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Conserved domains on  [gi|1720366917|ref|XP_030102047|]
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G protein pathway suppressor 2 isoform X1 [Mus musculus]

Protein Classification

UDM1_RNF168_RNF169-like domain-containing protein( domain architecture ID 12175665)

UDM1_RNF168_RNF169-like domain-containing protein

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
G_path_suppress pfam15991
G-protein pathway suppressor; This family of proteins inhibits G-protein- and ...
 5-292 1.50e-77

G-protein pathway suppressor; This family of proteins inhibits G-protein- and mitogen-activated protein kinase-mediated signal transduction.


:

Pssm-ID: 464961 [Multi-domain]  Cd Length: 272  Bit Score: 240.21  E-value: 1.50e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366917   5 LERPKLSNAMARALHRHIMMERERKRQEEEEvdKMMEQKMKEEQERRKKkemEERMSLEETKEQILKLQEKLSALQEEKH 84
Cdd:pfam15991   1 AARPKMSEQMWRALKRHIMRERERKKQEQEA--KMEEERLRREREEREK---EDRMTLEETKEQILKLEKKLADLKEEKH 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366917  85 QLFLQLKKVLHEEEKRRR--KEQSDLTTLTSAAYQqsltvhTGTHLLSMQGSPGGHNRPGTLMAADRAKQMFGPQVLTTr 162
Cdd:pfam15991  76 QLFLQLKKVLHEDETRKRqlKEQSELFALQQAAAQ------VFLPQLSMQGQPHHQQHPGPQVGVLKRTRSPSPPVQQQ- 148

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366917 163 HYVGSAAAFAGTPEHGQFQGSPGGAYGTAQPPPHYGPTQPAYSPSQQLrapsAFPAVQYLSQPQPQPYAVHGHfqptQTG 242
Cdd:pfam15991 149 AYYKQPAFSPGYAEHGQQKHDDGRRGYDVARFGSWNKSTAQYPPSGQL----FYPTHQYLPPPQTQGQADARL----QTI 220

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1720366917 243 FLQPGSTLSLQKQMEHANQQTSFSDSSSLRPM-HPQALH-PAPGLLASPQLP 292
Cdd:pfam15991 221 YPQPGYALPLQQQYEHANQPSPFVSSSPLKQMqSPKAGPgPQPMQLSVLHIP 272
 
Name Accession Description Interval E-value
G_path_suppress pfam15991
G-protein pathway suppressor; This family of proteins inhibits G-protein- and ...
 5-292 1.50e-77

G-protein pathway suppressor; This family of proteins inhibits G-protein- and mitogen-activated protein kinase-mediated signal transduction.


Pssm-ID: 464961 [Multi-domain]  Cd Length: 272  Bit Score: 240.21  E-value: 1.50e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366917   5 LERPKLSNAMARALHRHIMMERERKRQEEEEvdKMMEQKMKEEQERRKKkemEERMSLEETKEQILKLQEKLSALQEEKH 84
Cdd:pfam15991   1 AARPKMSEQMWRALKRHIMRERERKKQEQEA--KMEEERLRREREEREK---EDRMTLEETKEQILKLEKKLADLKEEKH 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366917  85 QLFLQLKKVLHEEEKRRR--KEQSDLTTLTSAAYQqsltvhTGTHLLSMQGSPGGHNRPGTLMAADRAKQMFGPQVLTTr 162
Cdd:pfam15991  76 QLFLQLKKVLHEDETRKRqlKEQSELFALQQAAAQ------VFLPQLSMQGQPHHQQHPGPQVGVLKRTRSPSPPVQQQ- 148

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366917 163 HYVGSAAAFAGTPEHGQFQGSPGGAYGTAQPPPHYGPTQPAYSPSQQLrapsAFPAVQYLSQPQPQPYAVHGHfqptQTG 242
Cdd:pfam15991 149 AYYKQPAFSPGYAEHGQQKHDDGRRGYDVARFGSWNKSTAQYPPSGQL----FYPTHQYLPPPQTQGQADARL----QTI 220

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1720366917 243 FLQPGSTLSLQKQMEHANQQTSFSDSSSLRPM-HPQALH-PAPGLLASPQLP 292
Cdd:pfam15991 221 YPQPGYALPLQQQYEHANQPSPFVSSSPLKQMqSPKAGPgPQPMQLSVLHIP 272
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 36-284 8.35e-04

