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Conserved domains on  [gi|31980980|ref|NP_062700|]
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G protein pathway suppressor 2 [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 3.68e-76

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: 234.81  E-value: 3.68e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980980     5 LERPKLSNAMARALHRHIMMERERKRQEEEEvdKMMEQKMKEEQERRKKkemEERMSLEETKEQILKLQEKLSALQEEKH 84
Cdd:pfam15991   1 AARPKMSEQMWRALKRHIMRERERKKQEQEA--KMEEERLRREREEREK---EDRMTLEETKEQILKLEKKLADLKEEKH 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980980    85 QLFLQLKKVLHEEEKRRR--KEQSDLTTLTSAAYQqsltvhTGTHLLSMQGSPGGHNRPGTLMAADRAKQMFGPQVLTTr 162
Cdd:pfam15991  76 QLFLQLKKVLHEDETRKRqlKEQSELFALQQAAAQ------VFLPQLSMQGQPHHQQHPGPQVGVLKRTRSPSPPVQQQ- 148

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980980   163 HYVGSAAAFAGTPEHGQFQGSPGGAYGTAQPPPHYGPTQPAYSPSQQLrapsAFPAVQYLSQPQPQPYAVHGHfqptQTG 242
Cdd:pfam15991 149 AYYKQPAFSPGYAEHGQQKHDDGRRGYDVARFGSWNKSTAQYPPSGQL----FYPTHQYLPPPQTQGQADARL----QTI 220

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|..
gi 31980980   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 3.68e-76

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: 234.81  E-value: 3.68e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980980     5 LERPKLSNAMARALHRHIMMERERKRQEEEEvdKMMEQKMKEEQERRKKkemEERMSLEETKEQILKLQEKLSALQEEKH 84
Cdd:pfam15991   1 AARPKMSEQMWRALKRHIMRERERKKQEQEA--KMEEERLRREREEREK---EDRMTLEETKEQILKLEKKLADLKEEKH 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980980    85 QLFLQLKKVLHEEEKRRR--KEQSDLTTLTSAAYQqsltvhTGTHLLSMQGSPGGHNRPGTLMAADRAKQMFGPQVLTTr 162
Cdd:pfam15991  76 QLFLQLKKVLHEDETRKRqlKEQSELFALQQAAAQ------VFLPQLSMQGQPHHQQHPGPQVGVLKRTRSPSPPVQQQ- 148

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980980   163 HYVGSAAAFAGTPEHGQFQGSPGGAYGTAQPPPHYGPTQPAYSPSQQLrapsAFPAVQYLSQPQPQPYAVHGHfqptQTG 242
Cdd:pfam15991 149 AYYKQPAFSPGYAEHGQQKHDDGRRGYDVARFGSWNKSTAQYPPSGQL----FYPTHQYLPPPQTQGQADARL----QTI 220

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|..
gi 31980980   243 FLQPGSTLSLQKQMEHANQQTSFSDSSSLRPM-HPQALH-PAPGLLASPQLP 292
Cdd:pfam15991 221 YPQPGYALPLQQQYEHANQPSPFVSSSPLKQMqSPKAGPgPQPMQLSVLHIP 272
PTZ00121 PTZ00121
MAEBL; Provisional
 41-105 7.81e-04

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 41.28  E-value: 7.81e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 31980980    41 EQKMKEEQERrkkKEMEERMSLEETK--EQILKLQEKLSALQEEKHQLFLQLKKvlHEEEKRRRKEQ 105
Cdd:PTZ00121 1604 EKKMKAEEAK---KAEEAKIKAEELKkaEEEKKKVEQLKKKEAEEKKKAEELKK--AEEENKIKAAE 1665
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 36-284 1.18e-03

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 40.20  E-value: 1.18e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980980  36 VDKMMEQ--KMKEEQERRKKKEMEERMSLEETKEQILKLQEKLSALQEEKHQLFLQLKKVLHEEEKRRRKEQSDLTTLTS 113
Cdd:COG3883 124 LSKIADAdaDLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEA 203

