NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|564372912|ref|XP_006246845|]
View 

G protein pathway suppressor 2 isoform X1 [Rattus norvegicus]

Protein Classification

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

UDM1_RNF168_RNF169-like domain-containing protein

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

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 9.64e-81

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: 249.07  E-value: 9.64e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372912    5 LERPKLSNAMARALHRHIMMERERKRQEEEEvdKMMEQKMKEEQERRKKkemEERMSLEETKEQILKLQQKLSALQEEKH 84
Cdd:pfam15991   1 AARPKMSEQMWRALKRHIMRERERKKQEQEA--KMEEERLRREREEREK---EDRMTLEETKEQILKLEKKLADLKEEKH 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372912   85 QLFLQLKKVLHEEEKRRR--KEQSDLTTLTSAAYQqsltvhTGTHLLSMQGSPGGHNRPGTLMAADRAKQMFGPQVLTTr 162
Cdd:pfam15991  76 QLFLQLKKVLHEDETRKRqlKEQSELFALQQAAAQ------VFLPQLSMQGQPHHQQHPGPQVGVLKRTRSPSPPVQQQ- 148

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372912  163 HYVGSAAAFAGTPEHGQFQGSPGGAYGTAQPPPHYGPTQPAYSPSQQLrapsAFPAVQYLSQPQPQPYAVHGHfqptQTG 242
Cdd:pfam15991 149 AYYKQPAFSPGYAEHGQQKHDDGRRGYDVARFGSWNKSTAQYPPSGQL----FYPTHQYLPPPQTQGQADARL----QTI 220

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|..
gi 564372912  243 FLQPGSALSLQKQMEHANQQTSFSDSSSLRPM-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 9.64e-81

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: 249.07  E-value: 9.64e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372912    5 LERPKLSNAMARALHRHIMMERERKRQEEEEvdKMMEQKMKEEQERRKKkemEERMSLEETKEQILKLQQKLSALQEEKH 84
Cdd:pfam15991   1 AARPKMSEQMWRALKRHIMRERERKKQEQEA--KMEEERLRREREEREK---EDRMTLEETKEQILKLEKKLADLKEEKH 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372912   85 QLFLQLKKVLHEEEKRRR--KEQSDLTTLTSAAYQqsltvhTGTHLLSMQGSPGGHNRPGTLMAADRAKQMFGPQVLTTr 162
Cdd:pfam15991  76 QLFLQLKKVLHEDETRKRqlKEQSELFALQQAAAQ------VFLPQLSMQGQPHHQQHPGPQVGVLKRTRSPSPPVQQQ- 148

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372912  163 HYVGSAAAFAGTPEHGQFQGSPGGAYGTAQPPPHYGPTQPAYSPSQQLrapsAFPAVQYLSQPQPQPYAVHGHfqptQTG 242
Cdd:pfam15991 149 AYYKQPAFSPGYAEHGQQKHDDGRRGYDVARFGSWNKSTAQYPPSGQL----FYPTHQYLPPPQTQGQADARL----QTI 220

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|..
gi 564372912  243 FLQPGSALSLQKQMEHANQQTSFSDSSSLRPM-HPQALH-PAPGLLASPQLP 292
Cdd:pfam15991 221 YPQPGYALPLQQQYEHANQPSPFVSSSPLKQMqSPKAGPgPQPMQLSVLHIP 272
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 36-284 8.65e-04

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 41.35  E-value: 8.65e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372912  36 VDKMMEQ--KMKEEQERRKKKEMEERMSLEETKEQILKLQQKLSALQEEKHQLFLQLKKVLHEEEKRRRKEQSDLTTLTS 113
Cdd:COG3883  124 LSKIADAdaDLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEA 203

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372912 114 AAYQQSLTVHTGTHLLSMQGSPGGHNRPGTLMAADRAKQMFGPQVLTTRHYVGSAAAFAGTPEHGQFQGSPGGAYGTAQP 193
Cdd:COG3883  204 ELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAASAAGAGAAGAAGAAAGSAGAAGAAAGAAGAGAAAASAAG 283

