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Conserved domains on  [gi|1239950402|ref|XP_022262475|]
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ATR-interacting protein isoform X3 [Canis lupus familiaris]

Protein Classification

OmpH family outer membrane protein( domain architecture ID 12048616)

OmpH family outer membrane protein may play an active role either as folding catalysts or as chaperones in extracytoplasmic compartments; similar to Flavobacterium psychrophilum outer membrane protein P18

Gene Ontology:  GO:0051082|GO:0016020
PubMed:  2318304

Graphical summary

 Zoom to residue level

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List of domain hits

 Name Accession Description Interval E-value
OmpH pfam03938
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH ...
 121-206 2.47e-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: 47.19  E-value: 2.47e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239950402 121 KELKEKMKAMEEEVLIKNGEIKILRDSLHQTESILEEQRrshflleQEKTQALGDKEKEFSKKLQSLQSELQFKDAE-MN 199
Cdd:pfam03938  22 AQLEKKFKKRQAELEAKQKELQKLYEELQKDGALLEEER-------EEKEQELQKKEQELQQLQQKAQQELQKKQQElLQ 94


                  ....*..
gi 1239950402 200 ELRTKLQ 206
Cdd:pfam03938  95 PIQDKIN 101
CCDC22 super family cl25503
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 ...
 39-187 2.96e-03

Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 (CCDC22) is involved in regulation of NF-kappa-B signalling; the function may involve association with COMMD8 and a CUL1-dependent E3 ubiquitin ligase complex. It is part of the OMMD/CCDC22/CCDC93 (CCC) complex, which interacts with the multisubunit WASH complex required for endosomal deposition of F-actin and cargo trafficking in conjunction with the retromer. This entry also includes CCDC22 homologs from animals and plants.


The actual alignment was detected with superfamily member pfam05667:

Pssm-ID: 461708 [Multi-domain]  Cd Length: 600  Bit Score: 40.40  E-value: 2.96e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239950402  39 AAAVPDPEDPFGAHGDftADDLEELDTLASQALSQCQAAARDTSNVH-------KVPRLDGMSKTPAGKNRELVPVKDNF 111
Cdd:pfam05667 258 SAALAGTEATSGASRS--AQDLAELLSSFSGSSTTDTGLTKGSRFTHteklqftNEAPAATSSPPTKVETEEELQQQREE 335

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239950402 112 ELEVLQTQYKELKEKMKAMEEevlikngEIKILRDSLHQTESILEEQRRSHFLLEQE---KTQALG--DKEKEFSKKLQS 186
Cdd:pfam05667 336 ELEELQEQLEDLESSIQELEK-------EIKKLESSIKQVEEELEELKEQNEELEKQykvKKKTLDllPDAEENIAKLQA 408


                  .
gi 1239950402 187 L 187
Cdd:pfam05667 409 L 409
 
Name Accession Description Interval E-value
OmpH pfam03938
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH ...
 121-206 2.47e-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: 47.19  E-value: 2.47e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239950402 121 KELKEKMKAMEEEVLIKNGEIKILRDSLHQTESILEEQRrshflleQEKTQALGDKEKEFSKKLQSLQSELQFKDAE-MN 199
Cdd:pfam03938  22 AQLEKKFKKRQAELEAKQKELQKLYEELQKDGALLEEER-------EEKEQELQKKEQELQQLQQKAQQELQKKQQElLQ 94


                  ....*..
gi 1239950402 200 ELRTKLQ 206
Cdd:pfam03938  95 PIQDKIN 101
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
112-210 1.16e-05

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 47.59  E-value: 1.16e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239950402 112 ELEVLQTQYKELKEKMKAMEEEVLIKNGEIKILRDSLHQTESILEEqrrshflLEQEKtQALGDKEKEFSKKLQSLQSEL 191
Cdd:COG4372    74 ELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEE-------LQKER-QDLEQQRKQLEAQIAELQSEI 145