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 40.97  E-value: 8.35e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366917  36 VDKMMEQ--KMKEEQERRKKKEMEERMSLEETKEQILKLQEKLSALQEEKHQLFLQLKKVLHEEEKRRRKEQSDLTTLTS 113
Cdd:COG3883   124 LSKIADAdaDLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEA 203

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366917 114 AAYQQSLTVHTGTHLLSMQGSPGGHNRPGTLMAADRAKQMFGPQVLTTRHYVGSAAAFAGTPEHGQFQGSPGGAYGTAQP 193
Cdd:COG3883   204 ELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAASAAGAGAAGAAGAAAGSAGAAGAAAGAAGAGAAAASAAG 283

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366917 194 PPHYGPTQPAYSPSQQLRAPSAFPAVQYLSQPQPQPYAVHGHFQPTQTGFLQPGSTLSLQKQMEHANQQTSFSDSSSLRP 273
Cdd:COG3883   284 GGAGGAGGGGGGGGAASGGSGGGSGGAGGVGSGGGAGAVVGGASAGGGGGSGGGGGSSGGGSGGGGGGGGGGGGSSSGGG 363

                         250
                  ....*....|.
gi 1720366917 274 MHPQALHPAPG 284
Cdd:COG3883   364 GGGVGLSVGGG 374
PTZ00121 PTZ00121
MAEBL; Provisional
 41-105 1.00e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 41.28  E-value: 1.00e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1720366917   41 EQKMKEEQERrkkKEMEERMSLEETK--EQILKLQEKLSALQEEKHQLFLQLKKvlHEEEKRRRKEQ 105
Cdd:PTZ00121  1604 EKKMKAEEAK---KAEEAKIKAEELKkaEEEKKKVEQLKKKEAEEKKKAEELKK--AEEENKIKAAE 1665
UDM1_RNF168_RNF169-like cd22249
UDM1 (ubiquitin-dependent DSB recruitment module 1) found in RING finger proteins RNF168, ...
 41-105 1.55e-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: 36.48  E-value: 1.55e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1720366917  41 EQKMKEEQERRKKKEMEERMSLeetkEQILKLQEklsalqEEKHQLFLQLkkvlheEEKRRRKEQ 105
Cdd:cd22249    13 AQLKKLEEERRKEREEEEKASE----ELIRKLQE------EEERQRKRER------EEQLKQDEE 61
 
Name Accession Description Interval E-value
G_path_suppress pfam15991
G-protein pathway suppressor; This family of proteins inhibits G-protein- and ...
 5-292 1.50e-77

G-protein pathway suppressor; This family of proteins inhibits G-protein- and mitogen-activated protein kinase-mediated signal transduction.


Pssm-ID: 464961 [Multi-domain]  Cd Length: 272  Bit Score: 240.21  E-value: 1.50e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366917   5 LERPKLSNAMARALHRHIMMERERKRQEEEEvdKMMEQKMKEEQERRKKkemEERMSLEETKEQILKLQEKLSALQEEKH 84
Cdd:pfam15991   1 AARPKMSEQMWRALKRHIMRERERKKQEQEA--KMEEERLRREREEREK---EDRMTLEETKEQILKLEKKLADLKEEKH 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366917  85 QLFLQLKKVLHEEEKRRR--KEQSDLTTLTSAAYQqsltvhTGTHLLSMQGSPGGHNRPGTLMAADRAKQMFGPQVLTTr 162
Cdd:pfam15991  76 QLFLQLKKVLHEDETRKRqlKEQSELFALQQAAAQ------VFLPQLSMQGQPHHQQHPGPQVGVLKRTRSPSPPVQQQ- 148

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366917 163 HYVGSAAAFAGTPEHGQFQGSPGGAYGTAQPPPHYGPTQPAYSPSQQLrapsAFPAVQYLSQPQPQPYAVHGHfqptQTG 242
Cdd:pfam15991 149 AYYKQPAFSPGYAEHGQQKHDDGRRGYDVARFGSWNKSTAQYPPSGQL----FYPTHQYLPPPQTQGQADARL----QTI 220