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980980 114 AAYQQSLTVHTGTHLLSMQGSPGGHNRPGTLMAADRAKQMFGPQVLTTRHYVGSAAAFAGTPEHGQFQGSPGGAYGTAQP 193
Cdd:COG3883 204 ELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAASAAGAGAAGAAGAAAGSAGAAGAAAGAAGAGAAAASAAG 283

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980980 194 PPHYGPTQPAYSPSQQLRAPSAFPAVQYLSQPQPQPYAVHGHFQPTQTGFLQPGSTLSLQKQMEHANQQTSFSDSSSLRP 273
Cdd:COG3883 284 GGAGGAGGGGGGGGAASGGSGGGSGGAGGVGSGGGAGAVVGGASAGGGGGSGGGGGSSGGGSGGGGGGGGGGGGSSSGGG 363

                       250
                ....*....|.
gi 31980980 274 MHPQALHPAPG 284
Cdd:COG3883 364 GGGVGLSVGGG 374
UDM1_RNF168_RNF169-like cd22249
UDM1 (ubiquitin-dependent DSB recruitment module 1) found in RING finger proteins RNF168, ...
 41-105 7.20e-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: 34.55  E-value: 7.20e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 31980980  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 3.68e-76

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: 234.81  E-value: 3.68e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980980     5 LERPKLSNAMARALHRHIMMERERKRQEEEEvdKMMEQKMKEEQERRKKkemEERMSLEETKEQILKLQEKLSALQEEKH 84
Cdd:pfam15991   1 AARPKMSEQMWRALKRHIMRERERKKQEQEA--KMEEERLRREREEREK---EDRMTLEETKEQILKLEKKLADLKEEKH 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980980    85 QLFLQLKKVLHEEEKRRR--KEQSDLTTLTSAAYQqsltvhTGTHLLSMQGSPGGHNRPGTLMAADRAKQMFGPQVLTTr 162
Cdd:pfam15991  76 QLFLQLKKVLHEDETRKRqlKEQSELFALQQAAAQ------VFLPQLSMQGQPHHQQHPGPQVGVLKRTRSPSPPVQQQ- 148

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980980   163 HYVGSAAAFAGTPEHGQFQGSPGGAYGTAQPPPHYGPTQPAYSPSQQLrapsAFPAVQYLSQPQPQPYAVHGHfqptQTG 242
Cdd:pfam15991 149 AYYKQPAFSPGYAEHGQQKHDDGRRGYDVARFGSWNKSTAQYPPSGQL----FYPTHQYLPPPQTQGQADARL----QTI 220

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|..
gi 31980980   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 9.53e-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: 50.82  E-value: 9.53e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 31980980    41 EQKMKEEQERRKKKEMEERMslEETKEQILKLQEKLsalqEEKHQLFLQLKKVLHEEEKRRRKEQS 106
Cdd:pfam15346  68 EERRKEEEERKKREELERIL--EENNRKIEEAQRKE----AEERLAMLEEQRRMKEERQRREKEEE 127
SMC_N pfam02463
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...
 41-102 2.62e-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: 42.65  E-value: 2.62e-04
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 31980980     41 EQKMKEEQERRKKKEMEERMSLEETKEQILKLQEKLSALQEEKHQLFLQLKKVLHEEEKRRR 102
Cdd:pfam02463  166 RLKRKKKEALKKLIEETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEYLL 227
CAF-1_p150 pfam11600
Chromatin assembly factor 1 complex p150 subunit, N-terminal; CAF-1_p150 is a polypeptide ...
 38-109 3.04e-04

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: 40.83  E-value: 3.04e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 31980980    38 KMMEQKMKEEQERRKKKEMEERMSLEETKEQILKLQEKLSALQ---EEKHQlfLQLKKVLHEEEKRRRKEQSDLT 109
Cdd:pfam11600  59 KKEEEKELKEKERREKKEKDEKEKAEKLRLKEEKRKEKQEALEaklEEKRK--KEEEKRLKEEEKRIKAEKAEIT 131
GAS pfam13851
Growth-arrest specific micro-tubule binding; This family is the highly conserved central ...
 42-91 4.59e-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: 40.66  E-value: 4.59e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 31980980    42 QKMKEEQERRKKKEMEERMSLEETKEQILKLQEKLSALQEEKHQLFLQLK 91
Cdd:pfam13851  29 KSLKEEIAELKKKEERNEKLMSEIQQENKRLTEPLQKAQEEVEELRKQLE 78
PTZ00121 PTZ00121
MAEBL; Provisional
 41-105 7.81e-04