                          90
                  ....*....|....*....
gi 1239950402 192 QFKDAEMNELRTKLQSSER 210
Cdd:COG4372   146 AEREEELKELEEQLESLQE 164
OmpH smart00935
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH ...
 93-206 2.24e-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: 44.50  E-value: 2.24e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239950402   93 MSKTPAGKNRElvpvkdnfelEVLQTQYKELKEKMKAMEEEvlikngeIKILRDSLHQTESILEEQRRshflleQEKTQA 172
Cdd:smart00935  10 LQESPAGKAAQ----------KQLEKEFKKRQAELEKLEKE-------LQKLKEKLQKDAATLSEAAR------EKKEKE 66

                           90       100       110
                   ....*....|....*....|....*....|....*
gi 1239950402  173 LGDKEKEFSKKLQSLQSELQFKDAE-MNELRTKLQ 206
Cdd:smart00935  67 LQKKVQEFQRKQQKLQQDLQKRQQEeLQKILDKIN 101
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 108-211 2.61e-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: 47.36  E-value: 2.61e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239950402  108 KDNFELEVLQTQYKELKEKMKAMEEEVLIKNGEIKILRDSLHQTESILEEQRRSHFLLEQEKTQALGDKEkEFSKKLQSL 187
Cdd:TIGR02168  334 ELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIE-RLEARLERL 412

                           90       100
                   ....*....|....*....|....
gi 1239950402  188 QSELQFKDAEMNELRTKLQSSERA 211
Cdd:TIGR02168  413 EDRRERLQQEIEELLKKLEEAELK 436
PRK12704 PRK12704
phosphodiesterase; Provisional
 112-206 1.15e-04

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 44.77  E-value: 1.15e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239950402 112 ELEVLQTQYKELKEKMKaMEEEVLIKNGEIKILRDSLHQTESILEEQRRshfLLEQEKtQALGDKEKEFSKKLQSLQSel 191
Cdd:PRK12704   56 KEALLEAKEEIHKLRNE-FEKELRERRNELQKLEKRLLQKEENLDRKLE---LLEKRE-EELEKKEKELEQKQQELEK-- 128

                          90
                  ....*....|....*
gi 1239950402 192 qfKDAEMNELRTKLQ 206
Cdd:PRK12704  129 --KEEELEELIEEQL 141
Prefoldin_alpha cd00584
Prefoldin alpha subunit; Alpha subunits of prefoldin, a hexameric molecular chaperone complex, ...
 112-207 1.92e-04

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: 41.44  E-value: 1.92e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239950402 112 ELEVLQTQYKELKEKMKAMEE---EVLIKNGEIKILRDSLHQTESILeeqrrSH----FLLEQEKTQA---LGDKEKEFS 181
Cdd:cd00584    21 QLEEEQAEIDEAKEALEELKKegsEVLVPLGGNAYVRAEVVDIDKVI-----VHlglgYYAERDPDGAieiLEKKEDELD 95

                          90       100
                  ....*....|....*....|....*.
gi 1239950402 182 KKLQSLQSELQFKDAEMNELRTKLQS 207
Cdd:cd00584    96 KRIEELQAELAELEDEYDQLEQQAQQ 121
CCDC22 pfam05667
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 ...
 39-187 2.96e-03

Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 (CCDC22) is involved in regulation of NF-kappa-B signalling; the function may involve association with COMMD8 and a CUL1-dependent E3 ubiquitin ligase complex. It is part of the OMMD/CCDC22/CCDC93 (CCC) complex, which interacts with the multisubunit WASH complex required for endosomal deposition of F-actin and cargo trafficking in conjunction with the retromer. This entry also includes CCDC22 homologs from animals and plants.


Pssm-ID: 461708 [Multi-domain]  Cd Length: 600  Bit Score: 40.40  E-value: 2.96e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239950402  39 AAAVPDPEDPFGAHGDftADDLEELDTLASQALSQCQAAARDTSNVH-------KVPRLDGMSKTPAGKNRELVPVKDNF 111
Cdd:pfam05667 258 SAALAGTEATSGASRS--AQDLAELLSSFSGSSTTDTGLTKGSRFTHteklqftNEAPAATSSPPTKVETEEELQQQREE 335