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1720366917 243 FLQPGSTLSLQKQMEHANQQTSFSDSSSLRPM-HPQALH-PAPGLLASPQLP 292
Cdd:pfam15991 221 YPQPGYALPLQQQYEHANQPSPFVSSSPLKQMqSPKAGPgPQPMQLSVLHIP 272
ARGLU pfam15346
Arginine and glutamate-rich 1; ARGLU, arginine and glutamate-rich 1 protein family, is ...
 41-106 1.60e-08

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


Pssm-ID: 405931 [Multi-domain]  Cd Length: 151  Bit Score: 53.13  E-value: 1.60e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1720366917  41 EQKMKEEQERRKKKEMEERMslEETKEQILKLQEKLsalqEEKHQLFLQLKKVLHEEEKRRRKEQS 106
Cdd:pfam15346  68 EERRKEEEERKKREELERIL--EENNRKIEEAQRKE----AEERLAMLEEQRRMKEERQRREKEEE 127
CAF-1_p150 pfam11600
Chromatin assembly factor 1 complex p150 subunit, N-terminal; CAF-1_p150 is a polypeptide ...
 38-109 4.58e-05

Chromatin assembly factor 1 complex p150 subunit, N-terminal; CAF-1_p150 is a polypeptide subunit of CAF-1, which functions in depositing newly synthesized and acetylated histones H3/H4 into chromatin during DNA replication and repair. CAF-1_p150 includes the HP1 interaction site, the PEST, KER and ED interacting sites. CAF-1_p150 interacts directly with newly synthesized and acetylated histones through the acidic KER and ED domains. The PEST domain is associated with proteins that undergo rapid proteolysis.


Pssm-ID: 402959 [Multi-domain]  Cd Length: 164  Bit Score: 43.52  E-value: 4.58e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1720366917  38 KMMEQKMKEEQERRKKKEMEERMSLEETKEQILKLQEKLSALQ---EEKHQlfLQLKKVLHEEEKRRRKEQSDLT 109
Cdd:pfam11600  59 KKEEEKELKEKERREKKEKDEKEKAEKLRLKEEKRKEKQEALEaklEEKRK--KEEEKRLKEEEKRIKAEKAEIT 131
MAP7 pfam05672
MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is ...
 41-105 2.20e-04

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: 41.18  E-value: 2.20e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1720366917  41 EQKMKEEQERRKKkEMEERMSLEETKEQilklQEKLSALQEEKHQLFLQLKKVLHEEEKRRRKEQ 105
Cdd:pfam05672  25 EQREREEQERLEK-EEEERLRKEELRRR----AEEERARREEEARRLEEERRREEEERQRKAEEE 84
SMC_N pfam02463
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...
 41-102 2.63e-04

RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.


Pssm-ID: 426784 [Multi-domain]  Cd Length: 1161  Bit Score: 43.04  E-value: 2.63e-04
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1720366917   41 EQKMKEEQERRKKKEMEERMSLEETKEQILKLQEKLSALQEEKHQLFLQLKKVLHEEEKRRR 102
Cdd:pfam02463  166 RLKRKKKEALKKLIEETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEYLL 227
GAS pfam13851
Growth-arrest specific micro-tubule binding; This family is the highly conserved central ...
 42-101 3.84e-04

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: 41.05  E-value: 3.84e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366917  42 QKMKEEQERRKKKEMEERMSLEETKEQILKLQEKLSALQEEKHQLFLQLKKvlHEEEKRR 101
Cdd:pfam13851  29 KSLKEEIAELKKKEERNEKLMSEIQQENKRLTEPLQKAQEEVEELRKQLEN--YEKDKQS 86
GBP_C pfam02841
Guanylate-binding protein, C-terminal domain; Transcription of the anti-viral ...
 40-108 5.71e-04

Guanylate-binding protein, C-terminal domain; Transcription of the anti-viral guanylate-binding protein (GBP) is induced by interferon-gamma during macrophage induction. This family contains GBP1 and GPB2, both GTPases capable of binding GTP, GDP and GMP.