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372912 194 PPHYGPTQPAYSPSQQLRAPSAFPAVQYLSQPQPQPYAVHGHFQPTQTGFLQPGSALSLQKQMEHANQQTSFSDSSSLRP 273
Cdd:COG3883  284 GGAGGAGGGGGGGGAASGGSGGGSGGAGGVGSGGGAGAVVGGASAGGGGGSGGGGGSSGGGSGGGGGGGGGGGGSSSGGG 363

                        250
                 ....*....|.
gi 564372912 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 1.30e-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: 36.86  E-value: 1.30e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 564372912  41 EQKMKEEQERRKKKEMEERMSLeetkEQILKLQqklsalQEEKHQLFLQLkkvlheEEKRRRKEQ 105
Cdd:cd22249   13 AQLKKLEEERRKEREEEEKASE----ELIRKLQ------EEEERQRKRER------EEQLKQDEE 61
PHA03377 PHA03377
EBNA-3C; Provisional
 81-377 1.92e-03

EBNA-3C; Provisional


Pssm-ID: 177614 [Multi-domain]  Cd Length: 1000  Bit Score: 40.42  E-value: 1.92e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372912   81 EEKHQLFLQLKKVLHEEEKRRRKEQSDLTTLTSAAYQQSLTVH----TGTHLLSMQGSP-GGHNRPGTLMAADRAKQMFG 155
Cdd:PHA03377  702 EESHLSSMSPTQPISHEEQPRYEDPDDPLDLSLHPDQAPPPSHqapySGHEEPQAQQAPyPGYWEPRPPQAPYLGYQEPQ 781

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372912  156 PQVLTTRHYVGSAAAFAGTPEHGQFQGSpggaYGTAQPPPHYGPTQPAYSPsqqlRAPsafpavqYLSqPQPQPYAVHGH 235
Cdd:PHA03377  782 AQGVQVSSYPGYAGPWGLRAQHPRYRHS----WAYWSQYPGHGHPQGPWAP----RPP-------HLP-PQWDGSAGHGQ 845

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372912  236 FQPTQTGFLQPGSA-----LSLQKQMEHANQQTSFSDSSSLRPMHPQALHPAPGLLASPQLPVQ------IQAAGKALPp 304
Cdd:PHA03377  846 DQVSQFPHLQSETGpprlqLSQVPQLPYSQTLVSSSAPSWSSPQPRAPIRPIPTRFPPPPMPLQdsmavgCDSSGTACP- 924

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 564372912  305 paNRALDSLSSNTARTHDSITSNHQITP----THPPSLRVGSYVSQTNKMYkiylpSCQSTVYLLPKPQKAVSYKAS 377
Cdd:PHA03377  925 --SMPFASDYSQGAFTPLDINAQTPKRPrveeSSHGPARCSQATTEAQEIL-----SDNSEISVFPKDAKQTDYDAS 994
 
Name Accession Description Interval E-value
G_path_suppress pfam15991
G-protein pathway suppressor; This family of proteins inhibits G-protein- and ...
 5-292 9.64e-81

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: 249.07  E-value: 9.64e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372912    5 LERPKLSNAMARALHRHIMMERERKRQEEEEvdKMMEQKMKEEQERRKKkemEERMSLEETKEQILKLQQKLSALQEEKH 84
Cdd:pfam15991   1 AARPKMSEQMWRALKRHIMRERERKKQEQEA--KMEEERLRREREEREK---EDRMTLEETKEQILKLEKKLADLKEEKH 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372912   85 QLFLQLKKVLHEEEKRRR--KEQSDLTTLTSAAYQqsltvhTGTHLLSMQGSPGGHNRPGTLMAADRAKQMFGPQVLTTr 162
Cdd:pfam15991  76 QLFLQLKKVLHEDETRKRqlKEQSELFALQQAAAQ------VFLPQLSMQGQPHHQQHPGPQVGVLKRTRSPSPPVQQQ- 148

