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Conserved domains on  [gi|21358155|ref|NP_649033|]
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uncharacterized protein Dmel_CG13699 [Drosophila melanogaster]

Protein Classification

DDRGK domain-containing protein( domain architecture ID 708811)

DDRGK domain-containing protein similar to Arabidopsis thaliana DDRGK domain-containing protein 1 that is a substrate adapter for ufmylation, the covalent attachment of the ubiquitin-like modifier UFM1 to substrate proteins

CATH:  1.10.10.10
Gene Ontology:  GO:0044389
SCOP:  4000147

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
DDRGK super family cl25550
DDRGK domain; This is a family of proteins of approximately 300 residues, found in plants and ...
823-891 1.37e-06

DDRGK domain; This is a family of proteins of approximately 300 residues, found in plants and vertebrates. They contain a highly conserved DDRGK motif.


The actual alignment was detected with superfamily member pfam09756:

Pssm-ID: 370664 [Multi-domain]  Cd Length: 188  Bit Score: 50.04  E-value: 1.37e-06
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21358155    823 REARILEEQIREQQIKEELFREEQIKEEQFREEQLREEEVRREQLREEE-IQRQQAQILRIREAQYSEQS 891
Cdd:pfam09756   18 RQQREAEEEEREEREKLEEKREEEYKEREEREEEAEKEKEEEERKQEEEqERKEQEEYEKLKSQFVVEEE 87
 
Name Accession Description Interval E-value
DDRGK pfam09756
DDRGK domain; This is a family of proteins of approximately 300 residues, found in plants and ...
823-891 1.37e-06

DDRGK domain; This is a family of proteins of approximately 300 residues, found in plants and vertebrates. They contain a highly conserved DDRGK motif.


Pssm-ID: 370664 [Multi-domain]  Cd Length: 188  Bit Score: 50.04  E-value: 1.37e-06
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21358155    823 REARILEEQIREQQIKEELFREEQIKEEQFREEQLREEEVRREQLREEE-IQRQQAQILRIREAQYSEQS 891
Cdd:pfam09756   18 RQQREAEEEEREEREKLEEKREEEYKEREEREEEAEKEKEEEERKQEEEqERKEQEEYEKLKSQFVVEEE 87
UDM1_RNF168_RNF169-like cd22249
UDM1 (ubiquitin-dependent DSB recruitment module 1) found in RING finger proteins RNF168, ...
823-881 1.09e-04

UDM1 (ubiquitin-dependent DSB recruitment module 1) found in RING finger proteins RNF168, RNF169 and similar proteins; This model represents the UDM1 (ubiquitin-dependent double-strand break [DSB] recruitment module 1) found in RING finger proteins, RNF168 and RNF169. RNF168 is an E3 ubiquitin-protein ligase that promotes non-canonical K27 ubiquitination to signal DNA damage. It functions, together with RNF8, as a DNA damage response (DDR) factor that promotes a series of ubiquitylation events on substrates such as H2A and H2AX. With H2AK13/15 ubiquitylation, it facilitates recruitment of repair factors p53-binding protein 1 (53BP1) or the RAP80-BRCA1 complex to sites of double-strand breaks (DSBs), and inhibits homologous recombination (HR) in cells deficient in the tumor suppressor BRCA1. RNF168 also promotes H2A neddylation, which antagonizes ubiquitylation of H2A and regulates DNA damage repair. In addition, RNF168 forms a functional complex with RAD6A or RAD6B during the DNA damage response. RNF169 is an uncharacterized E3 ubiquitin-protein ligase paralogous to RNF168. It functions as a negative regulator of the DNA damage signaling cascade. RNF169 recognizes polyubiquitin structures but does not itself contribute to double-strand break (DSB)-induced chromatin ubiquitylation. It contributes to the regulation of DSB repair pathway utilization via functionally competing with recruiting repair factors, 53BP1 and RAP80-BRCA1, for association with RNF168-modified chromatin, independent of its catalytic activity, limiting the magnitude of the RNF8/RNF168-dependent signaling response to DSBs. The UDM1 domain comprises LRM1 (LR motif 1), UMI (ubiquitin-interacting motif [UIM]- and MIU-related UBD) and MIU1 (motif interacting with ubiquitin 1). Mutations of Ub-interacting residues in UDM1 have little effect on the accumulation of RNF168 to DSB sites, suggesting that it may not be the main site of binding ubiquitylated and polyubiquitylated targets.


