113-212 1.13e-07

Tropomyosin like; This family is a set of eukaryotic tropomyosins. Within the yeast Tpm1 and Tpm2, biochemical and sequence analyses indicate that Tpm2p spans four actin monomers along a filament, whereas Tpm1p spans five. Despite its shorter length, Tpm2p can compete with Tpm1p for binding to F-actin. Over-expression of Tpm2p in vivo alters the axial budding of haploids to a bipolar pattern, and this can be partially suppressed by co-over-expression of Tpm1p. This suggests distinct functions for the two tropomyosins, and indicates that the ratio between them is important for correct morphogenesis. The family also contains higher eukaryote Tpm3 members.


Pssm-ID: 403808 [Multi-domain]  Cd Length: 142  Bit Score: 51.54  E-value: 1.13e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33991487   113 ELEVLQAQYKELKEKMKVMEEEVLIKNGEIKILRDSLHQTES---VLEEQRRSHFLLEQEKTQALSDKEKeFSKKLQSLQ 189
Cdd:pfam12718   8 EAENAQERAEELEEKVKELEQENLEKEQEIKSLTHKNQQLEEeveKLEEQLKEAKEKAEESEKLKTNNEN-LTRKIQLLE 86

                          90       100
                  ....*....|....*....|....
gi 33991487   190 SELQFKDAEMNELRTKL-QTSERA 212
Cdd:pfam12718  87 EELEESDKRLKETTEKLrETDVKA 110
OmpH pfam03938
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH ...
 118-207 4.12e-06

Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH among others. Skp (OmpH) has been characterized as a molecular chaperone that interacts with unfolded proteins as they emerge in the periplasm from the Sec translocation machinery.


Pssm-ID: 461098 [Multi-domain]  Cd Length: 140  Bit Score: 46.80  E-value: 4.12e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33991487   118 QAQyKELKEKMKVMEEEVLIKNGEIKILRDSLHQTESVLEEQRrshflleQEKTQALSDKEKEFSKKLQSLQSELQFKDA 197
Cdd:pfam03938  19 AAQ-AQLEKKFKKRQAELEAKQKELQKLYEELQKDGALLEEER-------EEKEQELQKKEQELQQLQQKAQQELQKKQQ 90

                          90
                  ....*....|.
gi 33991487   198 E-MNELRTKLQ 207
Cdd:pfam03938  91 ElLQPIQDKIN 101
ERM_helical pfam20492
Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related ...
 120-212 1.78e-05

Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related proteins, ezrin, radixin and moesin. Ezrin was first identified as a constituent of microvilli, radixin as a barbed, end-capping actin-modulating protein from isolated junctional fractions, and moesin as a heparin binding protein. A tumour suppressor molecule responsible for neurofibromatosis type 2 (NF2) is highly similar to ERM proteins and has been designated merlin (moesin-ezrin-radixin-like protein). ERM molecules contain 3 domains, an N-terminal globular domain, an extended alpha-helical domain and a charged C-terminal domain (pfam00769). Ezrin, radixin and merlin also contain a polyproline linker region between the helical and C-terminal domains. The N-terminal domain is highly conserved and is also found in merlin, band 4.1 proteins and members of the band 4.1 superfamily, designated the FERM domain. ERM proteins crosslink actin filaments with plasma membranes. They co-localize with CD44 at actin filament plasma membrane interaction sites, associating with CD44 via their N-terminal domains and with actin filaments via their C-terminal domains. This is the alpha-helical domain, which is involved in intramolecular masking of protein-protein interaction sites, regulating the activity of this proteins.