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372912  163 HYVGSAAAFAGTPEHGQFQGSPGGAYGTAQPPPHYGPTQPAYSPSQQLrapsAFPAVQYLSQPQPQPYAVHGHfqptQTG 242
Cdd:pfam15991 149 AYYKQPAFSPGYAEHGQQKHDDGRRGYDVARFGSWNKSTAQYPPSGQL----FYPTHQYLPPPQTQGQADARL----QTI 220

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|..
gi 564372912  243 FLQPGSALSLQKQMEHANQQTSFSDSSSLRPM-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 4.19e-09

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: 55.06  E-value: 4.19e-09
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 564372912   41 EQKMKEEQERRKKKEMEERMslEETKEQILKLQQKLsalqEEKHQLFLQLKKVLHEEEKRRRKEQS 106
Cdd:pfam15346  68 EERRKEEEERKKREELERIL--EENNRKIEEAQRKE----AEERLAMLEEQRRMKEERQRREKEEE 127
MAP7 pfam05672
MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is ...
 41-105 2.22e-05

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: 44.26  E-value: 2.22e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 564372912   41 EQKMKEEQERRKKkEMEERMSLEETKEQILKLQQKlsalQEEKHQLFLQLKKVLHEEEKRRRKEQ 105
Cdd:pfam05672  25 EQREREEQERLEK-EEEERLRKEELRRRAEEERAR----REEEARRLEEERRREEEERQRKAEEE 84
CAF-1_p150 pfam11600
Chromatin assembly factor 1 complex p150 subunit, N-terminal; CAF-1_p150 is a polypeptide ...
 38-109 9.27e-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: 42.75  E-value: 9.27e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 564372912   38 KMMEQKMKEEQERRKKKEMEERMSLEETKEQILKLQQKLSALQ---EEKHQlfLQLKKVLHEEEKRRRKEQSDLT 109
Cdd:pfam11600  59 KKEEEKELKEKERREKKEKDEKEKAEKLRLKEEKRKEKQEALEaklEEKRK--KEEEKRLKEEEKRIKAEKAEIT 131
PAT1 pfam09770
Topoisomerase II-associated protein PAT1; Members of this family are necessary for accurate ...
 187-338 1.54e-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: 43.87  E-value: 1.54e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372912  187 AYGTAQPPPHYGPTQPAYSPSQQLRAPSAFPAVQYLSQPQP----QPYAVHGHFQPTQTgfLQ-PGSALSLQKQMEHANQ 261
Cdd:pfam09770 207 AKKPAQQPAPAPAQPPAAPPAQQAQQQQQFPPQIQQQQQPQqqpqQPQQHPGQGHPVTI--LQrPQSPQPDPAQPSIQPQ 284

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 564372912  262 QTSFSDSSSLRPMHPQALHPAPGLLASPQLPVQIQAAGKALPPPANRAldslssntARTHDSITSNHQITpTHPPSL 338
Cdd:pfam09770 285 AQQFHQQPPPVPVQPTQILQNPNRLSAARVGYPQNPQPGVQPAPAHQA--------HRQQGSFGRQAPII-THPQQL 352
GBP_C pfam02841
Guanylate-binding protein, C-terminal domain; Transcription of the anti-viral ...
 40-108 4.59e-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: 41.89  E-value: 4.59e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 564372912   40 MEQKMKEEQERRKKKEMEERMSLEETKEQILKLQQKLSALQEEKHQLFLQLKK----VLHEEEK---RRRKEQSDL 108
Cdd:pfam02841 202 KEKAIEAERAKAEAAEAEQELLREKQKEEEQMMEAQERSYQEHVKQLIEKMEAereqLLAEQERmleHKLQEQEEL 277
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
 41-113 5.14e-04