Pssm-ID: 409016 [Multi-domain]  Cd Length: 66  Bit Score: 41.10  E-value: 1.09e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 21358155  823 REARILEEQIREQQIKEELFREEQIKeeqfreeQLREEEVRREQLREEEIQRQQAQILR 881
Cdd:cd22249   13 AQLKKLEEERRKEREEEEKASEELIR-------KLQEEEERQRKREREEQLKQDEELAK 64
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
820-909 7.10e-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: 7.10e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21358155  820 AELREARILEEQIREQQIKEELFREEQIKEEqfREEQLREEEVRREQLREEEIQRQQAQILRIREAQYSEQSFKDDSPAP 899
Cdd:COG1196  672 AALLEAEAELEELAERLAEEELELEEALLAE--EEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLE 749
                         90
                 ....*....|
gi 21358155  900 NAVYDDAAPP 909
Cdd:COG1196  750 EEALEELPEP 759
PRK12704 PRK12704
phosphodiesterase; Provisional
820-891 8.85e-03

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 39.76  E-value: 8.85e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 21358155   820 AELREARILEEQIRE-QQIKEELFREEQIKEEQFREEQlrEEEVRReqlREEEIQRQQAQILRiREAQYSEQS 891
Cdd:PRK12704   36 AEEEAKRILEEAKKEaEAIKKEALLEAKEEIHKLRNEF--EKELRE---RRNELQKLEKRLLQ-KEENLDRKL 102
 
Name Accession Description Interval E-value
DDRGK pfam09756
DDRGK domain; This is a family of proteins of approximately 300 residues, found in plants and ...
823-891 1.37e-06

DDRGK domain; This is a family of proteins of approximately 300 residues, found in plants and vertebrates. They contain a highly conserved DDRGK motif.


Pssm-ID: 370664 [Multi-domain]  Cd Length: 188  Bit Score: 50.04  E-value: 1.37e-06
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21358155    823 REARILEEQIREQQIKEELFREEQIKEEQFREEQLREEEVRREQLREEE-IQRQQAQILRIREAQYSEQS 891
Cdd:pfam09756   18 RQQREAEEEEREEREKLEEKREEEYKEREEREEEAEKEKEEEERKQEEEqERKEQEEYEKLKSQFVVEEE 87
MAP7 pfam05672
MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is ...
822-891 3.82e-06

MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is presumably controlled by tissue-specific microtubule-associated proteins (MAPs). The 115-kDa epithelial MAP (E-MAP-115/MAP7) has been identified as a microtubule-stabilising protein predominantly expressed in cell lines of epithelial origin. The binding of this microtubule associated protein is nucleotide independent.


Pssm-ID: 461709 [Multi-domain]  Cd Length: 153  Bit Score: 47.73  E-value: 3.82e-06
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 21358155    822 LREARILEEQIREQQIKEELFREEQIKEEQFREEQLREEEVRR---EQLREEEIQRQQAQILRIREAQYSEQS 891
Cdd:pfam05672   23 AREQREREEQERLEKEEEERLRKEELRRRAEEERARREEEARRleeERRREEEERQRKAEEEAEEREQREQEE 95
MAP7 pfam05672
MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is ...
825-886 6.84e-06

MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is presumably controlled by tissue-specific microtubule-associated proteins (MAPs). The 115-kDa epithelial MAP (E-MAP-115/MAP7) has been identified as a microtubule-stabilising protein predominantly expressed in cell lines of epithelial origin. The binding of this microtubule associated protein is nucleotide independent.