Pssm-ID: 460721 [Multi-domain]  Cd Length: 297  Bit Score: 41.50  E-value: 5.71e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1720366917  40 MEQKMKEEQERRKKKEMEERMSLEETKEQILKLQEKLSALQEEKHQLFLQLKK----VLHEEEK---RRRKEQSDL 108
Cdd:pfam02841 202 KEKAIEAERAKAEAAEAEQELLREKQKEEEQMMEAQERSYQEHVKQLIEKMEAereqLLAEQERmleHKLQEQEEL 277
PAT1 pfam09770
Topoisomerase II-associated protein PAT1; Members of this family are necessary for accurate ...
 187-338 7.54e-04

Topoisomerase II-associated protein PAT1; Members of this family are necessary for accurate chromosome transmission during cell division.


Pssm-ID: 401645 [Multi-domain]  Cd Length: 846  Bit Score: 41.56  E-value: 7.54e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366917 187 AYGTAQPPPHYGPTQPAYSPSQQLRAPSAFPAVQYLSQPQP----QPYAVHGHFQPTQTgfLQ-PGSTLSLQKQMEHANQ 261
Cdd:pfam09770 207 AKKPAQQPAPAPAQPPAAPPAQQAQQQQQFPPQIQQQQQPQqqpqQPQQHPGQGHPVTI--LQrPQSPQPDPAQPSIQPQ 284

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1720366917 262 QTSFSDSSSLRPMHPQALHPAPGLLASPQLPVQIQAAGKALPPPANLAPdslssntaRTQDSITSNHQrAPAHPPSL 338
Cdd:pfam09770 285 AQQFHQQPPPVPVQPTQILQNPNRLSAARVGYPQNPQPGVQPAPAHQAH--------RQQGSFGRQAP-IITHPQQL 352
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 36-284 8.35e-04

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 40.97  E-value: 8.35e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366917  36 VDKMMEQ--KMKEEQERRKKKEMEERMSLEETKEQILKLQEKLSALQEEKHQLFLQLKKVLHEEEKRRRKEQSDLTTLTS 113
Cdd:COG3883   124 LSKIADAdaDLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEA 203

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366917 114 AAYQQSLTVHTGTHLLSMQGSPGGHNRPGTLMAADRAKQMFGPQVLTTRHYVGSAAAFAGTPEHGQFQGSPGGAYGTAQP 193
Cdd:COG3883   204 ELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAASAAGAGAAGAAGAAAGSAGAAGAAAGAAGAGAAAASAAG 283

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366917 194 PPHYGPTQPAYSPSQQLRAPSAFPAVQYLSQPQPQPYAVHGHFQPTQTGFLQPGSTLSLQKQMEHANQQTSFSDSSSLRP 273
Cdd:COG3883   284 GGAGGAGGGGGGGGAASGGSGGGSGGAGGVGSGGGAGAVVGGASAGGGGGSGGGGGSSGGGSGGGGGGGGGGGGSSSGGG 363

                         250
                  ....*....|.
gi 1720366917 274 MHPQALHPAPG 284
Cdd:COG3883   364 GGGVGLSVGGG 374
PTZ00121 PTZ00121
MAEBL; Provisional
 41-105 1.00e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 41.28  E-value: 1.00e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1720366917   41 EQKMKEEQERrkkKEMEERMSLEETK--EQILKLQEKLSALQEEKHQLFLQLKKvlHEEEKRRRKEQ 105
Cdd:PTZ00121  1604 EKKMKAEEAK---KAEEAKIKAEELKkaEEEKKKVEQLKKKEAEEKKKAEELKK--AEEENKIKAAE 1665
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
41-109 1.12e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 41.20  E-value: 1.12e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366917  41 EQKMKEEQERRKKKE-MEERmsLEETKEQILKLQEKLSALqEEKHQLFlQLKKVLHEEEKRRRKEQSDLT 109
Cdd:PRK03918  320 EEEINGIEERIKELEeKEER--LEELKKKLKELEKRLEEL-EERHELY-EEAKAKKEELERLKKRLTGLT 385
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
 41-117 1.15e-03

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


Pssm-ID: 375164 [Multi-domain]  Cd Length: 722  Bit Score: 40.88  E-value: 1.15e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1720366917  41 EQKMKEEQERRKKKEMEERMSLEETKEQILKLQEKLSALQEEKHqlflQLKKVLHEEEKRRRKEQSDLTTLTSAAYQ 117
Cdd:pfam17380 533 ERRREAEEERRKQQEMEERRRIQEQMRKATEERSRLEAMERERE----MMRQIVESEKARAEYEATTPITTIKPIYR 605
DDRGK pfam09756
DDRGK domain; This is a family of proteins of approximately 300 residues, found in plants and ...
 38-113 1.33e-03