Pssm-ID: 466641 [Multi-domain]  Cd Length: 120  Bit Score: 44.52  E-value: 1.78e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33991487   120 QYKELKEKMKVMEEEVLIKNGEikiLRDSlHQTESVLEEQRR----SHFLLEQEKTQAL------------SDKEK---- 179
Cdd:pfam20492   7 EKQELEERLKQYEEETKKAQEE---LEES-EETAEELEEERRqaeeEAERLEQKRQEAEeekerleesaemEAEEKeqle 82

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 33991487   180 ----EFSKKLQSLQSELQFKDAEMNELRTKLQTSERA 212
Cdd:pfam20492  83 aelaEAQEEIARLEEEVERKEEEARRLQEELEEAREE 119
Prefoldin_2 pfam01920
Prefoldin subunit; This family includes prefoldin subunits that are not detected by pfam02996.
 113-207 1.89e-05

Prefoldin subunit; This family includes prefoldin subunits that are not detected by pfam02996.


Pssm-ID: 396482 [Multi-domain]  Cd Length: 102  Bit Score: 44.14  E-value: 1.89e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33991487   113 ELEVLQAQYKELKEKMKVMEEEVliknGEIKILRDSLhqteSVLEEQRRSHF-----LLEQEKTQALSD--KEKEF-SKK 184
Cdd:pfam01920   3 KFQQLQQQLQLLAQQIKQLETQL----KELELALEEL----ELLDEDTKVYKligdvLVKQDKEEVKEQleERKETlEKE 74

                          90       100
                  ....*....|....*....|...
gi 33991487   185 LQSLQSELQFKDAEMNELRTKLQ 207
Cdd:pfam01920  75 IKTLEKQLEKLEKELEELKEELY 97
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
113-212 2.15e-05

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 47.59  E-value: 2.15e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33991487 113 ELEVLQAQYKELKEKMKVMEEEVLIKNGEIKILRDSLHQTESVLEEQRRSHFLLEQEKtQALSDKEKEFSKKLQSLQSEL 192
Cdd:COG4372  46 ELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEEL-ESLQEEAEELQEELEELQKER 124

                        90       100
                ....*....|....*....|
gi 33991487 193 QFKDAEMNELRTKLQTSERA 212
Cdd:COG4372 125 QDLEQQRKQLEAQIAELQSE 144
PRK12704 PRK12704
phosphodiesterase; Provisional
 113-212 2.35e-05

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 47.85  E-value: 2.35e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33991487  113 ELEVLQAQYKELKEKMKvMEEEVLIKNGEIKILRDSLHQTESVLEEQRRshfLLEQEKtQALSDKEKEFSKKLQSLQSEL 192
Cdd:PRK12704  56 KEALLEAKEEIHKLRNE-FEKELRERRNELQKLEKRLLQKEENLDRKLE---LLEKRE-EELEKKEKELEQKQQELEKKE 130

                         90       100
                 ....*....|....*....|....*
gi 33991487  193 QFKDAEMNELRTKLQ-----TSERA 212
Cdd:PRK12704 131 EELEELIEEQLQELErisglTAEEA 155
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 101-211 2.70e-05

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: 47.71  E-value: 2.70e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33991487   101 KNRETvpIKD-NFELEVLQAQYKELKEKMKVMEEEVLIKNGEIKILRDSLHQTESVLEEQRRSHFLLEQEKTQaLSDKEK 179
Cdd:TIGR04523 437 KNNSE--IKDlTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKE-LEEKVK 513

                          90       100       110
                  ....*....|....*....|....*....|..
gi 33991487   180 EFSKKLQSLQSELQFKDAEMNELRTKLQTSER 211
Cdd:TIGR04523 514 DLTKKISSLKEKIEKLESEKKEKESKISDLED 545
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 107-212 3.19e-05

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: 47.74  E-value: 3.19e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33991487    107 PIKDNFELEVLQAQYKELKEKMKVMEEEVLIKNGEIKILRDSLHQTESVLEEQRRSHFLLEQEKTQaLSDKEKEFSKKLQ 186
Cdd:TIGR02168  332 LDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIAS-LNNEIERLEARLE 410

                           90       100
                   ....*....|....*....|....*.
gi 33991487    187 SLQSELQFKDAEMNELRTKLQTSERA 212
Cdd:TIGR02168  411 RLEDRRERLQQEIEELLKKLEEAELK 436
COG1340 COG1340
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
115-206 3.36e-05

Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];


Pssm-ID: 440951 [Multi-domain]  Cd Length: 297  Bit Score: 46.44  E-value: 3.36e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33991487 115 EVLQAQYKELKEKMKVMEEEVliknGEIKILRDSLHQTESVLEEQRRShfLLEQ-----EKTQALSDKEKEFSKKLQSLQ 189
Cdd:COG1340   4 DELSSSLEELEEKIEELREEI----EELKEKRDELNEELKELAEKRDE--LNAQvkelrEEAQELREKRDELNEKVKELK 77

                        90
                ....*....|....*..
gi 33991487 190 SELQFKDAEMNELRTKL 206
Cdd:COG1340  78 EERDELNEKLNELREEL 94
OmpH smart00935
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH ...
 115-208 3.80e-05

Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH among others. Skp (OmpH) has been characterized as a molecular chaperone that interacts with unfolded proteins as they emerge in the periplasm from the Sec translocation machinery.


Pssm-ID: 214922 [Multi-domain]  Cd Length: 140  Bit Score: 44.11  E-value: 3.80e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33991487    115 EVLQAQYKELKEKMKVMEEEvlikngeIKILRDSLHQTESVLEEQRRshflleQEKTQALSDKEKEFSKKLQSLQSELQF 194
Cdd:smart00935  21 KQLEKEFKKRQAELEKLEKE-------LQKLKEKLQKDAATLSEAAR------EKKEKELQKKVQEFQRKQQKLQQDLQK 87

                           90
                   ....*....|....*
gi 33991487    195 KDAE-MNELRTKLQT 208
Cdd:smart00935  88 RQQEeLQKILDKINK 102
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
113-211 4.59e-05

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 46.43  E-value: 4.59e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33991487 113 ELEVLQAQYKELKEKMKVMEEEVLIKNGEIKILRDSLHQTESVLEEqrrshflLEQEKtQALSDKEKEFSKKLQSLQSEL 192
Cdd:COG4372  74 ELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEE-------LQKER-QDLEQQRKQLEAQIAELQSEI 145

                        90
                ....*....|....*....
gi 33991487 193 QFKDAEMNELRTKLQTSER 211
Cdd:COG4372 146 AEREEELKELEEQLESLQE 164
Prefoldin_alpha cd00584
Prefoldin alpha subunit; Alpha subunits of prefoldin, a hexameric molecular chaperone complex, ...
 113-207 6.52e-05

Prefoldin alpha subunit; Alpha subunits of prefoldin, a hexameric molecular chaperone complex, found in both eukaryotes and archaea. Prefoldin binds and stabilizes newly synthesized polypeptides allowing them to fold correctly. The complex contains two alpha and four beta subunits, the two subunits being evolutionarily related. In archaea, there is usually only one gene for each subunit while in eukaryotes there two or more paralogous genes encoding each subunit adding heterogeneity to the structure of the hexamer. The structure of the complex consists of a double beta barrel assembly with six protruding coiled-coils.


Pssm-ID: 467468 [Multi-domain]  Cd Length: 121  Bit Score: 42.98  E-value: 6.52e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33991487 113 ELEVLQAQYKELKEKMKVMEE---EVLIKNGEIKILRDSLHQTESVLeeqrrSH----FLLEQEKTQA---LSDKEKEFS 182
Cdd:cd00584  21 QLEEEQAEIDEAKEALEELKKegsEVLVPLGGNAYVRAEVVDIDKVI-----VHlglgYYAERDPDGAieiLEKKEDELD 95

                        90       100
                ....*....|....*....|....*
gi 33991487 183 KKLQSLQSELQFKDAEMNELRTKLQ 207
Cdd:cd00584  96 KRIEELQAELAELEDEYDQLEQQAQ 120
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 113-214 1.84e-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: 45.05  E-value: 1.84e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33991487    113 ELEVLQAQYKELKEKMKVMEEEVLI--------------KNGEIKILRDSLHQTESVLEEQRRSHFLLEQEKtQALSDKE 178
Cdd:TIGR02168  261 ELQELEEKLEELRLEVSELEEEIEElqkelyalaneisrLEQQKQILRERLANLERQLEELEAQLEELESKL-DELAEEL 339