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: 42.42  E-value: 5.14e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 564372912   41 EQKMKEEQERRKKKEMEERMSLEETKEQILKLQQKLSALQEEKhQLFLQLKkvlheEEKRRRKEQSDLTTLTS 113
Cdd:pfam17380 533 ERRREAEEERRKQQEMEERRRIQEQMRKATEERSRLEAMERER-EMMRQIV-----ESEKARAEYEATTPITT 599
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 36-284 8.65e-04

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 41.35  E-value: 8.65e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372912  36 VDKMMEQ--KMKEEQERRKKKEMEERMSLEETKEQILKLQQKLSALQEEKHQLFLQLKKVLHEEEKRRRKEQSDLTTLTS 113
Cdd:COG3883  124 LSKIADAdaDLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEA 203

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372912 114 AAYQQSLTVHTGTHLLSMQGSPGGHNRPGTLMAADRAKQMFGPQVLTTRHYVGSAAAFAGTPEHGQFQGSPGGAYGTAQP 193
Cdd:COG3883  204 ELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAASAAGAGAAGAAGAAAGSAGAAGAAAGAAGAGAAAASAAG 283

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372912 194 PPHYGPTQPAYSPSQQLRAPSAFPAVQYLSQPQPQPYAVHGHFQPTQTGFLQPGSALSLQKQMEHANQQTSFSDSSSLRP 273
Cdd:COG3883  284 GGAGGAGGGGGGGGAASGGSGGGSGGAGGVGSGGGAGAVVGGASAGGGGGSGGGGGSSGGGSGGGGGGGGGGGGSSSGGG 363

                        250
                 ....*....|.
gi 564372912 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 1.30e-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: 36.86  E-value: 1.30e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 564372912  41 EQKMKEEQERRKKKEMEERMSLeetkEQILKLQqklsalQEEKHQLFLQLkkvlheEEKRRRKEQ 105
Cdd:cd22249   13 AQLKKLEEERRKEREEEEKASE----ELIRKLQ------EEEERQRKRER------EEQLKQDEE 61
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
42-118 1.73e-03

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 40.27  E-value: 1.73e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372912  42 QKMKEEQERRKKKEMEERMSLEETKEQILKLQQKLSALQEEKHQLFLQLKKVLHEE---EKRRRKEQSDLTTLTSAAYQQ 118
Cdd:COG4372   69 EQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERqdlEQQRKQLEAQIAELQSEIAER 148
PHA03377 PHA03377
EBNA-3C; Provisional
 81-377 1.92e-03

EBNA-3C; Provisional


Pssm-ID: 177614 [Multi-domain]  Cd Length: 1000  Bit Score: 40.42  E-value: 1.92e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372912   81 EEKHQLFLQLKKVLHEEEKRRRKEQSDLTTLTSAAYQQSLTVH----TGTHLLSMQGSP-GGHNRPGTLMAADRAKQMFG 155
Cdd:PHA03377  702 EESHLSSMSPTQPISHEEQPRYEDPDDPLDLSLHPDQAPPPSHqapySGHEEPQAQQAPyPGYWEPRPPQAPYLGYQEPQ 781

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372912  156 PQVLTTRHYVGSAAAFAGTPEHGQFQGSpggaYGTAQPPPHYGPTQPAYSPsqqlRAPsafpavqYLSqPQPQPYAVHGH 235
Cdd:PHA03377  782 AQGVQVSSYPGYAGPWGLRAQHPRYRHS----WAYWSQYPGHGHPQGPWAP----RPP-------HLP-PQWDGSAGHGQ 845

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372912  236 FQPTQTGFLQPGSA-----LSLQKQMEHANQQTSFSDSSSLRPMHPQALHPAPGLLASPQLPVQ------IQAAGKALPp 304
Cdd:PHA03377  846 DQVSQFPHLQSETGpprlqLSQVPQLPYSQTLVSSSAPSWSSPQPRAPIRPIPTRFPPPPMPLQdsmavgCDSSGTACP- 924