Pssm-ID: 461709 [Multi-domain]  Cd Length: 153  Bit Score: 46.96  E-value: 6.84e-06
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 21358155    825 ARILEE---QIREQQIKEELFREEQIKEEQFREEQLREEEVRREQLREEEIQRQQAQILRIREAQ 886
Cdd:pfam05672   13 ARILAEkrrQAREQREREEQERLEKEEEERLRKEELRRRAEEERARREEEARRLEEERRREEEER 77
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
823-893 1.65e-05

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


Pssm-ID: 375164 [Multi-domain]  Cd Length: 722  Bit Score: 48.97  E-value: 1.65e-05
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 21358155    823 REARILEEQiREQQIKEELFREEQIKEEQ--FREEQLR--EEEVRRE--QLREEEIQRQQaQILRIREaQYSEQSFK 893
Cdd:pfam17380  402 RKVKILEEE-RQRKIQQQKVEMEQIRAEQeeARQREVRrlEEERAREmeRVRLEEQERQQ-QVERLRQ-QEEERKRK 475
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
823-886 6.34e-05

Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.


Pssm-ID: 464007 [Multi-domain]  Cd Length: 341  Bit Score: 46.45  E-value: 6.34e-05
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 21358155    823 REARILEEQIREQQIKEELFREEQIKEEQFREEQLREEEVRREQLREEEIQRQQAQILRIREAQ 886
Cdd:pfam13868  137 EEQAEWKELEKEEEREEDERILEYLKEKAEREEEREAEREEIEEEKEREIARLRAQQEKAQDEK 200
UDM1_RNF168_RNF169-like cd22249
UDM1 (ubiquitin-dependent DSB recruitment module 1) found in RING finger proteins RNF168, ...
823-881 1.09e-04

UDM1 (ubiquitin-dependent DSB recruitment module 1) found in RING finger proteins RNF168, RNF169 and similar proteins; This model represents the UDM1 (ubiquitin-dependent double-strand break [DSB] recruitment module 1) found in RING finger proteins, RNF168 and RNF169. RNF168 is an E3 ubiquitin-protein ligase that promotes non-canonical K27 ubiquitination to signal DNA damage. It functions, together with RNF8, as a DNA damage response (DDR) factor that promotes a series of ubiquitylation events on substrates such as H2A and H2AX. With H2AK13/15 ubiquitylation, it facilitates recruitment of repair factors p53-binding protein 1 (53BP1) or the RAP80-BRCA1 complex to sites of double-strand breaks (DSBs), and inhibits homologous recombination (HR) in cells deficient in the tumor suppressor BRCA1. RNF168 also promotes H2A neddylation, which antagonizes ubiquitylation of H2A and regulates DNA damage repair. In addition, RNF168 forms a functional complex with RAD6A or RAD6B during the DNA damage response. RNF169 is an uncharacterized E3 ubiquitin-protein ligase paralogous to RNF168. It functions as a negative regulator of the DNA damage signaling cascade. RNF169 recognizes polyubiquitin structures but does not itself contribute to double-strand break (DSB)-induced chromatin ubiquitylation. It contributes to the regulation of DSB repair pathway utilization via functionally competing with recruiting repair factors, 53BP1 and RAP80-BRCA1, for association with RNF168-modified chromatin, independent of its catalytic activity, limiting the magnitude of the RNF8/RNF168-dependent signaling response to DSBs. The UDM1 domain comprises LRM1 (LR motif 1), UMI (ubiquitin-interacting motif [UIM]- and MIU-related UBD) and MIU1 (motif interacting with ubiquitin 1). Mutations of Ub-interacting residues in UDM1 have little effect on the accumulation of RNF168 to DSB sites, suggesting that it may not be the main site of binding ubiquitylated and polyubiquitylated targets.