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: 39.25  E-value: 1.33e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1720366917  38 KMMEQKMKEEQERRKKKEMEERmSLEETKEQIlKLQEKLSALQEEKhqlflqlkkvlhEEEKRRRKEQSDLTTLTS 113
Cdd:pfam09756  19 QQREAEEEEREEREKLEEKREE-EYKEREERE-EEAEKEKEEEERK------------QEEEQERKEQEEYEKLKS 80
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
42-118 1.43e-03

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 40.27  E-value: 1.43e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366917  42 QKMKEEQERRKKKEMEERMSLEETKEQILKLQEKLSALQEEKHQLFLQLKKVLHEE---EKRRRKEQSDLTTLTSAAYQQ 118
Cdd:COG4372    69 EQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERqdlEQQRKQLEAQIAELQSEIAER 148
UDM1_RNF168_RNF169-like cd22249
UDM1 (ubiquitin-dependent DSB recruitment module 1) found in RING finger proteins RNF168, ...
 41-105 1.55e-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: 36.48  E-value: 1.55e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1720366917  41 EQKMKEEQERRKKKEMEERMSLeetkEQILKLQEklsalqEEKHQLFLQLkkvlheEEKRRRKEQ 105
Cdd:cd22249    13 AQLKKLEEERRKEREEEEKASE----ELIRKLQE------EEERQRKRER------EEQLKQDEE 61
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
 41-105 1.75e-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: 39.90  E-value: 1.75e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1720366917  41 EQKMKEEQER----RKKKEME--ERMSLEETKEQILKLQEKLSALQEEKHQLFLQLKKVLHEEEKRRRKEQ 105
Cdd:pfam13868 254 EEAEREEEEFermlRKQAEDEeiEQEEAEKRRMKRLEHRRELEKQIEEREEQRAAEREEELEEGERLREEE 324
GBP_C pfam02841
Guanylate-binding protein, C-terminal domain; Transcription of the anti-viral ...
 39-108 1.85e-03

Guanylate-binding protein, C-terminal domain; Transcription of the anti-viral guanylate-binding protein (GBP) is induced by interferon-gamma during macrophage induction. This family contains GBP1 and GPB2, both GTPases capable of binding GTP, GDP and GMP.


Pssm-ID: 460721 [Multi-domain]  Cd Length: 297  Bit Score: 39.58  E-value: 1.85e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366917  39 MMEQKMKEEQERrkKKEMEERMslEETKEQILKLQEKLsALQEEKHQLFLqLKKVLHEEEKRRRKEQSDL 108
Cdd:pfam02841 233 MMEAQERSYQEH--VKQLIEKM--EAEREQLLAEQERM-LEHKLQEQEEL-LKEGFKTEAESLQKEIQDL 296
Atrophin-1 pfam03154
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
 171-367 2.27e-03

Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian atrophy (DRPLA) gene. DRPLA OMIM:125370 is a progressive neurodegenerative disorder. It is caused by the expansion of a CAG repeat in the DRPLA gene on chromosome 12p. This results in an extended polyglutamine region in atrophin-1, that is thought to confer toxicity to the protein, possibly through altering its interactions with other proteins. The expansion of a CAG repeat is also the underlying defect in six other neurodegenerative disorders, including Huntington's disease. One interaction of expanded polyglutamine repeats that is thought to be pathogenic is that with the short glutamine repeat in the transcriptional coactivator CREB binding protein, CBP. This interaction draws CBP away from its usual nuclear location to the expanded polyglutamine repeat protein aggregates that are characteriztic of the polyglutamine neurodegenerative disorders. This interferes with CBP-mediated transcription and causes cytotoxicity.