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 41.28  E-value: 7.81e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 31980980    41 EQKMKEEQERrkkKEMEERMSLEETK--EQILKLQEKLSALQEEKHQLFLQLKKvlHEEEKRRRKEQ 105
Cdd:PTZ00121 1604 EKKMKAEEAK---KAEEAKIKAEELKkaEEEKKKVEQLKKKEAEEKKKAEELKK--AEEENKIKAAE 1665
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
41-109 8.76e-04

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 41.20  E-value: 8.76e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980980   41 EQKMKEEQERRKKKE-MEERmsLEETKEQILKLQEKLSALqEEKHQLFlQLKKVLHEEEKRRRKEQSDLT 109
Cdd:PRK03918 320 EEEINGIEERIKELEeKEER--LEELKKKLKELEKRLEEL-EERHELY-EEAKAKKEELERLKKRLTGLT 385
GBP_C pfam02841
Guanylate-binding protein, C-terminal domain; Transcription of the anti-viral ...
 40-108 1.03e-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: 40.35  E-value: 1.03e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 31980980    40 MEQKMKEEQERRKKKEMEERMSLEETKEQILKLQEKLSALQEEKHQLFLQLKK----VLHEEEK---RRRKEQSDL 108
Cdd:pfam02841 202 KEKAIEAERAKAEAAEAEQELLREKQKEEEQMMEAQERSYQEHVKQLIEKMEAereqLLAEQERmleHKLQEQEEL 277
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 36-284 1.18e-03

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 40.20  E-value: 1.18e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980980  36 VDKMMEQ--KMKEEQERRKKKEMEERMSLEETKEQILKLQEKLSALQEEKHQLFLQLKKVLHEEEKRRRKEQSDLTTLTS 113
Cdd:COG3883 124 LSKIADAdaDLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEA 203

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980980 114 AAYQQSLTVHTGTHLLSMQGSPGGHNRPGTLMAADRAKQMFGPQVLTTRHYVGSAAAFAGTPEHGQFQGSPGGAYGTAQP 193
Cdd:COG3883 204 ELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAASAAGAGAAGAAGAAAGSAGAAGAAAGAAGAGAAAASAAG 283

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980980 194 PPHYGPTQPAYSPSQQLRAPSAFPAVQYLSQPQPQPYAVHGHFQPTQTGFLQPGSTLSLQKQMEHANQQTSFSDSSSLRP 273
Cdd:COG3883 284 GGAGGAGGGGGGGGAASGGSGGGSGGAGGVGSGGGAGAVVGGASAGGGGGSGGGGGSSGGGSGGGGGGGGGGGGSSSGGG 363

                       250
                ....*....|.
gi 31980980 274 MHPQALHPAPG 284
Cdd:COG3883 364 GGGVGLSVGGG 374
MAP7 pfam05672
MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is ...
 41-105 1.28e-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: 1.28e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 31980980    41 EQKMKEEQERRKKkEMEERMSLEETKEQilklQEKLSALQEEKHQLFLQLKKVLHEEEKRRRKEQ 105
Cdd:pfam05672  25 EQREREEQERLEK-EEEERLRKEELRRR----AEEERARREEEARRLEEERRREEEERQRKAEEE 84
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
 41-117 1.50e-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: 40.49  E-value: 1.50e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 31980980    41 EQKMKEEQERRKKKEMEERMSLEETKEQILKLQEKLSALQEEKHqlflQLKKVLHEEEKRRRKEQSDLTTLTSAAYQ 117
Cdd:pfam17380 533 ERRREAEEERRKQQEMEERRRIQEQMRKATEERSRLEAMERERE----MMRQIVESEKARAEYEATTPITTIKPIYR 605
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 41-120 3.06e-03