Pssm-ID: 409016 [Multi-domain]  Cd Length: 66  Bit Score: 41.10  E-value: 1.09e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 21358155  823 REARILEEQIREQQIKEELFREEQIKeeqfreeQLREEEVRREQLREEEIQRQQAQILR 881
Cdd:cd22249   13 AQLKKLEEERRKEREEEEKASEELIR-------KLQEEEERQRKREREEQLKQDEELAK 64
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
822-890 1.10e-04

Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.


Pssm-ID: 464007 [Multi-domain]  Cd Length: 341  Bit Score: 45.68  E-value: 1.10e-04
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 21358155    822 LREARILEEQIREQQIKEELFREEQIKE-EQFRE--EQLREEEVRREQLREE-------EIQRQQAQILRIREAQYSEQ 890
Cdd:pfam13868   72 KRYRQELEEQIEEREQKRQEEYEEKLQErEQMDEivERIQEEDQAEAEEKLEkqrqlreEIDEFNEEQAEWKELEKEEE 150
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
821-886 4.23e-04

Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.


Pssm-ID: 464007 [Multi-domain]  Cd Length: 341  Bit Score: 43.75  E-value: 4.23e-04
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 21358155    821 ELREARILEEQIREQQIKEELfREEQIKEEQFREEQLREEEVR-----REQLREEEIQRQQAQILRIREAQ 886
Cdd:pfam13868   32 KRIKAEEKEEERRLDEMMEEE-RERALEEEEEKEEERKEERKRyrqelEEQIEEREQKRQEEYEEKLQERE 101
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
820-909 7.10e-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: 7.10e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21358155  820 AELREARILEEQIREQQIKEELFREEQIKEEqfREEQLREEEVRREQLREEEIQRQQAQILRIREAQYSEQSFKDDSPAP 899
Cdd:COG1196  672 AALLEAEAELEELAERLAEEELELEEALLAE--EEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLE 749
                         90
                 ....*....|
gi 21358155  900 NAVYDDAAPP 909
Cdd:COG1196  750 EEALEELPEP 759
DUF4659 pfam15558
Domain of unknown function (DUF4659); This family of proteins is found in eukaryotes. Proteins ...
829-885 9.09e-04

Domain of unknown function (DUF4659); This family of proteins is found in eukaryotes. Proteins in this family are typically between 427 and 674 amino acids in length. There are two completely conserved residues (D and I) that may be functionally important.


Pssm-ID: 464768 [Multi-domain]  Cd Length: 374  Bit Score: 42.72  E-value: 9.09e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 21358155    829 EEQIREQQIKEELFREEQIKEEQFREEQLREEEVRREQLREEEIQRQQAQILRIREA 885
Cdd:pfam15558   78 ERRRADRREKQVIEKESRWREQAEDQENQRQEKLERARQEAEQRKQCQEQRLKEKEE 134
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
820-886 1.01e-03

Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.


Pssm-ID: 464007 [Multi-domain]  Cd Length: 341  Bit Score: 42.60  E-value: 1.01e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 21358155    820 AELREARILEEQIREQQI-----KEELFREEQIKEEQFREEQLREEEVRREQLREEEIQRQQAQI-----LRIREAQ 886
Cdd:pfam13868  235 QELQQAREEQIELKERRLaeeaeREEEEFERMLRKQAEDEEIEQEEAEKRRMKRLEHRRELEKQIeereeQRAAERE 311
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
819-889 1.44e-03

Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.