Pssm-ID: 460830 [Multi-domain]  Cd Length: 991  Bit Score: 40.14  E-value: 2.27e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366917 171 FAGTPEHGQFQGSPG---GAYGTAQPPPHYGPTQPAYSPSQQLRAPSAFPAvqylsqPQPQPyavhgHFQPTQTGFLQPG 247
Cdd:pfam03154 298 FPLTPQSSQSQVPPGpspAAPGQSQQRIHTPPSQSQLQSQQPPREQPLPPA------PLSMP-----HIKPPPTTPIPQL 366

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366917 248 STLSLQKQMEHANQQTSFSDSSSLRP------------MHPQALHPAPGLLASPQLPVQIQAA-------GKALPPPANL 308
Cdd:pfam03154 367 PNPQSHKHPPHLSGPSPFQMNSNLPPppalkplsslstHHPPSAHPPPLQLMPQSQQLPPPPAqppvltqSQSLPPPAAS 446

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1720366917 309 APDSLSSNTARTQdSITSNHQRAPAHPPSLRLGSYVPQT--NKMYKMYPPSCLSAVYLLPI 367
Cdd:pfam03154 447 HPPTSGLHQVPSQ-SPFPQHPFVPGGPPPITPPSGPPTStsSAMPGIQPPSSASVSSSGPV 506
ERM_helical pfam20492
Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related ...
 40-106 2.28e-03

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: 37.59  E-value: 2.28e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1720366917  40 MEQKMKEEQERRKKKEMEermsLEETKEQILKLQEKLSALQEEKHQlfLQLKKVLHEEEKRRRKEQS 106
Cdd:pfam20492  11 LEERLKQYEEETKKAQEE----LEESEETAEELEEERRQAEEEAER--LEQKRQEAEEEKERLEESA 71
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 41-120 2.61e-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: 2.61e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366917  41 EQKMKEEQERRKKKEMEERMSLEETKEQILKLQEKLSALQEEKHQLFLQLKKVLHEEEKRRRKEQSDLTTLTSAAYQQSL 120
Cdd:COG1196   416 LERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLL 495
PAT1 pfam09770
Topoisomerase II-associated protein PAT1; Members of this family are necessary for accurate ...
 190-348 2.87e-03

Topoisomerase II-associated protein PAT1; Members of this family are necessary for accurate chromosome transmission during cell division.


Pssm-ID: 401645 [Multi-domain]  Cd Length: 846  Bit Score: 39.63  E-value: 2.87e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366917 190 TAQPPPHYGPTQPAYSPSQ------------QLRAPSAFPAVQYLSQPQPQPyavhGHFQPTQTGFLQPGSTLSLQKQME 257
Cdd:pfam09770 171 AAPAPAPQPAAQPASLPAPsrkmmsleeveaAMRAQAKKPAQQPAPAPAQPP----AAPPAQQAQQQQQFPPQIQQQQQP 246

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366917 258 HANQQTSFSDSSSLRPMH----PQALHPAPGLL-ASPQLPVQIQAAGKALPPPANLA--PDSLSSNTARTQDSITSNHQR 330
Cdd:pfam09770 247 QQQPQQPQQHPGQGHPVTilqrPQSPQPDPAQPsIQPQAQQFHQQPPPVPVQPTQILqnPNRLSAARVGYPQNPQPGVQP 326

                         170
                  ....*....|....*...
gi 1720366917 331 APAHPPSLRLGSYVPQTN 348
Cdd:pfam09770 327 APAHQAHRQQGSFGRQAP 344
Troponin pfam00992
Troponin; Troponin (Tn) contains three subunits, Ca2+ binding (TnC), inhibitory (TnI), and ...
 38-109 4.72e-03

Troponin; Troponin (Tn) contains three subunits, Ca2+ binding (TnC), inhibitory (TnI), and tropomyosin binding (TnT). this Pfam contains members of the TnT subunit. Troponin is a complex of three proteins, Ca2+ binding (TnC), inhibitory (TnI), and tropomyosin binding (TnT). The troponin complex regulates Ca++ induced muscle contraction. This family includes troponin T and troponin I. Troponin I binds to actin and troponin T binds to tropomyosin.


