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Conserved domains on  [gi|217416374|ref|NP_659475|]
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dynein regulatory complex protein 1 [Homo sapiens]

Protein Classification

BAR and NYD-SP28_assoc domain-containing protein( domain architecture ID 13864807)

BAR and NYD-SP28_assoc domain-containing protein

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
NYD-SP28 pfam14772
Sperm tail; NYD-SP28 is expressed in a development-dependent manner, localized in ...
99-200 5.30e-27

Sperm tail; NYD-SP28 is expressed in a development-dependent manner, localized in spermatogenic cell cytoplams and human spermatozoa tail. It is post-translationally modified during sperm capacitation and ultimately contributes to the success of fertilization.


:

Pssm-ID: 464307 [Multi-domain]  Cd Length: 102  Bit Score: 105.37  E-value: 5.30e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217416374   99 VAIDIREIHRRVEEEEIKRQRIEKLENEVKTSQDKFDEITSKWEEGKQKRIPQELWEMLNTQQLHCAGLLEDKNKLISEL 178
Cdd:pfam14772   1 VAADAEEEQRRRKEEELRRFRKEKLEEEAKSSQEKFEKINQRWRSILRKNKPQELREELEEQKQACERIIDRKDKLIKEL 80
                          90       100
                  ....*....|....*....|..
gi 217416374  179 QQELKTKDDQYVKDLKKQSDDI 200
Cdd:pfam14772  81 QQELKEADEQYVKALRKQAEDI 102
NYD-SP28_assoc pfam14775
Sperm tail C-terminal domain; NYD-SP28 is expressed in a development-dependent manner, ...
660-719 1.01e-21

Sperm tail C-terminal domain; NYD-SP28 is expressed in a development-dependent manner, localized in spermatogenic cell cytoplams and human spermatozoa tail. It is post-translationally modified during sperm capacitation and ultimately contributes to the success of fertilization. This short region is found at the very C-terminus of family members of family NYD-SP28, pfam14772.


:

Pssm-ID: 464309  Cd Length: 60  Bit Score: 88.80  E-value: 1.01e-21
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 217416374  660 EYWQALTTVIPSSKQNLWDALYTALEKYHLVLTQRAKLLLENSSLEQQNTELQALLQQYL 719
Cdd:pfam14775   1 EYWERLANVIPEEKLRLWDALEKALEKYHEVLTERSKLIEETESLRQQNTELRNLLKQYL 60
SMC_N super family cl47134
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...
111-388 1.37e-05

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.


The actual alignment was detected with superfamily member TIGR02169:

Pssm-ID: 481474 [Multi-domain]  Cd Length: 1164  Bit Score: 48.91  E-value: 1.37e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217416374   111 EEEEIKRQRIEKLENEVKTSQDKFDEITSKWEEGKQK--------RIPQELWEMLNTQQLHCAGLLEDKNKLISELQQEL 182
Cdd:TIGR02169  674 AELQRLRERLEGLKRELSSLQSELRRIENRLDELSQElsdasrkiGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEI 753
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217416374   183 kTKDDQYVKDLKKQSDDICLLLERMEEQVKNV--------MKTFREELYNIEKafEVERQELLASNKKKWEQALQahnaK 254
Cdd:TIGR02169  754 -ENVKSELKELEARIEELEEDLHKLEEALNDLearlshsrIPEIQAELSKLEE--EVSRIEARLREIEQKLNRLT----L 826
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217416374   255 ELEYLNNRMKKVEDYEKQLNRQRIWDCEEYNMIKIKLEQDVQILEQ------QLQQRKAIYQLNQEKLEYNLQVLKKRDE 328
Cdd:TIGR02169  827 EKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEEleaalrDLESRLGDLKKERDELEAQLRELERKIE 906
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 217416374   329 ESTVIKSQQKRKINRLHDILNNLR---SKYAKQIKQFQEEnQSLTSDYKRLVMQFKELQKAMR 388
Cdd:TIGR02169  907 ELEAQIEKKRKRLSELKAKLEALEeelSEIEDPKGEDEEI-PEEELSLEDVQAELQRVEEEIR 968
 
Name Accession Description Interval E-value
NYD-SP28 pfam14772
Sperm tail; NYD-SP28 is expressed in a development-dependent manner, localized in ...
99-200 5.30e-27

Sperm tail; NYD-SP28 is expressed in a development-dependent manner, localized in spermatogenic cell cytoplams and human spermatozoa tail. It is post-translationally modified during sperm capacitation and ultimately contributes to the success of fertilization.