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239950402 112 ELEVLQTQYKELKEKMKAMEEevlikngEIKILRDSLHQTESILEEQRRSHFLLEQE---KTQALG--DKEKEFSKKLQS 186
Cdd:pfam05667 336 ELEELQEQLEDLESSIQELEK-------EIKKLESSIKQVEEELEELKEQNEELEKQykvKKKTLDllPDAEENIAKLQA 408


                  .
gi 1239950402 187 L 187
Cdd:pfam05667 409 L 409
 
Name Accession Description Interval E-value
OmpH pfam03938
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH ...
 121-206 2.47e-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: 47.19  E-value: 2.47e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239950402 121 KELKEKMKAMEEEVLIKNGEIKILRDSLHQTESILEEQRrshflleQEKTQALGDKEKEFSKKLQSLQSELQFKDAE-MN 199
Cdd:pfam03938  22 AQLEKKFKKRQAELEAKQKELQKLYEELQKDGALLEEER-------EEKEQELQKKEQELQQLQQKAQQELQKKQQElLQ 94


                  ....*..
gi 1239950402 200 ELRTKLQ 206
Cdd:pfam03938  95 PIQDKIN 101
Tropomyosin_1 pfam12718
Tropomyosin like; This family is a set of eukaryotic tropomyosins. Within the yeast Tpm1 and ...
 112-209 2.90e-06

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: 46.91  E-value: 2.90e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239950402 112 ELEVLQTQYKELKEKMKAMEEEVLIKNGEIKILRDSLHQTES---ILEEQRRSHFLLEQEKTQALGDKEKeFSKKLQSLQ 188
Cdd:pfam12718   8 EAENAQERAEELEEKVKELEQENLEKEQEIKSLTHKNQQLEEeveKLEEQLKEAKEKAEESEKLKTNNEN-LTRKIQLLE 86

                          90       100
                  ....*....|....*....|.
gi 1239950402 189 SELQFKDAEMNELRTKLQSSE 209
Cdd:pfam12718  87 EELEESDKRLKETTEKLRETD 107
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
112-210 1.16e-05

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 47.59  E-value: 1.16e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239950402 112 ELEVLQTQYKELKEKMKAMEEEVLIKNGEIKILRDSLHQTESILEEqrrshflLEQEKtQALGDKEKEFSKKLQSLQSEL 191
Cdd:COG4372    74 ELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEE-------LQKER-QDLEQQRKQLEAQIAELQSEI 145

                          90
                  ....*....|....*....
gi 1239950402 192 QFKDAEMNELRTKLQSSER 210
Cdd:COG4372   146 AEREEELKELEEQLESLQE 164
OmpH smart00935
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH ...
 93-206 2.24e-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: 44.50  E-value: 2.24e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239950402   93 MSKTPAGKNRElvpvkdnfelEVLQTQYKELKEKMKAMEEEvlikngeIKILRDSLHQTESILEEQRRshflleQEKTQA 172
Cdd:smart00935  10 LQESPAGKAAQ----------KQLEKEFKKRQAELEKLEKE-------LQKLKEKLQKDAATLSEAAR------EKKEKE 66

                           90       100       110
                   ....*....|....*....|....*....|....*
gi 1239950402  173 LGDKEKEFSKKLQSLQSELQFKDAE-MNELRTKLQ 206
Cdd:smart00935  67 LQKKVQEFQRKQQKLQQDLQKRQQEeLQKILDKIN 101
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 108-211 2.61e-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: 47.36  E-value: 2.61e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239950402  108 KDNFELEVLQTQYKELKEKMKAMEEEVLIKNGEIKILRDSLHQTESILEEQRRSHFLLEQEKTQALGDKEkEFSKKLQSL 187
Cdd:TIGR02168  334 ELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIE-RLEARLERL 412

                           90       100
                   ....*....|....*....|....
gi 1239950402  188 QSELQFKDAEMNELRTKLQSSERA 211
Cdd:TIGR02168  413 EDRRERLQQEIEELLKKLEEAELK 436
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 115-207 4.35e-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: 46.55  E-value: 4.35e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239950402 115 VLQTQYKELKEKMKAMEEEVLIKNGEIKILRDSLHQTESILEEQRRSHFLLEQEKTQA------LGDKEKEFSKKLQSLQ 188
Cdd:TIGR04523 451 VKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELeekvkdLTKKISSLKEKIEKLE 530

