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Conserved domains on  [gi|1838744807|ref|NP_001369318|]
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protein regulator of cytokinesis 1 isoform 9 [Mus musculus]

Protein Classification

protein regulator of cytokinesis family protein( domain architecture ID 12049048)

protein regulator of cytokinesis family protein is a microtubule-associated protein that plays a critical role in organizing the mitotic microtubule

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
MAP65_ASE1 pfam03999
Microtubule associated protein (MAP65/ASE1 family);
16-474 1.66e-174

Microtubule associated protein (MAP65/ASE1 family);


:

Pssm-ID: 427641 [Multi-domain]  Cd Length: 477  Bit Score: 504.15  E-value: 1.66e-174
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838744807  16 QKALTHLREIWELIGIPEEQRLQRTEVVKKHIKDLLDRMIAEEESLRERLLKSISICQKELSTLC-----SELQ--VKPF 88
Cdd:pfam03999   1 EKLLDHLHVIWQEIGFSEDKRLQILSRLKDHIKEFYTDALSEENDKEQRILQSIADLRAEAAILClymrnRLLHeeRDPF 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838744807  89 QEEKDTTILQLEKDLRTQVELMRKQKKERKQELKLLQEQEQELRDILCMPPCDVDSTSVPTLEELKLFRQRVATLRETKE 168
Cdd:pfam03999  81 EPKKGMSLLQKEKKLDTQLEHLRKEKAPRLAEIKELLEQLQQLCEELGEEPLPLLIDPLPSLEELESFRKHLENLRNEKE 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838744807 169 SRREEFVNIKKQIILCMEELEHSPDTSFERDVVCEDESAFCLSLENIATLQKLLKQLEMKKSQNEAECEGLRTQIRELWD 248
Cdd:pfam03999 161 RRLEEVNELKKQIKLLMEELDLVPGTDFEEDLLCESEDNFCLSRENIDKLRKLIKQLEEQKAEREEKIDDLREKILELWN 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838744807 249 RLQIPEEEREPVEAIMTGSKTKIRNALKLEVDRLEELKMQNIKQVIEKIRVELAQFWDQCFYSQEQRQAFAPYYSEDYTE 328
Cdd:pfam03999 241 RLQVPQEEQESFVRENNSLSQDTIDALREELQRLEELKKKNIKKLIEDLRVEIEELWDKLFYSTEQRKRFIPFFEELYTE 320
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838744807 329 NLLHLHDAEIVRLRNYYDVHKELFQGVQKWEESWKLFLEFERKASDPGRFTNRGGNL-LKEEKERAKLQKTLPKLEEELK 407
Cdd:pfam03999 321 DLLELHELELKRLKEEYESNKEILELVEKWEELWEDMEELEAKANDPSRFNNRGGKLlLKEEKERKRLTRKLPKIEQELT 400
                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1838744807 408 ARIEQWEQEHSTAFVVNGQKFMEYVTEQWELHRLEKE--RAKQERQLKNKKQTEAEMLYGSTP-----RTPSKR 474
Cdd:pfam03999 401 EKVEAWESEFGRPFLVNGEKLLEIIAEQWEELRQEKEreRLSQRKKLKGSKQTEREMLYGSAPnstlhRTPSKL 474
 
Name Accession Description Interval E-value
MAP65_ASE1 pfam03999
Microtubule associated protein (MAP65/ASE1 family);
16-474 1.66e-174

Microtubule associated protein (MAP65/ASE1 family);