                           90       100       110
                   ....*....|....*....|....*....|....*.
gi 33991487    179 KEFSKKLQSLQSELQFKDAEMNELRTKLQTSERANK 214
Cdd:TIGR02168  340 AELEEKLEELKEELESLEAELEELEAELEELESRLE 375
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 113-218 5.04e-04

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 43.77  E-value: 5.04e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33991487 113 ELEVLQAQYKELKEKMKVMEEEVLIKNGEIKILRDSLHQTESVLEEQRRSHFLLEQEKTQALSDKE------KEFSKKLQ 186
Cdd:COG1196 240 ELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIArleerrRELEERLE 319

                        90       100       110
                ....*....|....*....|....*....|..
gi 33991487 187 SLQSELQFKDAEMNELRTKLQTSERANKLAAP 218
Cdd:COG1196 320 ELEEELAELEEELEELEEELEELEEELEEAEE 351
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 101-214 5.33e-04

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: 43.47  E-value: 5.33e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33991487   101 KNRETVPIKDNfELEVLQAQYKELKEKMKVMEEEVLIKNGEIKILRDSLHQTESVLE--EQRRSHFlleQEKTQALSDKE 178
Cdd:TIGR04523 402 NQEKLNQQKDE-QIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKnlDNTRESL---ETQLKVLSRSI 477

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 33991487   179 KEFSKKLQSLQSELQFKDAEMNELRTKLQTSERANK 214
Cdd:TIGR04523 478 NKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVK 513
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 58-210 7.34e-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: 7.34e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33991487     58 DDLEELDTLASQALSQCPAAARDVSSDHKVHRLLDG-MSKNPSGKNRETvpikdnFELEVLQAQYKELKEKMKVMEEEVL 136
Cdd:TIGR02168  782 AEIEELEAQIEQLKEELKALREALDELRAELTLLNEeAANLRERLESLE------RRIAATERRLEDLEEQIEELSEDIE 855

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 33991487    137 IKNGEIKILRDSLHQTES---VLEEQRRSHflleQEKTQALSDKEKEFSKKLQSLQSELQFKDAEMNELRTKLQTSE 210
Cdd:TIGR02168  856 SLAAEIEELEELIEELESeleALLNERASL----EEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLE 928
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 108-206 1.25e-03

Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];


Pssm-ID: 441187 [Multi-domain]  Cd Length: 236  Bit Score: 41.06  E-value: 1.25e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33991487 108 IKDNFELEVLQAQYKELKEKMKVMEEEVLIKNGEIKILRDSLHQTESVLEEQRrshflleqektQALSDKEKEFSKKLQS 187
Cdd:COG1579  85 VRNNKEYEALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELE-----------AELEEKKAELDEELAE 153

                        90
                ....*....|....*....
gi 33991487 188 LQSELQFKDAEMNELRTKL 206
Cdd:COG1579 154 LEAELEELEAEREELAAKI 172
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
113-210 1.61e-03

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 42.06  E-value: 1.61e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33991487 113 ELEVLQAQYKELKEKMKVMEEevLIKngEIKILRDSLHQTESVLEEQRRSHFLLEQEKTQALSDKEKEFSKKLQSLQSEL 192
Cdd:COG4717 140 ELAELPERLEELEERLEELRE--LEE--ELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEEL 215

                        90
                ....*....|....*...
gi 33991487 193 QFKDAEMNELRTKLQTSE 210
Cdd:COG4717 216 EEAQEELEELEEELEQLE 233
rad50 TIGR00606
rad50; All proteins in this family for which functions are known are involvedin recombination, ...
 54-214 2.18e-03

rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).