Pssm-ID: 464307 [Multi-domain]  Cd Length: 102  Bit Score: 105.37  E-value: 5.30e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217416374   99 VAIDIREIHRRVEEEEIKRQRIEKLENEVKTSQDKFDEITSKWEEGKQKRIPQELWEMLNTQQLHCAGLLEDKNKLISEL 178
Cdd:pfam14772   1 VAADAEEEQRRRKEEELRRFRKEKLEEEAKSSQEKFEKINQRWRSILRKNKPQELREELEEQKQACERIIDRKDKLIKEL 80
                          90       100
                  ....*....|....*....|..
gi 217416374  179 QQELKTKDDQYVKDLKKQSDDI 200
Cdd:pfam14772  81 QQELKEADEQYVKALRKQAEDI 102
NYD-SP28_assoc pfam14775
Sperm tail C-terminal domain; NYD-SP28 is expressed in a development-dependent manner, ...
660-719 1.01e-21

Sperm tail C-terminal domain; NYD-SP28 is expressed in a development-dependent manner, localized in spermatogenic cell cytoplams and human spermatozoa tail. It is post-translationally modified during sperm capacitation and ultimately contributes to the success of fertilization. This short region is found at the very C-terminus of family members of family NYD-SP28, pfam14772.


Pssm-ID: 464309  Cd Length: 60  Bit Score: 88.80  E-value: 1.01e-21
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 217416374  660 EYWQALTTVIPSSKQNLWDALYTALEKYHLVLTQRAKLLLENSSLEQQNTELQALLQQYL 719
Cdd:pfam14775   1 EYWERLANVIPEEKLRLWDALEKALEKYHEVLTERSKLIEETESLRQQNTELRNLLKQYL 60
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
111-388 1.37e-05

chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 48.91  E-value: 1.37e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217416374   111 EEEEIKRQRIEKLENEVKTSQDKFDEITSKWEEGKQK--------RIPQELWEMLNTQQLHCAGLLEDKNKLISELQQEL 182
Cdd:TIGR02169  674 AELQRLRERLEGLKRELSSLQSELRRIENRLDELSQElsdasrkiGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEI 753
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217416374   183 kTKDDQYVKDLKKQSDDICLLLERMEEQVKNV--------MKTFREELYNIEKafEVERQELLASNKKKWEQALQahnaK 254
Cdd:TIGR02169  754 -ENVKSELKELEARIEELEEDLHKLEEALNDLearlshsrIPEIQAELSKLEE--EVSRIEARLREIEQKLNRLT----L 826
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217416374   255 ELEYLNNRMKKVEDYEKQLNRQRIWDCEEYNMIKIKLEQDVQILEQ------QLQQRKAIYQLNQEKLEYNLQVLKKRDE 328
Cdd:TIGR02169  827 EKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEEleaalrDLESRLGDLKKERDELEAQLRELERKIE 906
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 217416374   329 ESTVIKSQQKRKINRLHDILNNLR---SKYAKQIKQFQEEnQSLTSDYKRLVMQFKELQKAMR 388
Cdd:TIGR02169  907 ELEAQIEKKRKRLSELKAKLEALEeelSEIEDPKGEDEEI-PEEELSLEDVQAELQRVEEEIR 968
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
33-375 5.06e-05