                          90
                  ....*....|....*....
gi 1239950402 189 SELQFKDAEMNELRTKLQS 207
Cdd:TIGR04523 531 SEKKEKESKISDLEDELNK 549
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
112-211 4.65e-05

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 46.05  E-value: 4.65e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239950402 112 ELEVLQTQYKELKEKMKAMEEEVLIKNGEIKILRDSLHQTESILEEQRRSHFLLEQEKtQALGDKEKEFSKKLQSLQSEL 191
Cdd:COG4372    46 ELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEEL-ESLQEEAEELQEELEELQKER 124

                          90       100
                  ....*....|....*....|
gi 1239950402 192 QFKDAEMNELRTKLQSSERA 211
Cdd:COG4372   125 QDLEQQRKQLEAQIAELQSE 144
Prefoldin_2 pfam01920
Prefoldin subunit; This family includes prefoldin subunits that are not detected by pfam02996.
 117-206 6.25e-05

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


Pssm-ID: 396482 [Multi-domain]  Cd Length: 102  Bit Score: 42.21  E-value: 6.25e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239950402 117 QTQYKELKEKMKAMEEEVLIKNGEIKILRDSLHQTESiLEEQRRSHF-----LLEQEK---TQALGDKEKEFSKKLQSLQ 188
Cdd:pfam01920   1 INKFQQLQQQLQLLAQQIKQLETQLKELELALEELEL-LDEDTKVYKligdvLVKQDKeevKEQLEERKETLEKEIKTLE 79

                          90
                  ....*....|....*...
gi 1239950402 189 SELQFKDAEMNELRTKLQ 206
Cdd:pfam01920  80 KQLEKLEKELEELKEELY 97
PRK12704 PRK12704
phosphodiesterase; Provisional
 112-206 1.15e-04

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 44.77  E-value: 1.15e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239950402 112 ELEVLQTQYKELKEKMKaMEEEVLIKNGEIKILRDSLHQTESILEEQRRshfLLEQEKtQALGDKEKEFSKKLQSLQSel 191
Cdd:PRK12704   56 KEALLEAKEEIHKLRNE-FEKELRERRNELQKLEKRLLQKEENLDRKLE---LLEKRE-EELEKKEKELEQKQQELEK-- 128

                          90
                  ....*....|....*
gi 1239950402 192 qfKDAEMNELRTKLQ 206
Cdd:PRK12704  129 --KEEELEELIEEQL 141
ERM_helical pfam20492
Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related ...
 119-211 1.43e-04

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: 41.44  E-value: 1.43e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239950402 119 QYKELKEKMKAMEEEVLIKNGEikiLRDSlHQTESILEEQRR----SHFLLEQEKTQALGDKEK---------------- 178
Cdd:pfam20492   7 EKQELEERLKQYEEETKKAQEE---LEES-EETAEELEEERRqaeeEAERLEQKRQEAEEEKERleesaemeaeekeqle 82

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1239950402 179 ----EFSKKLQSLQSELQFKDAEMNELRTKLQSSERA 211
Cdd:pfam20492  83 aelaEAQEEIARLEEEVERKEEEARRLQEELEEAREE 119
Prefoldin_alpha cd00584
Prefoldin alpha subunit; Alpha subunits of prefoldin, a hexameric molecular chaperone complex, ...
 112-207 1.92e-04

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: 41.44  E-value: 1.92e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239950402 112 ELEVLQTQYKELKEKMKAMEE---EVLIKNGEIKILRDSLHQTESILeeqrrSH----FLLEQEKTQA---LGDKEKEFS 181
Cdd:cd00584    21 QLEEEQAEIDEAKEALEELKKegsEVLVPLGGNAYVRAEVVDIDKVI-----VHlglgYYAERDPDGAieiLEKKEDELD 95