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 564372912  305 paNRALDSLSSNTARTHDSITSNHQITP----THPPSLRVGSYVSQTNKMYkiylpSCQSTVYLLPKPQKAVSYKAS 377
Cdd:PHA03377  925 --SMPFASDYSQGAFTPLDINAQTPKRPrveeSSHGPARCSQATTEAQEIL-----SDNSEISVFPKDAKQTDYDAS 994
SMC_N pfam02463
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...
 41-102 1.94e-03

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: 40.34  E-value: 1.94e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 564372912    41 EQKMKEEQERRKKKEMEERMSLEE--TKEQILKLQQKLSALQEEKHQLFLQLKKVLHEEEKRRR 102
Cdd:pfam02463  164 GSRLKRKKKEALKKLIEETENLAEliIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEYLL 227
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
41-109 1.95e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 40.43  E-value: 1.95e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372912  41 EQKMKEEQERRKKKE-MEERmsLEETKEQILKLQQKLSALqEEKHQLFlQLKKVLHEEEKRRRKEQSDLT 109
Cdd:PRK03918 320 EEEINGIEERIKELEeKEER--LEELKKKLKELEKRLEEL-EERHELY-EEAKAKKEELERLKKRLTGLT 385
PTZ00121 PTZ00121
MAEBL; Provisional
 41-105 2.72e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 40.12  E-value: 2.72e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 564372912   41 EQKMKEEQERrkkKEMEERMSLEETK--EQILKLQQKLSALQEEKHQLFLQLKKvlHEEEKRRRKEQ 105
Cdd:PTZ00121 1604 EKKMKAEEAK---KAEEAKIKAEELKkaEEEKKKVEQLKKKEAEEKKKAEELKK--AEEENKIKAAE 1665
GBP_C pfam02841
Guanylate-binding protein, C-terminal domain; Transcription of the anti-viral ...
 39-108 2.75e-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: 39.19  E-value: 2.75e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372912   39 MMEQKMKEEQERrkKKEMEERMslEETKEQILKLQQKLsALQEEKHQLFLqLKKVLHEEEKRRRKEQSDL 108
Cdd:pfam02841 233 MMEAQERSYQEH--VKQLIEKM--EAEREQLLAEQERM-LEHKLQEQEEL-LKEGFKTEAESLQKEIQDL 296
GAS pfam13851
Growth-arrest specific micro-tubule binding; This family is the highly conserved central ...
 42-101 3.07e-03

Growth-arrest specific micro-tubule binding; This family is the highly conserved central region of a number of metazoan proteins referred to as growth-arrest proteins. In mouse, Gas8 is predominantly a testicular protein, whose expression is developmentally regulated during puberty and spermatogenesis. In humans, it is absent in infertile males who lack the ability to generate gametes. The localization of Gas8 in the motility apparatus of post-meiotic gametocytes and mature spermatozoa, together with the detection of Gas8 also in cilia at the apical surfaces of epithelial cells lining the pulmonary bronchi and Fallopian tubes suggests that the Gas8 protein may have a role in the functioning of motile cellular appendages. Gas8 is a microtubule-binding protein localized to regions of dynein regulation in mammalian cells.


Pssm-ID: 464001 [Multi-domain]  Cd Length: 200  Bit Score: 38.73  E-value: 3.07e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372912   42 QKMKEEQERRKKKEMEERMSLEETKEQILKLQQKLSALQEEKHQLFLQLKKvlHEEEKRR 101
Cdd:pfam13851  29 KSLKEEIAELKKKEERNEKLMSEIQQENKRLTEPLQKAQEEVEELRKQLEN--YEKDKQS 86
DDRGK pfam09756
DDRGK domain; This is a family of proteins of approximately 300 residues, found in plants and ...
 38-113 3.13e-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: 38.48  E-value: 3.13e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 564372912   38 KMMEQKMKEEQERRKKKEMEERmSLEETKEQILKLQQKLSALQEEkhqlflqlkkvlhEEEKRRRKEQSDLTTLTS 113
Cdd:pfam09756  19 QQREAEEEEREEREKLEEKREE-EYKEREEREEEAEKEKEEEERK-------------QEEEQERKEQEEYEKLKS 80
Cgr1 pfam03879
Cgr1 family; Members of this family are coiled-coil proteins that are involved in pre-rRNA ...
 38-104 3.25e-03