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


Pssm-ID: 375164 [Multi-domain]  Cd Length: 722  Bit Score: 46.66  E-value: 5.06e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217416374   33 QERIQARRLRIAARLEARRReaLGEYLDGKKESEEDQSKSYKQKEESRLKLAKLLlcgtelvTNIQVAIDIREIHR-RVE 111
Cdd:pfam17380 298 QERLRQEKEEKAREVERRRK--LEEAEKARQAEMDRQAAIYAEQERMAMEREREL-------ERIRQEERKRELERiRQE 368
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217416374  112 EEEIKRQRIEKLENEVKTSQDKFDEITSKWEEGKQKRIPQElwemlntqqlhcaglledknklisELQQELKTKDDQYVK 191
Cdd:pfam17380 369 EIAMEISRMRELERLQMERQQKNERVRQELEAARKVKILEE------------------------ERQRKIQQQKVEMEQ 424
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217416374  192 DLKKQSDDICLLLERMEEQVKNVMKTFREELYNIEKAFEVERQELLASNKKKWEQALQAHNAKELEYLNnrmKKVEDYEK 271
Cdd:pfam17380 425 IRAEQEEARQREVRRLEEERAREMERVRLEEQERQQQVERLRQQEEERKRKKLELEKEKRDRKRAEEQR---RKILEKEL 501
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217416374  272 QLNRQRIwdceeynmikIKLEQDVQILEQQLQQR-KAIYQLNQEKleynlqvlKKRDEESTVIKSQQKRKINRLHDILNN 350
Cdd:pfam17380 502 EERKQAM----------IEEERKRKLLEKEMEERqKAIYEEERRR--------EAEEERRKQQEMEERRRIQEQMRKATE 563
                         330       340
                  ....*....|....*....|....*
gi 217416374  351 LRSKYAKQIKQFQEENQSLTSDYKR 375
Cdd:pfam17380 564 ERSRLEAMEREREMMRQIVESEKAR 588
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
103-352 1.05e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 42.36  E-value: 1.05e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217416374 103 IREIHRRVEEEEIKRQRIEKLENEVKTSQDKFDEItskweEGKQKRIPQELWEMlntqqlhcaGLLEDKNKLISELQQEL 182
Cdd:PRK03918 206 LREINEISSELPELREELEKLEKEVKELEELKEEI-----EELEKELESLEGSK---------RKLEEKIRELEERIEEL 271
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217416374 183 KTKddqyVKDLKKQSDDICLLLERMEEQVK--NVMKTFREELYNIEKAFEVERQELLASNKKkweqalqahnAKELEYLN 260
Cdd:PRK03918 272 KKE----IEELEEKVKELKELKEKAEEYIKlsEFYEEYLDELREIEKRLSRLEEEINGIEER----------IKELEEKE 337
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217416374 261 NRMKKVEDYEKQLNRQRIW---DCEEYNMIKIKLEQdvqilEQQLQQRKAIYQLnqEKLEYNLQVLKKRDEESTVIKSQQ 337
Cdd:PRK03918 338 ERLEELKKKLKELEKRLEEleeRHELYEEAKAKKEE-----LERLKKRLTGLTP--EKLEKELEELEKAKEEIEEEISKI 410
                        250
                 ....*....|....*
gi 217416374 338 KRKINRLHDILNNLR 352
Cdd:PRK03918 411 TARIGELKKEIKELK 425
 
Name Accession Description Interval E-value
NYD-SP28 pfam14772
Sperm tail; NYD-SP28 is expressed in a development-dependent manner, localized in ...
99-200 5.30e-27

Sperm tail; NYD-SP28 is expressed in a development-dependent manner, localized in spermatogenic cell cytoplams and human spermatozoa tail. It is post-translationally modified during sperm capacitation and ultimately contributes to the success of fertilization.


Pssm-ID: 464307 [Multi-domain]  Cd Length: 102  Bit Score: 105.37  E-value: 5.30e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217416374   99 VAIDIREIHRRVEEEEIKRQRIEKLENEVKTSQDKFDEITSKWEEGKQKRIPQELWEMLNTQQLHCAGLLEDKNKLISEL 178
Cdd:pfam14772   1 VAADAEEEQRRRKEEELRRFRKEKLEEEAKSSQEKFEKINQRWRSILRKNKPQELREELEEQKQACERIIDRKDKLIKEL 80
                          90       100
                  ....*....|....*....|..
gi 217416374  179 QQELKTKDDQYVKDLKKQSDDI 200
Cdd:pfam14772  81 QQELKEADEQYVKALRKQAEDI 102
NYD-SP28_assoc pfam14775
Sperm tail C-terminal domain; NYD-SP28 is expressed in a development-dependent manner, ...
660-719 1.01e-21

Sperm tail C-terminal domain; NYD-SP28 is expressed in a development-dependent manner, localized in spermatogenic cell cytoplams and human spermatozoa tail. It is post-translationally modified during sperm capacitation and ultimately contributes to the success of fertilization. This short region is found at the very C-terminus of family members of family NYD-SP28, pfam14772.


Pssm-ID: 464309  Cd Length: 60  Bit Score: 88.80  E-value: 1.01e-21
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 217416374  660 EYWQALTTVIPSSKQNLWDALYTALEKYHLVLTQRAKLLLENSSLEQQNTELQALLQQYL 719
Cdd:pfam14775   1 EYWERLANVIPEEKLRLWDALEKALEKYHEVLTERSKLIEETESLRQQNTELRNLLKQYL 60
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
111-388 1.37e-05

chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 48.91  E-value: 1.37e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217416374   111 EEEEIKRQRIEKLENEVKTSQDKFDEITSKWEEGKQK--------RIPQELWEMLNTQQLHCAGLLEDKNKLISELQQEL 182
Cdd:TIGR02169  674 AELQRLRERLEGLKRELSSLQSELRRIENRLDELSQElsdasrkiGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEI 753
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217416374   183 kTKDDQYVKDLKKQSDDICLLLERMEEQVKNV--------MKTFREELYNIEKafEVERQELLASNKKKWEQALQahnaK 254
Cdd:TIGR02169  754 -ENVKSELKELEARIEELEEDLHKLEEALNDLearlshsrIPEIQAELSKLEE--EVSRIEARLREIEQKLNRLT----L 826
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217416374   255 ELEYLNNRMKKVEDYEKQLNRQRIWDCEEYNMIKIKLEQDVQILEQ------QLQQRKAIYQLNQEKLEYNLQVLKKRDE 328
Cdd:TIGR02169  827 EKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEEleaalrDLESRLGDLKKERDELEAQLRELERKIE 906
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 217416374   329 ESTVIKSQQKRKINRLHDILNNLR---SKYAKQIKQFQEEnQSLTSDYKRLVMQFKELQKAMR 388
Cdd:TIGR02169  907 ELEAQIEKKRKRLSELKAKLEALEeelSEIEDPKGEDEEI-PEEELSLEDVQAELQRVEEEIR 968
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
33-375 5.06e-05

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


Pssm-ID: 375164 [Multi-domain]  Cd Length: 722  Bit Score: 46.66  E-value: 5.06e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217416374   33 QERIQARRLRIAARLEARRReaLGEYLDGKKESEEDQSKSYKQKEESRLKLAKLLlcgtelvTNIQVAIDIREIHR-RVE 111
Cdd:pfam17380 298 QERLRQEKEEKAREVERRRK--LEEAEKARQAEMDRQAAIYAEQERMAMEREREL-------ERIRQEERKRELERiRQE 368
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217416374  112 EEEIKRQRIEKLENEVKTSQDKFDEITSKWEEGKQKRIPQElwemlntqqlhcaglledknklisELQQELKTKDDQYVK 191
Cdd:pfam17380 369 EIAMEISRMRELERLQMERQQKNERVRQELEAARKVKILEE------------------------ERQRKIQQQKVEMEQ 424
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217416374  192 DLKKQSDDICLLLERMEEQVKNVMKTFREELYNIEKAFEVERQELLASNKKKWEQALQAHNAKELEYLNnrmKKVEDYEK 271
Cdd:pfam17380 425 IRAEQEEARQREVRRLEEERAREMERVRLEEQERQQQVERLRQQEEERKRKKLELEKEKRDRKRAEEQR---RKILEKEL 501
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217416374  272 QLNRQRIwdceeynmikIKLEQDVQILEQQLQQR-KAIYQLNQEKleynlqvlKKRDEESTVIKSQQKRKINRLHDILNN 350
Cdd:pfam17380 502 EERKQAM----------IEEERKRKLLEKEMEERqKAIYEEERRR--------EAEEERRKQQEMEERRRIQEQMRKATE 563
                         330       340
                  ....*....|....*....|....*
gi 217416374  351 LRSKYAKQIKQFQEENQSLTSDYKR 375
Cdd:pfam17380 564 ERSRLEAMEREREMMRQIVESEKAR 588
SMC_N pfam02463
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...
29-386 4.35e-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: 43.81  E-value: 4.35e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217416374    29 SDNSQERIQARRLRIAARLEARRRE--ALGEYLDGKKESEEDQSKSYKQKEESRLKLAKLLLCGTELVTNIQVAIDIREI 106
Cdd:pfam02463  626 EGILKDTELTKLKESAKAKESGLRKgvSLEEGLAEKSEVKASLSELTKELLEIQELQEKAESELAKEEILRRQLEIKKKE 705
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217416374   107 HRRVEEEEIKRQRIEKLENEVKTSQDKFDEITSKWEEGKQKRIPQELWEMLNTQqlhcaglLEDKNKLISELQQELKTKD 186
Cdd:pfam02463  706 QREKEELKKLKLEAEELLADRVQEAQDKINEELKLLKQKIDEEEEEEEKSRLKK-------EEKEEEKSELSLKEKELAE 778
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217416374   187 DQYVKDLKKQSDDICLLLERMEEQVKNVMKTFREELYNIEKAFEVERQELLASNKKKWEQALQAHNAKELEYLN------ 260
Cdd:pfam02463  779 EREKTEKLKVEEEKEEKLKAQEEELRALEEELKEEAELLEEEQLLIEQEEKIKEEELEELALELKEEQKLEKLAeeeler 858
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217416374   261 ---NRMKKVEDYEKQLNRQRIWDCEEYNMIKIKLEQDVQILEQQLQQRKAIYQLNQEKLEYNLQVLKKRDEESTVIKSQQ 337
Cdd:pfam02463  859 leeEITKEELLQELLLKEEELEEQKLKDELESKEEKEKEEKKELEEESQKLNLLEEKENEIEERIKEEAEILLKYEEEPE 938
                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|.
gi 217416374   338 KRKINRLHDI--LNNLRSKYAKQIKQFQEENQSLTSDYKRLVMQFKELQKA 386
Cdd:pfam02463  939 ELLLEEADEKekEENNKEEEEERNKRLLLAKEELGKVNLMAIEEFEEKEER 989
SMC_N pfam02463
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...
34-353 4.69e-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: 43.81  E-value: 4.69e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217416374    34 ERIQARRLRIAARLEARRREALGEYLDGKKESEEDQSKSYKQKEESRLKLAKLL-LCGTELVTNIQVAIDIREIHRRVEE 112
Cdd:pfam02463  179 IEETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEYLLYLDYLkLNEERIDLLQELLRDEQEEIESSKQ 258
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217416374   113 EEIKRQRIEKLENEVKTSQDKFDEITSKWEEGKQKRIPQELWEMLNTQQLHCAGLLEDKNKLISELQQELKTKDDQYVKD 192
Cdd:pfam02463  259 EIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDEEKLKESEKEKKKAEKELKKEKEEIE 338
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217416374   193 ----LKKQSDDICLLLERMEEQVKNVMKTFREELYNIEKAFEVERQELLASNKKKWEQALQAHNAKELEYLNNRMKKVED 268
Cdd:pfam02463  339 elekELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEEELELKSEEEKEAQLLLELARQLE 418
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217416374   269 YEKQLNRQriwdceEYNMIKIKLEQDVQILEQQLQQRKAIYQLNQEKLEYNLQVLKK--RDEESTVIKSQQKRKINRLHD 346
Cdd:pfam02463  419 DLLKEEKK------EELEILEEEEESIELKQGKLTEEKEELEKQELKLLKDELELKKseDLLKETQLVKLQEQLELLLSR 492

                   ....*..
gi 217416374   347 ILNNLRS 353
Cdd:pfam02463  493 QKLEERS 499
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
35-379 6.25e-04

chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 43.51  E-value: 6.25e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217416374    35 RIQARRLRIAARLEARRREALGEYLDGKKESEEDqsksykQKEESRLKLAKLllcgTELVTNIQvaidiREIHRRVEEEE 114
Cdd:TIGR02168  206 ERQAEKAERYKELKAELRELELALLVLRLEELRE------ELEELQEELKEA----EEELEELT-----AELQELEEKLE 270
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217416374   115 IKRQRIEKLENEVKTSQDKFDEITSkweegKQKRIPQELwEMLNTQQLHcaglLEDKNKLISELQQELKTKDDQYVKDLK 194
Cdd:TIGR02168  271 ELRLEVSELEEEIEELQKELYALAN-----EISRLEQQK-QILRERLAN----LERQLEELEAQLEELESKLDELAEELA 340
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217416374   195 KQSDDICLLLERMEEQvKNVMKTFREELYNIEKAFEVERQELLASNKKKWEQALQ-AHNAKELEYLNNRMKKVEDyekql 273
Cdd:TIGR02168  341 ELEEKLEELKEELESL-EAELEELEAELEELESRLEELEEQLETLRSKVAQLELQiASLNNEIERLEARLERLED----- 414
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217416374   274 nRQRIWDCEEYNMIKIKLEQDVQILEQQLQQRKAIYQLNQEKLEYNLQVLKKRDEESTVIKSQQKRKINRLHDILNNLRS 353
Cdd:TIGR02168  415 -RRERLQQEIEELLKKLEEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDS 493
                          330       340
                   ....*....|....*....|....*.
gi 217416374   354 kyakqIKQFQEENQSLTSDYKRLVMQ 379
Cdd:TIGR02168  494 -----LERLQENLEGFSEGVKALLKN 514
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
103-352 1.05e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 42.36  E-value: 1.05e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217416374 103 IREIHRRVEEEEIKRQRIEKLENEVKTSQDKFDEItskweEGKQKRIPQELWEMlntqqlhcaGLLEDKNKLISELQQEL 182
Cdd:PRK03918 206 LREINEISSELPELREELEKLEKEVKELEELKEEI-----EELEKELESLEGSK---------RKLEEKIRELEERIEEL 271
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217416374 183 KTKddqyVKDLKKQSDDICLLLERMEEQVK--NVMKTFREELYNIEKAFEVERQELLASNKKkweqalqahnAKELEYLN 260
Cdd:PRK03918 272 KKE----IEELEEKVKELKELKEKAEEYIKlsEFYEEYLDELREIEKRLSRLEEEINGIEER----------IKELEEKE 337
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217416374 261 NRMKKVEDYEKQLNRQRIW---DCEEYNMIKIKLEQdvqilEQQLQQRKAIYQLnqEKLEYNLQVLKKRDEESTVIKSQQ 337
Cdd:PRK03918 338 ERLEELKKKLKELEKRLEEleeRHELYEEAKAKKEE-----LERLKKRLTGLTP--EKLEKELEELEKAKEEIEEEISKI 410
                        250
                 ....*....|....*
gi 217416374 338 KRKINRLHDILNNLR 352
Cdd:PRK03918 411 TARIGELKKEIKELK 425
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
102-414 1.20e-03

chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 42.36  E-value: 1.20e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217416374   102 DIREIHRRVEE----EEIKRQRIEKLENEvKTSQDKFDEITSKWEEGKQKRIPQElWEMLNTQqlhcaglLEDKNKLISE 177
Cdd:TIGR02169  178 ELEEVEENIERldliIDEKRQQLERLRRE-REKAERYQALLKEKREYEGYELLKE-KEALERQ-------KEAIERQLAS 248
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217416374   178 LQQELkTKDDQYVKDLKKQSDDICLLLERMEEQVK----NVMKTFREELYNIEKafEVERQELLASNKKKWEQALQAHNA 253
Cdd:TIGR02169  249 LEEEL-EKLTEEISELEKRLEEIEQLLEELNKKIKdlgeEEQLRVKEKIGELEA--EIASLERSIAEKERELEDAEERLA 325
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217416374   254 KELEYLNNRMKKVEDYEKQLnrqriwdcEEYNMIKIKLEQDVQILEQQLqqrkaiyqlnqEKLEYNLQVLKKRDEESTVI 333
Cdd:TIGR02169  326 KLEAEIDKLLAEIEELEREI--------EEERKRRDKLTEEYAELKEEL-----------EDLRAELEEVDKEFAETRDE 386
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217416374   334 KSQQKRKINRLHDILNNLRskyaKQIKQFQEENQSLTSDYKRLVMQFKELQKAMRHFALIDDEKFWEIWlMNEEEAKDLI 413
Cdd:TIGR02169  387 LKDYREKLEKLKREINELK----RELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIK-KQEWKLEQLA 461

                   .
gi 217416374   414 A 414
Cdd:TIGR02169  462 A 462
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
31-375 3.71e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 40.82  E-value: 3.71e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217416374  31 NSQERIQARRLRIAARLEARRREaLGEYLDGKKESEED------QSKSYKQKEESRLKLAKLLLCGTELVTNIQVAI--- 101
Cdd:PRK03918 241 EELEKELESLEGSKRKLEEKIRE-LEERIEELKKEIEEleekvkELKELKEKAEEYIKLSEFYEEYLDELREIEKRLsrl 319
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217416374 102 --DIREIHRRVEEEEIKRQRIEKLENEVKTSQDKFDEITSK---WEEGKQK-------------RIPQELWEMLNTQQLH 163
Cdd:PRK03918 320 eeEINGIEERIKELEEKEERLEELKKKLKELEKRLEELEERhelYEEAKAKkeelerlkkrltgLTPEKLEKELEELEKA 399
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217416374 164 CAGLLEDKNKL---ISELQQELKTKDDQyVKDLKKqSDDICLLLERM--EEQVKNVMKTFREELYNIEKAFE--VERQEL 236
Cdd:PRK03918 400 KEEIEEEISKItarIGELKKEIKELKKA-IEELKK-AKGKCPVCGREltEEHRKELLEEYTAELKRIEKELKeiEEKERK 477
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217416374 237 LASNKKKWEQALQAHN--------AKELEYLNNRMKK--VEDYEKqlnrqriwDCEEYNMIK---IKLEQDVQILEQQLQ 303
Cdd:PRK03918 478 LRKELRELEKVLKKESeliklkelAEQLKELEEKLKKynLEELEK--------KAEEYEKLKeklIKLKGEIKSLKKELE 549
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 217416374 304 QrkaiyqlnqekleynLQVLKKRDEEstvIKSQQKRKINRLHDILNNLRSKYAKQIKQFQEENQSLTSDYKR 375
Cdd:PRK03918 550 K---------------LEELKKKLAE---LEKKLDELEEELAELLKELEELGFESVEELEERLKELEPFYNE 603
PRK12704 PRK12704
phosphodiesterase; Provisional
204-365 4.05e-03

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 40.53  E-value: 4.05e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217416374 204 LERMEEQVKNVMKTFREELYNIEKAFEVERQELLASNKKKWEQALQAHNAKeleyLNNRMKKVEDYEKQLNRQriwdcEE 283
Cdd:PRK12704  33 IKEAEEEAKRILEEAKKEAEAIKKEALLEAKEEIHKLRNEFEKELRERRNE----LQKLEKRLLQKEENLDRK-----LE 103
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217416374 284 YNmikIKLEQDVQILEQQLQQRKAIYQLNQEKLEYNLQVLKKRDEESTVIKSQQKRKInrlhdILNNLRSKY----AKQI 359
Cdd:PRK12704 104 LL---EKREEELEKKEKELEQKQQELEKKEEELEELIEEQLQELERISGLTAEEAKEI-----LLEKVEEEArheaAVLI 175

                 ....*.
gi 217416374 360 KQFQEE 365
Cdd:PRK12704 176 KEIEEE 181
SMC_N pfam02463
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...
70-397 8.38e-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: 39.57  E-value: 8.38e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217416374    70 SKSYKQKEESRLKLAKlllcgtELVTNIQVAIDIREIHRRVEEEEIKRQRIEKLENEVKTSQDKFDEITSKWEEGKQKRI 149
Cdd:pfam02463  165 SRLKRKKKEALKKLIE------ETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEYLLYLDYLKLNEER 238
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217416374   150 PQELWEMLNTQQLHCAGLLEDKNKLISELQQELKtKDDQYVKDLKKQSDDICLLLERMEEQVKNVMKTFREELYNIEKAF 229
Cdd:pfam02463  239 IDLLQELLRDEQEEIESSKQEIEKEEEKLAQVLK-ENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDEEKLK 317
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217416374   230 EVERQELLASNKKKWEQALQAHNAKELEYLNNRMKKVEDYEKQLNRQRiwdcEEYNMIKIKLEQDVQILEQQLQQRKAIY 309
Cdd:pfam02463  318 ESEKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQ----EKLEQLEEELLAKKKLESERLSSAAKLK 393
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217416374   310 QLNQEKLEYNLQVLKKRDEESTVIKSQQKRKINRLHDILNNLRSKYAKQIKQFQEENQSLTSDYKRLVMQFKELQKAMRH 389
Cdd:pfam02463  394 EEELELKSEEEKEAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKLLKDELELKKSEDL 473

                   ....*...
gi 217416374   390 FALIDDEK 397
Cdd:pfam02463  474 LKETQLVK 481
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
100-389 9.46e-03

Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.


Pssm-ID: 464943 [Multi-domain]  Cd Length: 1112  Bit Score: 39.33  E-value: 9.46e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217416374   100 AIDIREIHRRVEEEEIKRQRIEKLENEVKT------------------SQDKFDEITSKWEEGKQkrIPQELWEMLNTQQ 161
Cdd:pfam15921  411 SITIDHLRRELDDRNMEVQRLEALLKAMKSecqgqmerqmaaiqgkneSLEKVSSLTAQLESTKE--MLRKVVEELTAKK 488
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217416374   162 LhcagLLEDKNKLISELQQELKTKDdqyvKDLKKQSDDICLLLERMEEQVKNV--MKTFREELYNIEKAFEVERQELLAS 239
Cdd:pfam15921  489 M----TLESSERTVSDLTASLQEKE----RAIEATNAEITKLRSRVDLKLQELqhLKNEGDHLRNVQTECEALKLQMAEK 560
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 217416374   240 NKKKWEQALQAHNAKELEYLNNRMK---KVE--DYEKQLNRQRIwDCEEYNMIKIKLEQDVQILEQQLQ----QRKAIYQ 310
Cdd:pfam15921  561 DKVIEILRQQIENMTQLVGQHGRTAgamQVEkaQLEKEINDRRL-ELQEFKILKDKKDAKIRELEARVSdlelEKVKLVN 639
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 217416374   311 LNQEKLEYNLQVLKKRDEESTVIKSQQKRkinrlhdiLNNLRSKYAKQIKQFQEENQSLTSDYKRLVMQFKELQKAMRH 389
Cdd:pfam15921  640 AGSERLRAVKDIKQERDQLLNEVKTSRNE--------LNSLSEDYEVLKRNFRNKSEEMETTTNKLKMQLKSAQSELEQ 710
 
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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