Pssm-ID: 460018 [Multi-domain]  Cd Length: 132  Bit Score: 36.77  E-value: 4.72e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366917  38 KMMEQKMKEE--QERRKKKEmEERMSLEETKEQiLKL----QEKLSALQEEKHQLFLQL---KKVLHEEEKRRRKEQSDL 108
Cdd:pfam00992   6 SLLLQKAAEEleFEQEKKEE-EKLRYLAERIPP-LRLrglsAEQLQELCEELHERIDKLeeeRYDIEEKVAKKDKEINDL 83


                  .
gi 1720366917 109 T 109
Cdd:pfam00992  84 K 84
PTZ00121 PTZ00121
MAEBL; Provisional
 41-105 4.91e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 39.35  E-value: 4.91e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1720366917   41 EQKMKEEQERR-----KKKEMEERMSLEETK--EQILKLQ-EKLSALQEEKHQLFLQLKKvlHEEEKRRRKEQ 105
Cdd:PTZ00121  1623 EELKKAEEEKKkveqlKKKEAEEKKKAEELKkaEEENKIKaAEEAKKAEEDKKKAEEAKK--AEEDEKKAAEA 1693
DUF4200 pfam13863
Domain of unknown function (DUF4200); This family is found in eukaryotes. It is a coiled-coil ...
 41-89 5.04e-03

Domain of unknown function (DUF4200); This family is found in eukaryotes. It is a coiled-coil domain of unknwon function.


Pssm-ID: 464003 [Multi-domain]  Cd Length: 119  Bit Score: 36.39  E-value: 5.04e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1720366917  41 EQKMKEEQERRKKKEMEER---MSLEETKEQILKLQEKLSALQeeKHQLFLQ 89
Cdd:pfam13863  65 LKKAEEETKLKKEKEKEIKkltAQIEELKSEISKLEEKLEEYK--PYEDFLE 114
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
 40-104 5.84e-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: 38.36  E-value: 5.84e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1720366917  40 MEQKMKEEQERRKKKEMEERMSLEETKEQILKLQEKLSALQEekHQLFLQLKKVLHEEEKRRRKE 104
Cdd:pfam13868  90 QEEYEEKLQEREQMDEIVERIQEEDQAEAEEKLEKQRQLREE--IDEFNEEQAEWKELEKEEERE 152
DDRGK pfam09756
DDRGK domain; This is a family of proteins of approximately 300 residues, found in plants and ...
 43-104 6.95e-03

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: 37.33  E-value: 6.95e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1720366917  43 KMKEEQERRKKKEMEERmsLEETKEQilKLQEKLSALQEEKHQLFLQLKK------VLHEEEKRRRKE 104
Cdd:pfam09756  10 KLELKEAKRQQREAEEE--EREEREK--LEEKREEEYKEREEREEEAEKEkeeeerKQEEEQERKEQE 73
Casc1_N pfam15927
Cancer susceptibility candidate 1 N-terminus; This presumed domain is functionally ...
 45-103 8.43e-03

Cancer susceptibility candidate 1 N-terminus; This presumed domain is functionally uncharacterized. This domain family is found in eukaryotes, and is approximately 200 amino acids in length. The family is found in association with pfam12366. There are two completely conserved residues (N and W) that may be functionally important.


Pssm-ID: 464947 [Multi-domain]  Cd Length: 201  Bit Score: 37.34  E-value: 8.43e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1720366917  45 KEEQERRKKKEMEERMSLEETKEQILKLQEKLSALQEEKHQLFlQLKKVLHEEEKRRRK 103
Cdd:pfam15927   4 REEEEERLRAEEEEAERLEEERREEEEEERLAAEQDRRAEELE-ELKHLLEERKEALEK 61
GBP_C cd16269
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal ...
 38-108 9.10e-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: 37.56  E-value: 9.10e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1720366917  38 KMMEQKMKEEQERRKKKEMEERM-SLEETKEQIL-KLQEKLSALQEEKHQLfLQLKKVLHEEEKRRR-KEQSDL 108
Cdd:cd16269   210 AEQERKLLEEQQRELEQKLEDQErSYEEHLRQLKeKMEEERENLLKEQERA-LESKLKEQEALLEEGfKEQAEL 282
PTZ00121 PTZ00121
MAEBL; Provisional
 38-105 9.46e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 38.20  E-value: 9.46e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1720366917   38 KMMEQKMKEEQERRK----KKEMEERMSLEET---KEQILKLQEKLSALQEEKHQLFLQLKKvlHEEEKRRRKEQ 105
Cdd:PTZ00121  1662 KAAEEAKKAEEDKKKaeeaKKAEEDEKKAAEAlkkEAEEAKKAEELKKKEAEEKKKAEELKK--AEEENKIKAEE 1734
 
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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