Pssm-ID: 427641 [Multi-domain]  Cd Length: 477  Bit Score: 504.15  E-value: 1.66e-174
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838744807  16 QKALTHLREIWELIGIPEEQRLQRTEVVKKHIKDLLDRMIAEEESLRERLLKSISICQKELSTLC-----SELQ--VKPF 88
Cdd:pfam03999   1 EKLLDHLHVIWQEIGFSEDKRLQILSRLKDHIKEFYTDALSEENDKEQRILQSIADLRAEAAILClymrnRLLHeeRDPF 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838744807  89 QEEKDTTILQLEKDLRTQVELMRKQKKERKQELKLLQEQEQELRDILCMPPCDVDSTSVPTLEELKLFRQRVATLRETKE 168
Cdd:pfam03999  81 EPKKGMSLLQKEKKLDTQLEHLRKEKAPRLAEIKELLEQLQQLCEELGEEPLPLLIDPLPSLEELESFRKHLENLRNEKE 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838744807 169 SRREEFVNIKKQIILCMEELEHSPDTSFERDVVCEDESAFCLSLENIATLQKLLKQLEMKKSQNEAECEGLRTQIRELWD 248
Cdd:pfam03999 161 RRLEEVNELKKQIKLLMEELDLVPGTDFEEDLLCESEDNFCLSRENIDKLRKLIKQLEEQKAEREEKIDDLREKILELWN 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838744807 249 RLQIPEEEREPVEAIMTGSKTKIRNALKLEVDRLEELKMQNIKQVIEKIRVELAQFWDQCFYSQEQRQAFAPYYSEDYTE 328
Cdd:pfam03999 241 RLQVPQEEQESFVRENNSLSQDTIDALREELQRLEELKKKNIKKLIEDLRVEIEELWDKLFYSTEQRKRFIPFFEELYTE 320
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838744807 329 NLLHLHDAEIVRLRNYYDVHKELFQGVQKWEESWKLFLEFERKASDPGRFTNRGGNL-LKEEKERAKLQKTLPKLEEELK 407
Cdd:pfam03999 321 DLLELHELELKRLKEEYESNKEILELVEKWEELWEDMEELEAKANDPSRFNNRGGKLlLKEEKERKRLTRKLPKIEQELT 400
                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1838744807 408 ARIEQWEQEHSTAFVVNGQKFMEYVTEQWELHRLEKE--RAKQERQLKNKKQTEAEMLYGSTP-----RTPSKR 474
Cdd:pfam03999 401 EKVEAWESEFGRPFLVNGEKLLEIIAEQWEELRQEKEreRLSQRKKLKGSKQTEREMLYGSAPnstlhRTPSKL 474
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
1-262 1.62e-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: 48.14  E-value: 1.62e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838744807    1 MRRSEVLADESITCLQKALTHLREIWELIGIPEEQRLQRTEVVKKHIKDL-------LDRMIAEEESLRERLLKSISICQ 73
Cdd:TIGR02169  235 LERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLgeeeqlrVKEKIGELEAEIASLERSIAEKE 314
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838744807   74 KELSTLcsELQVKPFQEEKDTTILQLEkDLRTQVELMRKQKKERKQELKLLQEQEQELRDILCmppcDVDSTSVPTLEEL 153
Cdd:TIGR02169  315 RELEDA--EERLAKLEAEIDKLLAEIE-ELEREIEEERKRRDKLTEEYAELKEELEDLRAELE----EVDKEFAETRDEL 387
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838744807  154 KLFRQRVATL-RETKESRREEFVNIKKQIILCMEELEHSPDTSFERDVVCEDESAFCLSLENIATLQKLLKQLEMKKSQN 232
Cdd:TIGR02169  388 KDYREKLEKLkREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKY 467
                          250       260       270
                   ....*....|....*....|....*....|
gi 1838744807  233 EAECEGLRTQIRELWDRLQIPEEEREPVEA 262
Cdd:TIGR02169  468 EQELYDLKEEYDRVEKELSKLQRELAEAEA 497
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
50-258 5.56e-04

Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 42.83  E-value: 5.56e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838744807  50 LLDRMIAEEESLRERLLKSISICQKELSTLCSELQVKPFQEEKDTTILQLEKDLRTQVELMRKQKKERKQELKLLQEQEQ 129
Cdd:COG4717    47 LLERLEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQ 126
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838744807 130 ELRDILCMPPCDVDSTSVPT-LEELKLFRQRVATLRETKESRREEFVNIKKQIILCMEELEHSPDTSFERdvvcedesaf 208
Cdd:COG4717   127 LLPLYQELEALEAELAELPErLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQD---------- 196
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 1838744807 209 clSLENIATLQKLLKQLEMKKSQNEAECEGLRTQIRELWDRLQIPEEERE 258
Cdd:COG4717   197 --LAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEER 244
 
Name Accession Description Interval E-value
MAP65_ASE1 pfam03999
Microtubule associated protein (MAP65/ASE1 family);
16-474 1.66e-174

Microtubule associated protein (MAP65/ASE1 family);