Pssm-ID: 464007 [Multi-domain]  Cd Length: 341  Bit Score: 42.21  E-value: 1.44e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 21358155    819 EAELREARILEEQIREQQIKEELF--REEQI--KEEQFREEQLREEE----VRREQLREEEIQRQQAQILRIREAQYSE 889
Cdd:pfam13868  215 QERKERQKEREEAEKKARQRQELQqaREEQIelKERRLAEEAEREEEeferMLRKQAEDEEIEQEEAEKRRMKRLEHRR 293
GBP_C cd16269
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal ...
826-883 1.90e-03

Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal domain. Guanylate-binding proteins (GBPs) are synthesized after activation of the cell by interferons. The biochemical properties of GBPs are clearly different from those of Ras-like and heterotrimeric GTP-binding proteins. They bind guanine nucleotides with low affinity (micromolar range), are stable in their absence, and have a high turnover GTPase. In addition to binding GDP/GTP, they have the unique ability to bind GMP with equal affinity and hydrolyze GTP not only to GDP, but also to GMP. This C-terminal domain has been shown to mediate inhibition of endothelial cell proliferation by inflammatory cytokines.


Pssm-ID: 293879 [Multi-domain]  Cd Length: 291  Bit Score: 41.41  E-value: 1.90e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 21358155  826 RILEEQIREQQIKEELFREEQIKE-EQFREEQLREEEVRREQLREEEIQRQQAQILRIR 883
Cdd:cd16269  233 RSYEEHLRQLKEKMEEERENLLKEqERALESKLKEQEALLEEGFKEQAELLQEEIRSLK 291
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
821-886 2.49e-03

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 41.85  E-value: 2.49e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21358155  821 ELREARI-LEEQIREQQIKEELFREEQIKEEQ---FREEQLREEEVRREQLrEEEIQRQQAQILRIREAQ 886
Cdd:COG1196  271 ELRLELEeLELELEEAQAEEYELLAELARLEQdiaRLEERRRELEERLEEL-EEELAELEEELEELEEEL 339
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
821-890 2.49e-03

Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.


Pssm-ID: 464007 [Multi-domain]  Cd Length: 341  Bit Score: 41.44  E-value: 2.49e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 21358155    821 ELREARILEEQIREQQIKEEL--FREEQIKEEQFREEQLRE-EEVRREQLREEEIQRQQAQILRIREAQYSEQ 890
Cdd:pfam13868  183 EREIARLRAQQEKAQDEKAERdeLRAKLYQEEQERKERQKErEEAEKKARQRQELQQAREEQIELKERRLAEE 255
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
820-890 2.86e-03

Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.


Pssm-ID: 464007 [Multi-domain]  Cd Length: 341  Bit Score: 41.06  E-value: 2.86e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21358155    820 AELREA---RILEEQIRE-QQIKEELFREEQIKEEQFREEQLR--EEEVRREQLREEEIQRQQAQI---LRIREAQYSEQ 890
Cdd:pfam13868   13 SKLLAAkcnKERDAQIAEkKRIKAEEKEEERRLDEMMEEERERalEEEEEKEEERKEERKRYRQELeeqIEEREQKRQEE 92
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
820-895 2.99e-03

Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.


Pssm-ID: 464007 [Multi-domain]  Cd Length: 341  Bit Score: 41.06  E-value: 2.99e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21358155    820 AELREARILEEQIREQ-QIKEEL--FREEQIKEEQFREEQLREEEVR--------------REQLREEEIQRQQAQILRI 882
Cdd:pfam13868  110 IQEEDQAEAEEKLEKQrQLREEIdeFNEEQAEWKELEKEEEREEDERileylkekaereeeREAEREEIEEEKEREIARL 189
                           90
                   ....*....|...
gi 21358155    883 REAQYSEQSFKDD 895
Cdd:pfam13868  190 RAQQEKAQDEKAE 202
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
821-895 3.18e-03

Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.


Pssm-ID: 464007 [Multi-domain]  Cd Length: 341  Bit Score: 41.06  E-value: 3.18e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 21358155    821 ELREARILEEQIREQQIKEelfREEQIKEEQFREEqLREEevRREQLREEEIQRQQAQILRIREAQYSEQSFKDD 895
Cdd:pfam13868  205 ELRAKLYQEEQERKERQKE---REEAEKKARQRQE-LQQA--REEQIELKERRLAEEAEREEEEFERMLRKQAED 273
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
820-890 3.29e-03

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 41.46  E-value: 3.29e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 21358155  820 AELREARI----LEEQIREQQIKEELFREEQIKEEQ---FREEQLREEEVRREQLREEEIQ-RQQAQILRIREAQYSEQ 890
Cdd:COG1196  267 AELEELRLeleeLELELEEAQAEEYELLAELARLEQdiaRLEERRRELEERLEELEEELAElEEELEELEEELEELEEE 345
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
821-890 3.69e-03

Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.