Pssm-ID: 129694 [Multi-domain]  Cd Length: 1311  Bit Score: 41.57  E-value: 2.18e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33991487     54 DFTADDLEELDTLASQaLSQCPAAARDVSSDHKVHRlldgmSKNPSGKNRETVpIKDNFELEVLQAQYKELKEKMKVMEE 133
Cdd:TIGR00606  970 DYLKQKETELNTVNAQ-LEECEKHQEKINEDMRLMR-----QDIDTQKIQERW-LQDNLTLRKRENELKEVEEELKQHLK 1042

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33991487    134 EVliknGEIKILRdsLHQTESVLEEQRRshfLLEQEKTQALSdKEKEFSKKLQSLQSEL---QFKDAEMN--ELRTKLQT 208
Cdd:TIGR00606 1043 EM----GQMQVLQ--MKQEHQKLEENID---LIKRNHVLALG-RQKGYEKEIKHFKKELrepQFRDAEEKyrEMMIVMRT 1112


                   ....*.
gi 33991487    209 SERANK 214
Cdd:TIGR00606 1113 TELVNK 1118
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
117-214 2.48e-03

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 41.04  E-value: 2.48e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33991487 117 LQAQYKELKEKMKVMEEEVLIKNGEIKILRDSLHQTESVLEEQRRshfllEQEKTQA-LSDKEKEFSKKLQSL---QSEL 192
Cdd:COG4372  29 LSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARS-----ELEQLEEeLEELNEQLQAAQAELaqaQEEL 103

                        90       100
                ....*....|....*....|..
gi 33991487 193 QFKDAEMNELRTKLQTSERANK 214
Cdd:COG4372 104 ESLQEEAEELQEELEELQKERQ 125
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
109-206 2.86e-03

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 41.05  E-value: 2.86e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33991487  109 KDNFELEVLQAQYKELKEKMKVMEEEVLIKNGEIKILRDSLHQTESVLEEQRR------------SHFLLEQEKTQALSD 176
Cdd:COG4913  682 ASSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDrleaaedlarleLRALLEERFAAALGD 761

                         90       100       110
                 ....*....|....*....|....*....|.
gi 33991487  177 K-EKEFSKKLQSLQSELQfkdAEMNELRTKL 206
Cdd:COG4913  762 AvERELRENLEERIDALR---ARLNRAEEEL 789
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
113-211 3.31e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 40.82  E-value: 3.31e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33991487  113 ELEVLQAQYKEL---KEKMKVMEEEVLIKNGEIKILRDSLHQTESVLEEQR-RSHFLLEQEK------------------ 170
Cdd:PRK03918 222 ELEKLEKEVKELeelKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKkEIEELEEKVKelkelkekaeeyiklsef 301

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 33991487  171 ----TQALSDKEKEFSK---KLQSLQ---SELQFKDAEMNELRTKLQTSER 211
Cdd:PRK03918 302 yeeyLDELREIEKRLSRleeEINGIEeriKELEEKEERLEELKKKLKELEK 352
Cast pfam10174
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ...
 120-239 3.76e-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: 40.58  E-value: 3.76e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33991487   120 QYKELKEKMKVMEEEVLIKNGEIKILRDSLHQTESVLEEQRRSHFLLEQEKTQALSD--KE-KEFSKKLQSLQSELQFKD 196
Cdd:pfam10174 416 QLAGLKERVKSLQTDSSNTDTALTTLEEALSEKERIIERLKEQREREDRERLEELESlkKEnKDLKEKVSALQPELTEKE 495

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 33991487   197 AEMNELRtklqtsERANKLAAPSVSHVSPRKNPSVVI--KPEACS 239
Cdd:pfam10174 496 SSLIDLK------EHASSLASSGLKKDSKLKSLEIAVeqKKEECS 534
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 114-226 3.94e-03

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: 40.13  E-value: 3.94e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33991487 114 LEVLQAQYKELKEKMKVME---EEVLIKNGEIKILRDSLHQTESVLEEQRRSHFLLEQEKTQALSDKEKEFSKKLQSLQs 190
Cdd:COG4942 138 LQYLKYLAPARREQAEELRadlAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELA- 216