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 39.53  E-value: 3.06e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980980  41 EQKMKEEQERRKKKEMEERMSLEETKEQILKLQEKLSALQEEKHQLFLQLKKVLHEEEKRRRKEQSDLTTLTSAAYQQSL 120
Cdd:COG1196 416 LERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLL 495
PAT1 pfam09770
Topoisomerase II-associated protein PAT1; Members of this family are necessary for accurate ...
 187-320 3.35e-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: 39.25  E-value: 3.35e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980980   187 AYGTAQPPPHYGPTQPAYSPSQQLRAPSAFPAVQYLSQPQP----QPYAVHGHFQPTQTgfLQ-PGSTLSLQKQMEHANQ 261
Cdd:pfam09770 207 AKKPAQQPAPAPAQPPAAPPAQQAQQQQQFPPQIQQQQQPQqqpqQPQQHPGQGHPVTI--LQrPQSPQPDPAQPSIQPQ 284

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 31980980   262 QTSFSDSSSLRPMHP-QALH----PAPGLLASPQLPVQIQAAGKSGFATTSQP--GPRLPFIQHSQ 320
Cdd:pfam09770 285 AQQFHQQPPPVPVQPtQILQnpnrLSAARVGYPQNPQPGVQPAPAHQAHRQQGsfGRQAPIITHPQ 350
DDRGK pfam09756
DDRGK domain; This is a family of proteins of approximately 300 residues, found in plants and ...
 38-113 3.54e-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: 37.71  E-value: 3.54e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 31980980    38 KMMEQKMKEEQERRKKKEMEERmSLEETKEQIlKLQEKLSALQEEKhqlflqlkkvlhEEEKRRRKEQSDLTTLTS 113
Cdd:pfam09756  19 QQREAEEEEREEREKLEEKREE-EYKEREERE-EEAEKEKEEEERK------------QEEEQERKEQEEYEKLKS 80
GBP_C pfam02841
Guanylate-binding protein, C-terminal domain; Transcription of the anti-viral ...
 39-108 3.67e-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: 38.42  E-value: 3.67e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980980    39 MMEQKMKEEQERrkKKEMEERMslEETKEQILKLQEKLsALQEEKHQLFLqLKKVLHEEEKRRRKEQSDL 108
Cdd:pfam02841 233 MMEAQERSYQEH--VKQLIEKM--EAEREQLLAEQERM-LEHKLQEQEEL-LKEGFKTEAESLQKEIQDL 296
PTZ00121 PTZ00121
MAEBL; Provisional
 41-105 3.88e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 39.35  E-value: 3.88e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 31980980    41 EQKMKEEQERR-----KKKEMEERMSLEETK--EQILKLQ-EKLSALQEEKHQLFLQLKKvlHEEEKRRRKEQ 105
Cdd:PTZ00121 1623 EELKKAEEEKKkveqlKKKEAEEKKKAEELKkaEEENKIKaAEEAKKAEEDKKKAEEAKK--AEEDEKKAAEA 1693
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
42-118 3.96e-03

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 38.73  E-value: 3.96e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980980  42 QKMKEEQERRKKKEMEERMSLEETKEQILKLQEKLSALQEEKHQLFLQLKKVLHEE---EKRRRKEQSDLTTLTSAAYQQ 118
Cdd:COG4372  69 EQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERqdlEQQRKQLEAQIAELQSEIAER 148
Casc1_N pfam15927
Cancer susceptibility candidate 1 N-terminus; This presumed domain is functionally ...
 45-103 6.93e-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: 6.93e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 31980980    45 KEEQERRKKKEMEERMSLEETKEQILKLQEKLSALQEEKHQLFlQLKKVLHEEEKRRRK 103
Cdd:pfam15927   4 REEEEERLRAEEEEAERLEEERREEEEEERLAAEQDRRAEELE-ELKHLLEERKEALEK 61
Troponin pfam00992
Troponin; Troponin (Tn) contains three subunits, Ca2+ binding (TnC), inhibitory (TnI), and ...
 38-109 6.99e-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: 36.39  E-value: 6.99e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980980    38 KMMEQKMKEE--QERRKKKEmEERMSLEETKEQiLKL----QEKLSALQEEKHQLFLQL---KKVLHEEEKRRRKEQSDL 108
Cdd:pfam00992   6 SLLLQKAAEEleFEQEKKEE-EKLRYLAERIPP-LRLrglsAEQLQELCEELHERIDKLeeeRYDIEEKVAKKDKEINDL 83