                          90       100
                  ....*....|....*....|....*.
gi 1239950402 182 KKLQSLQSELQFKDAEMNELRTKLQS 207
Cdd:cd00584    96 KRIEELQAELAELEDEYDQLEQQAQQ 121
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 112-213 2.24e-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: 44.28  E-value: 2.24e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239950402  112 ELEVLQTQYKELKEKMKAMEEEVLI--------------KNGEIKILRDSLHQTESILEEQRRSHFLLEQEKtQALGDKE 177
Cdd:TIGR02168  261 ELQELEEKLEELRLEVSELEEEIEElqkelyalaneisrLEQQKQILRERLANLERQLEELEAQLEELESKL-DELAEEL 339

                           90       100       110
                   ....*....|....*....|....*....|....*.
gi 1239950402  178 KEFSKKLQSLQSELQFKDAEMNELRTKLQSSERANK 213
Cdd:TIGR02168  340 AELEEKLEELKEELESLEAELEELEAELEELESRLE 375
COG1340 COG1340
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
114-217 2.93e-04

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


Pssm-ID: 440951 [Multi-domain]  Cd Length: 297  Bit Score: 42.98  E-value: 2.93e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239950402 114 EVLQTQYKELKEKMKAMEEEVliknGEIKILRDSLHQTESILEEQRRShfLLEQ-----EKTQALGDKEKEFSKKLQSLQ 188
Cdd:COG1340     4 DELSSSLEELEEKIEELREEI----EELKEKRDELNEELKELAEKRDE--LNAQvkelrEEAQELREKRDELNEKVKELK 77

                          90       100       110
                  ....*....|....*....|....*....|.
gi 1239950402 189 SELQFKDAEMNELRTKL--QSSERANKLAAP 217
Cdd:COG1340    78 EERDELNEKLNELREELdeLRKELAELNKAG 108
Cast pfam10174
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ...
 119-233 3.13e-04

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: 43.66  E-value: 3.13e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239950402 119 QYKELKEKMKAMEEEVLIKNGEIKILRDSLHQTESILEEQRRSHFLLEQEKTQALGD--KE-KEFSKKLQSLQSELQFKD 195
Cdd:pfam10174 416 QLAGLKERVKSLQTDSSNTDTALTTLEEALSEKERIIERLKEQREREDRERLEELESlkKEnKDLKEKVSALQPELTEKE 495

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1239950402 196 AEMNELRtklqssERANKLAAPSIPHASPRKSPSVAIK 233
Cdd:pfam10174 496 SSLIDLK------EHASSLASSGLKKDSKLKSLEIAVE 527
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
108-205 3.83e-04

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 43.37  E-value: 3.83e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239950402  108 KDNFELEVLQTQYKELKEKMKAMEEEVLIKNGEIKILRDSLHQTESILEEQRR------------SHFLLEQEKTQALGD 175
Cdd:COG4913    682 ASSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDrleaaedlarleLRALLEERFAAALGD 761

                           90       100       110
                   ....*....|....*....|....*....|.
gi 1239950402  176 K-EKEFSKKLQSLQSELQfkdAEMNELRTKL 205
Cdd:COG4913    762 AvERELRENLEERIDALR---ARLNRAEEEL 789
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 108-213 7.22e-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: 42.31  E-value: 7.22e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239950402 108 KDNfELEVLQTQYKELKEKMKAMEEEVLIKNGEIKILRDSLHQTESILE--EQRRSHFlleQEKTQALGDKEKEFSKKLQ 185
Cdd:TIGR04523 410 KDE-QIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKnlDNTRESL---ETQLKVLSRSINKIKQNLE 485

                          90       100
                  ....*....|....*....|....*...
gi 1239950402 186 SLQSELQFKDAEMNELRTKLQSSERANK 213
Cdd:TIGR04523 486 QKQKELKSKEKELKKLNEEKKELEEKVK 513
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 112-217 7.22e-04

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 42.62  E-value: 7.22e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239950402 112 ELEVLQTQYKELKEKMKAMEEEVLIKNGEIKILRDSLHQTESILEEQRRSHFLLEQEKTQALGDKE------KEFSKKLQ 185
Cdd:COG1196   240 ELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIArleerrRELEERLE 319

                          90       100       110
                  ....*....|....*....|....*....|..
gi 1239950402 186 SLQSELQFKDAEMNELRTKLQSSERANKLAAP 217
Cdd:COG1196   320 ELEEELAELEEELEELEEELEELEEELEEAEE 351
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
112-209 8.82e-04