Cgr1 family; Members of this family are coiled-coil proteins that are involved in pre-rRNA processing.


Pssm-ID: 427562 [Multi-domain]  Cd Length: 107  Bit Score: 36.83  E-value: 3.25e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372912   38 KMMEQKMKEEQE---RRKKKEMEERMSLEETKEQILKLQQKLSAlqeekhqlflqlKKVlheeEKRRRKE 104
Cdd:pfam03879  46 KAKEKELKDEKEaerQRRIQAIKERREAKEEKERYEELAAKMHA------------KKV----ERLKRKE 99
Casc1_N pfam15927
Cancer susceptibility candidate 1 N-terminus; This presumed domain is functionally ...
 45-103 3.27e-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: 38.50  E-value: 3.27e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 564372912   45 KEEQERRKKKEMEERMSLEETKEQILKLQQKLSALQEEKHQLFlQLKKVLHEEEKRRRK 103
Cdd:pfam15927   4 REEEEERLRAEEEEAERLEEERREEEEEERLAAEQDRRAEELE-ELKHLLEERKEALEK 61
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 41-120 3.37e-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: 3.37e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372912  41 EQKMKEEQERRKKKEMEERMSLEETKEQILKLQQKLSALQEEKHQLFLQLKKVLHEEEKRRRKEQSDLTTLTSAAYQQSL 120
Cdd:COG1196  416 LERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLL 495
PRK10263 PRK10263
DNA translocase FtsK; Provisional
 168-337 3.53e-03

DNA translocase FtsK; Provisional


Pssm-ID: 236669 [Multi-domain]  Cd Length: 1355  Bit Score: 39.68  E-value: 3.53e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372912  168 AAAFAGTPEHGQFQGSPGGAYGTAQPPPHYGPTQPAY--SPSQQLRAPSAFPAVQYLSQPQPQP-YAVHGHFQPTQTGFL 244
Cdd:PRK10263  700 ARQFAQTQQQRYSGEQPAGANPFSLDDFEFSPMKALLddGPHEPLFTPIVEPVQQPQQPVAPQQqYQQPQQPVAPQPQYQ 779

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372912  245 QPGSALSLQKQMEHANQQTSFSDSSSL--RPMHPQALHPAPGLLASPQLPVQiqaagKALPPPANRALDSLssntarTHD 322
Cdd:PRK10263  780 QPQQPVAPQPQYQQPQQPVAPQPQYQQpqQPVAPQPQYQQPQQPVAPQPQYQ-----QPQQPVAPQPQDTL------LHP 848

                         170
                  ....*....|....*
gi 564372912  323 SITSNHQITPTHPPS 337
Cdd:PRK10263  849 LLMRNGDSRPLHKPT 863
Troponin pfam00992
Troponin; Troponin (Tn) contains three subunits, Ca2+ binding (TnC), inhibitory (TnI), and ...
 38-109 3.68e-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: 37.16  E-value: 3.68e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372912   38 KMMEQKMKEE--QERRKKKEmEERMSLEETKEQiLKL----QQKLSALQEEKHQLFLQL---KKVLHEEEKRRRKEQSDL 108
Cdd:pfam00992   6 SLLLQKAAEEleFEQEKKEE-EKLRYLAERIPP-LRLrglsAEQLQELCEELHERIDKLeeeRYDIEEKVAKKDKEINDL 83