                        90       100       110
                ....*....|....*....|....*....|....*.
gi 33991487 191 ELQFKDAEMNELRTKLQTSERANKLAAPSVSHVSPR 226
Cdd:COG4942 217 ELQQEAEELEALIARLEAEAAAAAERTPAAGFAALK 252
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 122-210 4.01e-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: 40.81  E-value: 4.01e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33991487    122 KELKEKMKVMEEEVLIKNGEIKILRDSLHQTESVLEEQRRshflLEQEKTQALSDKEKEFSK----------KLQSLQSE 191
Cdd:TIGR02168  680 EELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRK----ELEELSRQISALRKDLARleaeveqleeRIAQLSKE 755

                           90
                   ....*....|....*....
gi 33991487    192 LQFKDAEMNELRTKLQTSE 210
Cdd:TIGR02168  756 LTELEAEIEELEERLEEAE 774
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
113-217 4.05e-03

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 40.52  E-value: 4.05e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33991487 113 ELEVLQAQYKELKEKMKVMEEEVLIKNGEIKILRDSLHQTESVLEEQRRSHF-----LLEQEKTQALSDKEKEFSKKLQS 187
Cdd:COG4717 364 QLEELEQEIAALLAEAGVEDEEELRAALEQAEEYQELKEELEELEEQLEELLgeleeLLEALDEEELEEELEELEEELEE 443

                        90       100       110
                ....*....|....*....|....*....|
gi 33991487 188 LQSELQFKDAEMNELRTKLQTSERANKLAA 217
Cdd:COG4717 444 LEEELEELREELAELEAELEQLEEDGELAE 473
GAS pfam13851
Growth-arrest specific micro-tubule binding; This family is the highly conserved central ...
 109-202 4.16e-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: 39.12  E-value: 4.16e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33991487   109 KDNFELEVLQAQYKELKEKMKVMEEE--VLI-KNGEIKILRDSLH--QTESVLEEQRRSHF---LLEqektqalsdkeke 180
Cdd:pfam13851  82 KDKQSLKNLKARLKVLEKELKDLKWEheVLEqRFEKVERERDELYdkFEAAIQDVQQKTGLknlLLE------------- 148

                          90       100
                  ....*....|....*....|..
gi 33991487   181 fsKKLQSLQSELQFKDAEMNEL 202
Cdd:pfam13851 149 --KKLQALGETLEKKEAQLNEV 168
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 113-212 5.24e-03

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 40.31  E-value: 5.24e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33991487 113 ELEVLQAQYKELKEKMKVMEEEVLIKNGEIKILRDSLHQTESVLEEQRRSHFLLEQEKTQALSDkEKEFSKKLQSLQSEL 192
Cdd:COG1196 226 EAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAE-EYELLAELARLEQDI 304

                        90       100
                ....*....|....*....|
gi 33991487 193 QFKDAEMNELRTKLQTSERA 212
Cdd:COG1196 305 ARLEERRRELEERLEELEEE 324
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
117-235 6.65e-03

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


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 40.00  E-value: 6.65e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33991487 117 LQAQYKELKEKMKVMEEEVLIkngEIKILRDSLHQTESVLEEQrrshflLEQEKTQALSDKEKEfsKKLQSLQSELQFKD 196
Cdd:COG3206 296 LRAQIAALRAQLQQEAQRILA---SLEAELEALQAREASLQAQ------LAQLEARLAELPELE--AELRRLEREVEVAR 364

                        90       100       110
                ....*....|....*....|....*....|....*....
gi 33991487 197 AEMNELRTKLQTSERANKLAAPSVSHVSPRKNPSVVIKP 235
Cdd:COG3206 365 ELYESLLQRLEEARLAEALTVGNVRVIDPAVVPLKPVSP 403
Atg16_CCD cd22887
Coiled-coiled domain of autophagy-related 16 (Atg16) family proteins; The Atg16 family ...
 113-169 8.08e-03

Coiled-coiled domain of autophagy-related 16 (Atg16) family proteins; The Atg16 family includes Saccharomyces cerevisiae Atg16 (also called cytoplasm to vacuole targeting protein 11, CVT11, or SAP18), human autophagy-related protein 16-1 (also called APG16-like 1, ATG16L1, or APG16L) and autophagy-related protein 16-2 (also called APG16-like 2, ATG16L2, WD repeat-containing protein 80 or WDR80), and similar proteins. Atg16 stabilizes the Atg5-Atg12 conjugate and mediates the formation of the 350 kDa complex, which is necessary for autophagy. The Atg5-Atg12/Atg16 complex is required for efficient promotion of Atg8-conjugation to phosphatidylethanolamine and Atg8 localization to the pre-autophagosomal structure (PAS). Similarly, human ATG16L1 plays an essential role in autophagy and acts as a molecular scaffold which mediates protein-protein interactions essential for autophagosome formation. ATG16L2, though structurally similar to ATG16L1 and able to form a complex with the autophagy proteins Atg5 and Atg12, is not essential for autophagy. Single-nucleotide polymorphisms in ATG16L1 is associated with an increased risk of developing Crohn disease. Saccharomyces cerevisiae Atg16 contains an N-terminal domain (NTD) that interacts with the Atg5-Atg12 protein conjugate and a coiled-coil domain (CCD) that dimerizes and mediates self-assembly. Human ATG16L1 and ATG16L2 also contains an N-terminal region that binds Atg5, a CCD homologous to the yeast CCD, and a WD40 domain that represents approximately 50% of the full-length protein. This model corresponds to the CCD of Atg16 family proteins.


Pssm-ID: 439196 [Multi-domain]  Cd Length: 91  Bit Score: 36.39  E-value: 8.08e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 33991487 113 ELEVLQAQYKELKEKMKVMEEEVLIKNGEIKILRD---SLHQTESVLEEQRRShflLEQE 169
Cdd:cd22887  12 RLAELEAELASLEEEIKDLEEELKEKNKANEILNDeliALQIENNLLEEKLRK---LQEE 68
DUF4670 pfam15709
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ...
 117-216 8.24e-03

Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins in this family are typically between 373 and 763 amino acids in length.


Pssm-ID: 464815 [Multi-domain]  Cd Length: 522  Bit Score: 39.55  E-value: 8.24e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33991487   117 LQAQYKELKEKMKV-MEEEVLIKNGEIKILRDSLHQTESVLEEQRRSHFLLEQEKTQALSDKEKEFSKKLQSLQSELQFK 195
Cdd:pfam15709 363 LQQEQLERAEKMREeLELEQQRRFEEIRLRKQRLEEERQRQEEEERKQRLQLQAAQERARQQQEEFRRKLQELQRKKQQE 442

                          90       100
                  ....*....|....*....|....*..
gi 33991487   196 D---AEMNELRTK---LQTSERANKLA 216
Cdd:pfam15709 443 EaerAEAEKQRQKeleMQLAEEQKRLM 469
sbcc TIGR00618
exonuclease SbcC; All proteins in this family for which functions are known are part of an ...
 113-217 8.67e-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: 39.57  E-value: 8.67e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33991487    113 ELEVLQAQYKELKEkmkVMEEEVLIKNGEIKILRDSLHQTESVLEEQRRSHFLL--EQEKTQALSDKEKEFSKKLQSLQs 190
Cdd:TIGR00618  195 KAELLTLRSQLLTL---CTPCMPDTYHERKQVLEKELKHLREALQQTQQSHAYLtqKREAQEEQLKKQQLLKQLRARIE- 270

                           90       100
                   ....*....|....*....|....*..
gi 33991487    191 ELQFKDAEMNELRTKLQTSERANKLAA 217
Cdd:TIGR00618  271 ELRAQEAVLEETQERINRARKAAPLAA 297
 
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.
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