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 42.06  E-value: 8.82e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239950402 112 ELEVLQTQYKELKEKMKAMEEevLIKngEIKILRDSLHQTESILEEQRRSHFLLEQEKTQALGDKEKEFSKKLQSLQSEL 191
Cdd:COG4717   140 ELAELPERLEELEERLEELRE--LEE--ELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEEL 215

                          90
                  ....*....|....*...
gi 1239950402 192 QFKDAEMNELRTKLQSSE 209
Cdd:COG4717   216 EEAQEELEELEEELEQLE 233
OmpH smart00935
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH ...
 114-208 1.22e-03

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: 39.49  E-value: 1.22e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239950402  114 EVLQtQYKELKEKMKAMEEEVLIKNGEIKILRDSLHQTESILEEQRRShfLLEQEKTQalgdKEKEFSKKLQSLQSELQF 193
Cdd:smart00935   8 KILQ-ESPAGKAAQKQLEKEFKKRQAELEKLEKELQKLKEKLQKDAAT--LSEAAREK----KEKELQKKVQEFQRKQQK 80

                           90
                   ....*....|....*
gi 1239950402  194 KDAEMNELRTKLQSS 208
Cdd:smart00935  81 LQQDLQKRQQEELQK 95
GAS pfam13851
Growth-arrest specific micro-tubule binding; This family is the highly conserved central ...
 108-201 1.24e-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: 40.27  E-value: 1.24e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239950402 108 KDNFELEVLQTQYKELKEKMKAMEEE--VLI-KNGEIKILRDSLH--QTESILEEQRRSHF---LLEqektqalgdkeke 179
Cdd:pfam13851  82 KDKQSLKNLKARLKVLEKELKDLKWEheVLEqRFEKVERERDELYdkFEAAIQDVQQKTGLknlLLE------------- 148

                          90       100
                  ....*....|....*....|..
gi 1239950402 180 fsKKLQSLQSELQFKDAEMNEL 201
Cdd:pfam13851 149 --KKLQALGETLEKKEAQLNEV 168
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 113-225 1.40e-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: 41.29  E-value: 1.40e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239950402 113 LEVLQTQYKELKEKMKAME---EEVLIKNGEIKILRDSLHQTESILEEQRRSHFLLEQEKTQALGDKEKEFSKKLQSLQs 189
Cdd:COG4942   138 LQYLKYLAPARREQAEELRadlAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELA- 216

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1239950402 190 ELQFKDAEMNELRTKLQSSERANKLAAPSIPHASPR 225
Cdd:COG4942   217 ELQQEAEELEALIARLEAEAAAAAERTPAAGFAALK 252
Cast pfam10174
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ...
 113-207 1.59e-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: 1.59e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239950402 113 LEVLQTQYKE-------LKEKMKAMEEEVLIKNGEIKILRDSLHQTESIL-EEQRRSHFLLEQEKTQA---------LGD 175
Cdd:pfam10174 312 LETLTNQNSDckqhievLKESLTAKEQRAAILQTEVDALRLRLEEKESFLnKKTKQLQDLTEEKSTLAgeirdlkdmLDV 391

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1239950402 176 KEKE---FSKKLQSLQSELQFKDAEMNELRTKLQS 207
Cdd:pfam10174 392 KERKinvLQKKIENLQEQLRDKDKQLAGLKERVKS 426
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 102-211 1.88e-03

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 41.08  E-value: 1.88e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239950402 102 RELVPVKDNFELEVLQTQYKELKEKMKAMEEEVLIKNGEIKILRDSLHQTESILEEQRRSHFLLEQEKtQALGDKEKEFS 181
Cdd:COG1196   216 RELKEELKELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELEL-EEAQAEEYELL 294

                          90       100       110
                  ....*....|....*....|....*....|
gi 1239950402 182 KKLQSLQSELQFKDAEMNELRTKLQSSERA 211
Cdd:COG1196   295 AELARLEQDIARLEERRRELEERLEELEEE 324
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
119-216 2.65e-03