                  .
gi 564372912  109 T 109
Cdd:pfam00992  84 K 84
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
 40-104 4.34e-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: 38.75  E-value: 4.34e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 564372912   40 MEQKMKEEQERRKKKEMEERMSLEETKEQILKLQQKLSALQEekHQLFLQLKKVLHEEEKRRRKE 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 4.49e-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: 38.10  E-value: 4.49e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 564372912   43 KMKEEQERRKKKEMEERmsLEETKEQilKLQQKLSALQEEKHQLFLQLKK------VLHEEEKRRRKE 104
Cdd:pfam09756  10 KLELKEAKRQQREAEEE--EREEREK--LEEKREEEYKEREEREEEAEKEkeeeerKQEEEQERKEQE 73
Atrophin-1 pfam03154
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
 171-368 6.17e-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: 38.98  E-value: 6.17e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372912  171 FAGTPEHGQFQGSPG---GAYGTAQPPPHYGPTQPAYSPSQQLRAPSAFPAvqylsqPQPQPyavhgHFQPTQTGFLQPG 247
Cdd:pfam03154 298 FPLTPQSSQSQVPPGpspAAPGQSQQRIHTPPSQSQLQSQQPPREQPLPPA------PLSMP-----HIKPPPTTPIPQL 366

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372912  248 SALSLQKQMEHANQQTSFSDSSSLRP------------MHPQALHPAPGLLASPQLPVQIQAA-------GKALPPPANR 308
Cdd:pfam03154 367 PNPQSHKHPPHLSGPSPFQMNSNLPPppalkplsslstHHPPSAHPPPLQLMPQSQQLPPPPAqppvltqSQSLPPPAAS 446

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 564372912  309 ALDSLSSNTARTHdSITSNHQITPTHPPSLR--VGSYVSQTNKMYKIYLPSCQSTVYLLPKP 368
Cdd:pfam03154 447 HPPTSGLHQVPSQ-SPFPQHPFVPGGPPPITppSGPPTSTSSAMPGIQPPSSASVSSSGPVP 507
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
 37-105 6.87e-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: 6.87e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 564372912   37 DKMME---QKMKEEQERRKKKEMEERMSL-EETKEQIL-KLQQKLSALQEEKH--QLFLQLKKVLHEEEKRRRKEQ 105
Cdd:pfam13868  46 DEMMEeerERALEEEEEKEEERKEERKRYrQELEEQIEeREQKRQEEYEEKLQerEQMDEIVERIQEEDQAEAEEK 121
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
 36-105 7.18e-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: 38.36  E-value: 7.18e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372912   36 VDKMMEQKMKEEQERRKKKEMEERMSLEEtkEQILKLQQKLSALQEEKHQLFLQLKKVLHEEEKRRRKEQ 105
Cdd:pfam13868 215 QERKERQKEREEAEKKARQRQELQQAREE--QIELKERRLAEEAEREEEEFERMLRKQAEDEEIEQEEAE 282
DUF4200 pfam13863
Domain of unknown function (DUF4200); This family is found in eukaryotes. It is a coiled-coil ...
 42-89 8.69e-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: 36.01  E-value: 8.69e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 564372912   42 QKMKEEQERRKKKEMEermsLEETKEQILKLQQKLSALQEE-----KHQLFLQ 89
Cdd:pfam13863  66 KKAEEETKLKKEKEKE----IKKLTAQIEELKSEISKLEEKleeykPYEDFLE 114
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
 32-105 9.87e-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: 37.59  E-value: 9.87e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 564372912   32 EEEEVDKMMEQKMKEEQERRKKKEMEERMSLEETKEQILKLQQKLSALQEEKHQLFLQLKKVLHEE--EKRRRKEQ 105
Cdd:pfam13868 149 EEREEDERILEYLKEKAEREEEREAEREEIEEEKEREIARLRAQQEKAQDEKAERDELRAKLYQEEqeRKERQKER 224
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH