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Conserved domains on  [gi|2217287339|ref|XP_047284215|]
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dynein regulatory complex protein 10 isoform X1 [Homo sapiens]

Protein Classification

coiled-coil domain-containing protein( domain architecture ID 1000037)

coiled-coil domain-containing protein contains a region with alpha-helical coiled-coil sequence signatures that is being annotated by a variety of protein family models, not necessarily indicating family membership

Graphical summary

 Zoom to residue level

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List of domain hits

Name Accession Description Interval E-value
46 super family cl33686
endonuclease subunit; Provisional
95-305 3.76e-03

endonuclease subunit; Provisional


The actual alignment was detected with superfamily member PHA02562:

Pssm-ID: 222878 [Multi-domain]  Cd Length: 562  Bit Score: 39.61  E-value: 3.76e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217287339  95 EDL--CQVLLENVRCLKEKERQLQEQkeaeeegwlrdrLLSIELQKSSLSplmQQIKDSTKNVLRLLLSNPQA-ARLLQM 171
Cdd:PHA02562  157 EDLldISVLSEMDKLNKDKIRELNQQ------------IQTLDMKIDHIQ---QQIKTYNKNIEEQRKKNGENiARKQNK 221
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217287339 172 QTQGRsAEAQNFIDSLIELRGFLFEklLTSPMEARDKA-----QFLQDISRQNSN-----------------NQQIIDTL 229
Cdd:PHA02562  222 YDELV-EEAKTIKAEIEELTDELLN--LVMDIEDPSAAlnklnTAAAKIKSKIEQfqkvikmyekggvcptcTQQISEGP 298
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2217287339 230 EK--ELAERMKNRNAEVEKENFVIQELKNHLHQVLKFSENSL-VRTKQEAEKQqkaDFRASQARVAKIQQEILQLQSQF 305
Cdd:PHA02562  299 DRitKIKDKLKELQHSLEKLDTAIDELEEIMDEFNEQSKKLLeLKNKISTNKQ---SLITLVDKAKKVKAAIEELQAEF 374
 
Name Accession Description Interval E-value
46 PHA02562
endonuclease subunit; Provisional
95-305 3.76e-03

endonuclease subunit; Provisional


Pssm-ID: 222878 [Multi-domain]  Cd Length: 562  Bit Score: 39.61  E-value: 3.76e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217287339  95 EDL--CQVLLENVRCLKEKERQLQEQkeaeeegwlrdrLLSIELQKSSLSplmQQIKDSTKNVLRLLLSNPQA-ARLLQM 171
Cdd:PHA02562  157 EDLldISVLSEMDKLNKDKIRELNQQ------------IQTLDMKIDHIQ---QQIKTYNKNIEEQRKKNGENiARKQNK 221
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217287339 172 QTQGRsAEAQNFIDSLIELRGFLFEklLTSPMEARDKA-----QFLQDISRQNSN-----------------NQQIIDTL 229
Cdd:PHA02562  222 YDELV-EEAKTIKAEIEELTDELLN--LVMDIEDPSAAlnklnTAAAKIKSKIEQfqkvikmyekggvcptcTQQISEGP 298
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2217287339 230 EK--ELAERMKNRNAEVEKENFVIQELKNHLHQVLKFSENSL-VRTKQEAEKQqkaDFRASQARVAKIQQEILQLQSQF 305
Cdd:PHA02562  299 DRitKIKDKLKELQHSLEKLDTAIDELEEIMDEFNEQSKKLLeLKNKISTNKQ---SLITLVDKAKKVKAAIEELQAEF 374
MUTSd smart00533
DNA-binding domain of DNA mismatch repair MUTS family;
129-323 3.98e-03

DNA-binding domain of DNA mismatch repair MUTS family;


Pssm-ID: 214710 [Multi-domain]  Cd Length: 308  Bit Score: 39.20  E-value: 3.98e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217287339  129 DRLLS-IELQKSSLSPLmQQIKDSTKNVLRLllsnpqAARLLQMQTQGRSAEAQNFIDSLIELRGFLFEKLLTS-PMEAR 206
Cdd:smart00533  65 ERLLSrIERGRASPRDL-LRLYDSLEGLKEI------RQLLESLDGPLLGLLLKVILEPLLELLELLLELLNDDdPLEVN 137
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217287339  207 DKAQFLQDISRQNSNNQQIIDTLEKELAERMKNrnaevEKENFVIQELKNHLHQVLKFsensLVRTKQEAEKQQKADFRA 286
Cdd:smart00533 138 DGGLIKDGFDPELDELREKLEELEEELEELLKK-----EREELGIDSLKLGYNKVHGY----YIEVTKSEAKKVPKDFIR 208
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|
gi 2217287339  287 SQARVAKIQ---QEILQLQSQFYNLVMENREAEQALRRNI 323
Cdd:smart00533 209 RSSLKNTERfttPELKELENELLEAKEEIERLEKEILREL 248
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
108-322 7.17e-03

Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 38.59  E-value: 7.17e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217287339 108 LKEKERQLQEQKEAEEEgwLRDRLLSIELQKSSLSPLMQQIKDSTKNVLRLLLSNPQAARLLQMQTQGRSAEAQNFIDSL 187
Cdd:COG4942    36 IAELEKELAALKKEEKA--LLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELAELLRAL 113
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217287339 188 IELRGFLFEKLLTSPMEARDKAQFLQDISRQNSNNQQIIDTLEKELAErMKNRNAEVEKENFVIQELKNhlhqvlkfsEN 267
Cdd:COG4942   114 YRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAE-LAALRAELEAERAELEALLA---------EL 183
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 2217287339 268 SLVRTKQEAEKQQKADFRAS-QARVAKIQQEILQLQSQFYNL--VMENREAEQALRRN 322
Cdd:COG4942   184 EEERAALEALKAERQKLLARlEKELAELAAELAELQQEAEELeaLIARLEAEAAAAAE 241
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
85-320 8.38e-03

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: 38.88  E-value: 8.38e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217287339   85 EDVMRAVREHEDLCQVLLENVRCLKEKERQLQEQKEAEEEgwLRDRLLSIELQKSSLSPLMQQIKDSTKNVLRLLLSNPQ 164
Cdd:TIGR02168  733 KDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEE--AEEELAEAEAEIEELEAQIEQLKEELKALREALDELRA 810
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217287339  165 AARLLQmqtqGRSAEAQNFIDSLIELRGFLFEKLLTSPMEARDKAQFLQDISRQNSNNQQIIDTLEKELaERMKNRNAEV 244
Cdd:TIGR02168  811 ELTLLN----EEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESEL-EALLNERASL 885
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2217287339  245 EKENFVIQELKNHLHQVLKFSENSLVRTKQEAEKQQKAdFRASQARVAKIQQEILQLQSQF---YNLVMENREAEQALR 320
Cdd:TIGR02168  886 EEALALLRSELEELSEELRELESKRSELRRELEELREK-LAQLELRLEGLEVRIDNLQERLseeYSLTLEEAEALENKI 963
 
Name Accession Description Interval E-value
46 PHA02562
endonuclease subunit; Provisional
95-305 3.76e-03

endonuclease subunit; Provisional


Pssm-ID: 222878 [Multi-domain]  Cd Length: 562  Bit Score: 39.61  E-value: 3.76e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217287339  95 EDL--CQVLLENVRCLKEKERQLQEQkeaeeegwlrdrLLSIELQKSSLSplmQQIKDSTKNVLRLLLSNPQA-ARLLQM 171
Cdd:PHA02562  157 EDLldISVLSEMDKLNKDKIRELNQQ------------IQTLDMKIDHIQ---QQIKTYNKNIEEQRKKNGENiARKQNK 221
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217287339 172 QTQGRsAEAQNFIDSLIELRGFLFEklLTSPMEARDKA-----QFLQDISRQNSN-----------------NQQIIDTL 229
Cdd:PHA02562  222 YDELV-EEAKTIKAEIEELTDELLN--LVMDIEDPSAAlnklnTAAAKIKSKIEQfqkvikmyekggvcptcTQQISEGP 298
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2217287339 230 EK--ELAERMKNRNAEVEKENFVIQELKNHLHQVLKFSENSL-VRTKQEAEKQqkaDFRASQARVAKIQQEILQLQSQF 305
Cdd:PHA02562  299 DRitKIKDKLKELQHSLEKLDTAIDELEEIMDEFNEQSKKLLeLKNKISTNKQ---SLITLVDKAKKVKAAIEELQAEF 374
MUTSd smart00533
DNA-binding domain of DNA mismatch repair MUTS family;
129-323 3.98e-03

DNA-binding domain of DNA mismatch repair MUTS family;


Pssm-ID: 214710 [Multi-domain]  Cd Length: 308  Bit Score: 39.20  E-value: 3.98e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217287339  129 DRLLS-IELQKSSLSPLmQQIKDSTKNVLRLllsnpqAARLLQMQTQGRSAEAQNFIDSLIELRGFLFEKLLTS-PMEAR 206
Cdd:smart00533  65 ERLLSrIERGRASPRDL-LRLYDSLEGLKEI------RQLLESLDGPLLGLLLKVILEPLLELLELLLELLNDDdPLEVN 137
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217287339  207 DKAQFLQDISRQNSNNQQIIDTLEKELAERMKNrnaevEKENFVIQELKNHLHQVLKFsensLVRTKQEAEKQQKADFRA 286
Cdd:smart00533 138 DGGLIKDGFDPELDELREKLEELEEELEELLKK-----EREELGIDSLKLGYNKVHGY----YIEVTKSEAKKVPKDFIR 208
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|
gi 2217287339  287 SQARVAKIQ---QEILQLQSQFYNLVMENREAEQALRRNI 323
Cdd:smart00533 209 RSSLKNTERfttPELKELENELLEAKEEIERLEKEILREL 248
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
108-322 7.17e-03

Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 38.59  E-value: 7.17e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217287339 108 LKEKERQLQEQKEAEEEgwLRDRLLSIELQKSSLSPLMQQIKDSTKNVLRLLLSNPQAARLLQMQTQGRSAEAQNFIDSL 187
Cdd:COG4942    36 IAELEKELAALKKEEKA--LLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELAELLRAL 113
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217287339 188 IELRGFLFEKLLTSPMEARDKAQFLQDISRQNSNNQQIIDTLEKELAErMKNRNAEVEKENFVIQELKNhlhqvlkfsEN 267
Cdd:COG4942   114 YRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAE-LAALRAELEAERAELEALLA---------EL 183
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 2217287339 268 SLVRTKQEAEKQQKADFRAS-QARVAKIQQEILQLQSQFYNL--VMENREAEQALRRN 322
Cdd:COG4942   184 EEERAALEALKAERQKLLARlEKELAELAAELAELQQEAEELeaLIARLEAEAAAAAE 241
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
85-320 8.38e-03

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: 38.88  E-value: 8.38e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217287339   85 EDVMRAVREHEDLCQVLLENVRCLKEKERQLQEQKEAEEEgwLRDRLLSIELQKSSLSPLMQQIKDSTKNVLRLLLSNPQ 164
Cdd:TIGR02168  733 KDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEE--AEEELAEAEAEIEELEAQIEQLKEELKALREALDELRA 810
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217287339  165 AARLLQmqtqGRSAEAQNFIDSLIELRGFLFEKLLTSPMEARDKAQFLQDISRQNSNNQQIIDTLEKELaERMKNRNAEV 244
Cdd:TIGR02168  811 ELTLLN----EEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESEL-EALLNERASL 885
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2217287339  245 EKENFVIQELKNHLHQVLKFSENSLVRTKQEAEKQQKAdFRASQARVAKIQQEILQLQSQF---YNLVMENREAEQALR 320
Cdd:TIGR02168  886 EEALALLRSELEELSEELRELESKRSELRRELEELREK-LAQLELRLEGLEVRIDNLQERLseeYSLTLEEAEALENKI 963
PRK10929 PRK10929
putative mechanosensitive channel protein; Provisional
96-325 8.47e-03

putative mechanosensitive channel protein; Provisional


Pssm-ID: 236798 [Multi-domain]  Cd Length: 1109  Bit Score: 38.88  E-value: 8.47e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217287339   96 DLCQVLLENVRCLKEKERQLQEQKEaeeegwlRDRLLSielqkSSLSPLMQQIKDStknvlRLLLSnpQAARLLQMQTQG 175
Cdd:PRK10929   106 ALEQEILQVSSQLLEKSRQAQQEQD-------RAREIS-----DSLSQLPQQQTEA-----RRQLN--EIERRLQTLGTP 166
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217287339  176 RSAEAQnfidslielrgflfEKLLTSPME-ARDKAQFLQ-DISRQNSNNQQIIDTLEKELAERmknRNAEVEKEnfvIQE 253
Cdd:PRK10929   167 NTPLAQ--------------AQLTALQAEsAALKALVDElELAQLSANNRQELARLRSELAKK---RSQQLDAY---LQA 226
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217287339  254 LKNHLH-QVLKFSENSLVRTKQEAEkqQKADFRASQARVAKIQQEILQL---QSQFYNLV-----------MENREAEQA 318
Cdd:PRK10929   227 LRNQLNsQRQREAERALESTELLAE--QSGDLPKSIVAQFKINRELSQAlnqQAQRMDLIasqqrqaasqtLQVRQALNT 304

                   ....*..
gi 2217287339  319 LRRNIKW 325
Cdd:PRK10929   305 LREQSQW 311
 
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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