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 40.27  E-value: 2.65e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239950402 119 QYKELKEKMKAMEEEVLIKNGEIKILRDSLHQTESILEEQRRshfllEQEKTQalgdkekefsKKLQSLQSELQFKDAEM 198
Cdd:COG4372    32 QLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARS-----ELEQLE----------EELEELNEQLQAAQAEL 96

                          90
                  ....*....|....*....
gi 1239950402 199 NELRTKLQS-SERANKLAA 216
Cdd:COG4372    97 AQAQEELESlQEEAEELQE 115
CCDC22 pfam05667
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 ...
 39-187 2.96e-03

Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 (CCDC22) is involved in regulation of NF-kappa-B signalling; the function may involve association with COMMD8 and a CUL1-dependent E3 ubiquitin ligase complex. It is part of the OMMD/CCDC22/CCDC93 (CCC) complex, which interacts with the multisubunit WASH complex required for endosomal deposition of F-actin and cargo trafficking in conjunction with the retromer. This entry also includes CCDC22 homologs from animals and plants.


Pssm-ID: 461708 [Multi-domain]  Cd Length: 600  Bit Score: 40.40  E-value: 2.96e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239950402  39 AAAVPDPEDPFGAHGDftADDLEELDTLASQALSQCQAAARDTSNVH-------KVPRLDGMSKTPAGKNRELVPVKDNF 111
Cdd:pfam05667 258 SAALAGTEATSGASRS--AQDLAELLSSFSGSSTTDTGLTKGSRFTHteklqftNEAPAATSSPPTKVETEEELQQQREE 335

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239950402 112 ELEVLQTQYKELKEKMKAMEEevlikngEIKILRDSLHQTESILEEQRRSHFLLEQE---KTQALG--DKEKEFSKKLQS 186
Cdd:pfam05667 336 ELEELQEQLEDLESSIQELEK-------EIKKLESSIKQVEEELEELKEQNEELEKQykvKKKTLDllPDAEENIAKLQA 408


                  .
gi 1239950402 187 L 187
Cdd:pfam05667 409 L 409
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 121-209 3.08e-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: 3.08e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239950402  121 KELKEKMKAMEEEVLIKNGEIKILRDSLHQtesiLEEQRRSHFLLEQEKTQALGDKEKEFSK----------KLQSLQSE 190
Cdd:TIGR02168  680 EELEEKIEELEEKIAELEKALAELRKELEE----LEEELEQLRKELEELSRQISALRKDLARleaeveqleeRIAQLSKE 755

                           90
                   ....*....|....*....
gi 1239950402  191 LQFKDAEMNELRTKLQSSE 209
Cdd:TIGR02168  756 LTELEAEIEELEERLEEAE 774
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
60-210 3.71e-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: 3.71e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239950402  60 LEELDTLASQaLSQCQAAARDTSNvhkvpRLDGMSKTPAGKNRELVPVKDNFELEVLQTQYKELKEKMKAMEEEVLIKNG 139
Cdd:COG3206   218 LQQLSELESQ-LAEARAELAEAEA-----RLAALRAQLGSGPDALPELLQSPVIQQLRAQLAELEAELAELSARYTPNHP 291

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1239950402 140 EIKILRDSLHQTES-ILEEQRRSHFLLEQEKtQALGDKEKEFSKKLQSLQSELQfkdaEMNELRTKLQSSER 210
Cdd:COG3206   292 DVIALRAQIAALRAqLQQEAQRILASLEAEL-EALQAREASLQAQLAQLEARLA----ELPELEAELRRLER 358
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 107-205 4.22e-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: 39.14  E-value: 4.22e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239950402 107 VKDNFELEVLQTQYKELKEKMKAMEEEVLIKNGEIKILRDSLHQTESILEEQRrshflleqektQALGDKEKEFSKKLQS 186
Cdd:COG1579    85 VRNNKEYEALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELE-----------AELEEKKAELDEELAE 153

                          90
                  ....*....|....*....
gi 1239950402 187 LQSELQFKDAEMNELRTKL 205
Cdd:COG1579   154 LEAELEELEAEREELAAKI 172
DUF641 pfam04859
Plant protein of unknown function (DUF641); Plant protein of unknown function.
 187-213 5.52e-03

Plant protein of unknown function (DUF641); Plant protein of unknown function.