                  .
gi 31980980   109 T 109
Cdd:pfam00992  84 K 84
UDM1_RNF168_RNF169-like cd22249
UDM1 (ubiquitin-dependent DSB recruitment module 1) found in RING finger proteins RNF168, ...
 41-105 7.20e-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: 34.55  E-value: 7.20e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 31980980  41 EQKMKEEQERRKKKEMEERMSLeetkEQILKLQEklsalqEEKHQLFLQLkkvlheEEKRRRKEQ 105
Cdd:cd22249  13 AQLKKLEEERRKEREEEEKASE----ELIRKLQE------EEERQRKRER------EEQLKQDEE 61
PTZ00121 PTZ00121
MAEBL; Provisional
 38-105 7.50e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 38.20  E-value: 7.50e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 31980980    38 KMMEQKMKEEQERRK----KKEMEERMSLEET---KEQILKLQEKLSALQEEKHQLFLQLKKvlHEEEKRRRKEQ 105
Cdd:PTZ00121 1662 KAAEEAKKAEEDKKKaeeaKKAEEDEKKAAEAlkkEAEEAKKAEELKKKEAEEKKKAEELKK--AEEENKIKAEE 1734
PHA03247 PHA03247
large tegument protein UL36; Provisional
 183-326 7.74e-03

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 38.38  E-value: 7.74e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980980   183 SPGGAY---GTAQPPPHYgPTQPAYSPSQQLRAPSAFPAVQYLSQPQPQPYAVHGHFQPTQTgflQPGSTLSLQKQMEHA 259
Cdd:PHA03247 2857 APGGDVrrrPPSRSPAAK-PAAPARPPVRRLARPAVSRSTESFALPPDQPERPPQPQAPPPP---QPQPQPPPPPQPQPP 2932

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 31980980   260 NQQTSFSDSSSLRPMHPQALHPAPGLLASPQLPVQIQAAGKSGFATTSQPGPRLPFIQHSQNPRFYH 326
Cdd:PHA03247 2933 PPPPPRPQPPLAPTTDPAGAGEPSGAVPQPWLGALVPGRVAVPRFRVPQPAPSREAPASSTPPLTGH 2999
CAF-1_p150 pfam11600
Chromatin assembly factor 1 complex p150 subunit, N-terminal; CAF-1_p150 is a polypeptide ...
 5-107 9.02e-03

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: 36.59  E-value: 9.02e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980980     5 LERPKLSNAMARALHRHIMMERERKRQEEEEVDKMMEQKMKEEQERRKKKEMEERMSLE-ETKEQILKLQEKLSALQEEK 83
Cdd:pfam11600  18 LEKDKERLRRQLKLEAEKEEKERLKEEAKAEKERAKEEARRKKEEEKELKEKERREKKEkDEKEKAEKLRLKEEKRKEKQ 97

                          90       100
                  ....*....|....*....|....
gi 31980980    84 HQLFLQLKKVLHEEEKRRRKEQSD 107
Cdd:pfam11600  98 EALEAKLEEKRKKEEEKRLKEEEK 121
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
 41-105 9.35e-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: 37.21  E-value: 9.35e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 31980980    41 EQKMKEEQER----RKKKEME--ERMSLEETKEQILKLQEKLSALQEEKHQLFLQLKKVLHEEEKRRRKEQ 105
Cdd:pfam13868 254 EEAEREEEEFermlRKQAEDEeiEQEEAEKRRMKRLEHRRELEKQIEEREEQRAAEREEELEEGERLREEE 324
 
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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