Pssm-ID: 464007 [Multi-domain]  Cd Length: 341  Bit Score: 40.67  E-value: 3.69e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21358155    821 ELREARILEEQIREQQIKEELFREEQikEEQFREEQLREEEVRREQlreEEIQRQQAQILRIREAQYSEQ 890
Cdd:pfam13868  150 EREEDERILEYLKEKAEREEEREAER--EEIEEEKEREIARLRAQQ---EKAQDEKAERDELRAKLYQEE 214
MAP7 pfam05672
MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is ...
824-878 3.98e-03

MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is presumably controlled by tissue-specific microtubule-associated proteins (MAPs). The 115-kDa epithelial MAP (E-MAP-115/MAP7) has been identified as a microtubule-stabilising protein predominantly expressed in cell lines of epithelial origin. The binding of this microtubule associated protein is nucleotide independent.


Pssm-ID: 461709 [Multi-domain]  Cd Length: 153  Bit Score: 38.87  E-value: 3.98e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 21358155    824 EARILEEQIREQQIKEELFREE---QIKEEQFREE-----QLREEEVRREQLREEEIQRQQAQ 878
Cdd:pfam05672   40 EERLRKEELRRRAEEERARREEearRLEEERRREEeerqrKAEEEAEEREQREQEEQERLQKQ 102
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
820-889 4.00e-03

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 41.46  E-value: 4.00e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21358155  820 AELREARILEEQIREQQIKEELFREEQIKEEQFREEQLREEEVRREQLREEEIQRQQAQILRIREAQYSE 889
Cdd:COG1196  412 LLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAE 481
DUF4659 pfam15558
Domain of unknown function (DUF4659); This family of proteins is found in eukaryotes. Proteins ...
820-890 4.15e-03

Domain of unknown function (DUF4659); This family of proteins is found in eukaryotes. Proteins in this family are typically between 427 and 674 amino acids in length. There are two completely conserved residues (D and I) that may be functionally important.


Pssm-ID: 464768 [Multi-domain]  Cd Length: 374  Bit Score: 40.79  E-value: 4.15e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 21358155    820 AELREARILEEQ-IREQQIKEELFREEQIKEEQFReeQLREEEVRREQLREEEIQRQQAQILRIREAQYSEQ 890
Cdd:pfam15558   10 AALMLARHKEEQrMRELQQQAALAWEELRRRDQKR--QETLERERRLLLQQSQEQWQAEKEQRKARLGREER 79
MAP7 pfam05672
MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is ...
820-886 6.04e-03

MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is presumably controlled by tissue-specific microtubule-associated proteins (MAPs). The 115-kDa epithelial MAP (E-MAP-115/MAP7) has been identified as a microtubule-stabilising protein predominantly expressed in cell lines of epithelial origin. The binding of this microtubule associated protein is nucleotide independent.


Pssm-ID: 461709 [Multi-domain]  Cd Length: 153  Bit Score: 38.48  E-value: 6.04e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 21358155    820 AELREARILEEQIREQQIKEELFREEQI-KEEQFREEQLREEEVRREQlREEEIQRQQAQILRIREAQ 886
Cdd:pfam05672   64 RRLEEERRREEEERQRKAEEEAEEREQReQEEQERLQKQKEEAEAKAR-EEAERQRQEREKIMQQEEQ 130
UDM1_RNF168_RNF169-like cd22249
UDM1 (ubiquitin-dependent DSB recruitment module 1) found in RING finger proteins RNF168, ...
846-884 6.67e-03