Pssm-ID: 461458 [Multi-domain]  Cd Length: 127  Bit Score: 37.19  E-value: 5.52e-03
                          10        20
                  ....*....|....*....|....*..
gi 1239950402 187 LQSELQFKDAEMNELRTKLQSSERANK 213
Cdd:pfam04859  96 LEAELKAKDSEIDSLREKLDEAERSNR 122
Atg16_CCD cd22887
Coiled-coiled domain of autophagy-related 16 (Atg16) family proteins; The Atg16 family ...
 112-168 7.08e-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: 36.00  E-value: 7.08e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239950402 112 ELEVLQTQYKELKEKMKAMEEEVLIKNGEIKILRD---SLHQTESILEEQRRShflLEQE 168
Cdd:cd22887    12 RLAELEAELASLEEEIKDLEEELKEKNKANEILNDeliALQIENNLLEEKLRK---LQEE 68
rad50 TIGR00606
rad50; All proteins in this family for which functions are known are involvedin recombination, ...
 54-213 7.69e-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: 39.26  E-value: 7.69e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239950402   54 DFTADDLEELDTLASQaLSQCQAAARDTSNVHKVPRLDGMSKtpagKNRELVpVKDNFELEVLQTQYKELKEKMKAMEEE 133
Cdd:TIGR00606  970 DYLKQKETELNTVNAQ-LEECEKHQEKINEDMRLMRQDIDTQ----KIQERW-LQDNLTLRKRENELKEVEEELKQHLKE 1043

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239950402  134 VliknGEIKILRdsLHQTESILEEQRRshfLLEQEKTQALGdKEKEFSKKLQSLQSEL---QFKDAEMN--ELRTKLQSS 208
Cdd:TIGR00606 1044 M----GQMQVLQ--MKQEHQKLEENID---LIKRNHVLALG-RQKGYEKEIKHFKKELrepQFRDAEEKyrEMMIVMRTT 1113


                   ....*
gi 1239950402  209 ERANK 213
Cdd:TIGR00606 1114 ELVNK 1118
DUF4670 pfam15709
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ...
 116-200 8.44e-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: 38.78  E-value: 8.44e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239950402 116 LQTQYKELKEKMKA-MEEEVLIKNGEIKILRDSLHQTESILEEQRRSHFLLEQEKTQALGDKEKEFSKKLQSLQSELQFK 194
Cdd:pfam15709 363 LQQEQLERAEKMREeLELEQQRRFEEIRLRKQRLEEERQRQEEEERKQRLQLQAAQERARQQQEEFRRKLQELQRKKQQE 442


                  ....*.
gi 1239950402 195 DAEMNE 200
Cdd:pfam15709 443 EAERAE 448
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
112-214 8.59e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 38.89  E-value: 8.59e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239950402 112 ELEVLQTQYKEL---KEKMKAMEEEVLIKNGEIKILRDSLHQTESILEEQRRSHFLLEQ------------EKTQALGDK 176
Cdd:PRK03918  222 ELEKLEKEVKELeelKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEkvkelkelkekaEEYIKLSEF 301

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1239950402 177 EKEFSKKLQSLQSELQFKDAEMNELRTKLQS----SERANKL 214
Cdd:PRK03918  302 YEEYLDELREIEKRLSRLEEEINGIEERIKEleekEERLEEL 343
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
 122-211 8.81e-03

Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.


Pssm-ID: 460256 [Multi-domain]  Cd Length: 1081  Bit Score: 39.00  E-value: 8.81e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239950402  122 ELKEKMKAMEEEVLIKNGEIKILRDSLHQTESILEEQ----RRSHFLLEQEKtQALGDKEKEFSKKLQSLQ-----SELQ 192
Cdd:pfam01576  328 EVTELKKALEEETRSHEAQLQEMRQKHTQALEELTEQleqaKRNKANLEKAK-QALESENAELQAELRTLQqakqdSEHK 406

                           90       100
                   ....*....|....*....|.
gi 1239950402  193 FKDAE--MNELRTKLQSSERA 211
Cdd:pfam01576  407 RKKLEgqLQELQARLSESERQ 427
 
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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