UDM1 (ubiquitin-dependent DSB recruitment module 1) found in RING finger proteins RNF168, RNF169 and similar proteins; This model represents the UDM1 (ubiquitin-dependent double-strand break [DSB] recruitment module 1) found in RING finger proteins, RNF168 and RNF169. RNF168 is an E3 ubiquitin-protein ligase that promotes non-canonical K27 ubiquitination to signal DNA damage. It functions, together with RNF8, as a DNA damage response (DDR) factor that promotes a series of ubiquitylation events on substrates such as H2A and H2AX. With H2AK13/15 ubiquitylation, it facilitates recruitment of repair factors p53-binding protein 1 (53BP1) or the RAP80-BRCA1 complex to sites of double-strand breaks (DSBs), and inhibits homologous recombination (HR) in cells deficient in the tumor suppressor BRCA1. RNF168 also promotes H2A neddylation, which antagonizes ubiquitylation of H2A and regulates DNA damage repair. In addition, RNF168 forms a functional complex with RAD6A or RAD6B during the DNA damage response. RNF169 is an uncharacterized E3 ubiquitin-protein ligase paralogous to RNF168. It functions as a negative regulator of the DNA damage signaling cascade. RNF169 recognizes polyubiquitin structures but does not itself contribute to double-strand break (DSB)-induced chromatin ubiquitylation. It contributes to the regulation of DSB repair pathway utilization via functionally competing with recruiting repair factors, 53BP1 and RAP80-BRCA1, for association with RNF168-modified chromatin, independent of its catalytic activity, limiting the magnitude of the RNF8/RNF168-dependent signaling response to DSBs. The UDM1 domain comprises LRM1 (LR motif 1), UMI (ubiquitin-interacting motif [UIM]- and MIU-related UBD) and MIU1 (motif interacting with ubiquitin 1). Mutations of Ub-interacting residues in UDM1 have little effect on the accumulation of RNF168 to DSB sites, suggesting that it may not be the main site of binding ubiquitylated and polyubiquitylated targets.


Pssm-ID: 409016 [Multi-domain]  Cd Length: 66  Bit Score: 36.09  E-value: 6.67e-03
                         10        20        30
                 ....*....|....*....|....*....|....*....
gi 21358155  846 QIKEEqfREEQLREEEVRREQLREEEIQRQQAQILRIRE 884
Cdd:cd22249    6 EIREE--YEAQLKKLEEERRKEREEEEKASEELIRKLQE 42
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
820-899 6.77e-03

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 40.69  E-value: 6.77e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21358155  820 AELREARILEEQIREQQIKEELFREEQIKEEQFREEQLREEevRREQLREEEIQRQQAQILRIREAQYSEQSFKDDSPAP 899
Cdd:COG1196  684 LAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEE--ALEEQLEAEREELLEELLEEEELLEEEALEELPEPPD 761
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
820-886 8.81e-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: 8.81e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 21358155  820 AELREARILEEQIREQQIKEELFREEQIKEEQFREEQLREEEVRREQLREEEIQRQQAQILRIREAQ 886
Cdd:COG1196  372 AELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEE 438
PRK12704 PRK12704
phosphodiesterase; Provisional
820-891 8.85e-03

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 39.76  E-value: 8.85e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 21358155   820 AELREARILEEQIRE-QQIKEELFREEQIKEEQFREEQlrEEEVRReqlREEEIQRQQAQILRiREAQYSEQS 891
Cdd:PRK12704   36 AEEEAKRILEEAKKEaEAIKKEALLEAKEEIHKLRNEF--EKELRE---RRNELQKLEKRLLQ-KEENLDRKL 102
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
820-886 9.27e-03

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 39.92  E-value: 9.27e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 21358155  820 AELREARILEEQIREQQIKEELFREEQIKEEQFREEQLREEEVRREQLREEEIQRQQAQILRIREAQ 886
Cdd:COG1196  395 AAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEAL 461
 
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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