Pssm-ID: 427641 [Multi-domain]  Cd Length: 477  Bit Score: 504.15  E-value: 1.66e-174
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838744807  16 QKALTHLREIWELIGIPEEQRLQRTEVVKKHIKDLLDRMIAEEESLRERLLKSISICQKELSTLC-----SELQ--VKPF 88
Cdd:pfam03999   1 EKLLDHLHVIWQEIGFSEDKRLQILSRLKDHIKEFYTDALSEENDKEQRILQSIADLRAEAAILClymrnRLLHeeRDPF 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838744807  89 QEEKDTTILQLEKDLRTQVELMRKQKKERKQELKLLQEQEQELRDILCMPPCDVDSTSVPTLEELKLFRQRVATLRETKE 168
Cdd:pfam03999  81 EPKKGMSLLQKEKKLDTQLEHLRKEKAPRLAEIKELLEQLQQLCEELGEEPLPLLIDPLPSLEELESFRKHLENLRNEKE 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838744807 169 SRREEFVNIKKQIILCMEELEHSPDTSFERDVVCEDESAFCLSLENIATLQKLLKQLEMKKSQNEAECEGLRTQIRELWD 248
Cdd:pfam03999 161 RRLEEVNELKKQIKLLMEELDLVPGTDFEEDLLCESEDNFCLSRENIDKLRKLIKQLEEQKAEREEKIDDLREKILELWN 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838744807 249 RLQIPEEEREPVEAIMTGSKTKIRNALKLEVDRLEELKMQNIKQVIEKIRVELAQFWDQCFYSQEQRQAFAPYYSEDYTE 328
Cdd:pfam03999 241 RLQVPQEEQESFVRENNSLSQDTIDALREELQRLEELKKKNIKKLIEDLRVEIEELWDKLFYSTEQRKRFIPFFEELYTE 320
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838744807 329 NLLHLHDAEIVRLRNYYDVHKELFQGVQKWEESWKLFLEFERKASDPGRFTNRGGNL-LKEEKERAKLQKTLPKLEEELK 407
Cdd:pfam03999 321 DLLELHELELKRLKEEYESNKEILELVEKWEELWEDMEELEAKANDPSRFNNRGGKLlLKEEKERKRLTRKLPKIEQELT 400
                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1838744807 408 ARIEQWEQEHSTAFVVNGQKFMEYVTEQWELHRLEKE--RAKQERQLKNKKQTEAEMLYGSTP-----RTPSKR 474
Cdd:pfam03999 401 EKVEAWESEFGRPFLVNGEKLLEIIAEQWEELRQEKEreRLSQRKKLKGSKQTEREMLYGSAPnstlhRTPSKL 474
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
1-262 1.62e-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: 48.14  E-value: 1.62e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838744807    1 MRRSEVLADESITCLQKALTHLREIWELIGIPEEQRLQRTEVVKKHIKDL-------LDRMIAEEESLRERLLKSISICQ 73
Cdd:TIGR02169  235 LERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLgeeeqlrVKEKIGELEAEIASLERSIAEKE 314
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838744807   74 KELSTLcsELQVKPFQEEKDTTILQLEkDLRTQVELMRKQKKERKQELKLLQEQEQELRDILCmppcDVDSTSVPTLEEL 153
Cdd:TIGR02169  315 RELEDA--EERLAKLEAEIDKLLAEIE-ELEREIEEERKRRDKLTEEYAELKEELEDLRAELE----EVDKEFAETRDEL 387
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838744807  154 KLFRQRVATL-RETKESRREEFVNIKKQIILCMEELEHSPDTSFERDVVCEDESAFCLSLENIATLQKLLKQLEMKKSQN 232
Cdd:TIGR02169  388 KDYREKLEKLkREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKY 467
                          250       260       270
                   ....*....|....*....|....*....|
gi 1838744807  233 EAECEGLRTQIRELWDRLQIPEEEREPVEA 262
Cdd:TIGR02169  468 EQELYDLKEEYDRVEKELSKLQRELAEAEA 497
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
33-422 2.23e-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: 47.76  E-value: 2.23e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838744807   33 EEQRLQRTEVVKKHIKDLLDRMIAEEESLRER---LLKSISICQKELSTLCSELQVKPFQEEKDTTILqleKDLRTQVEL 109
Cdd:TIGR02169  672 EPAELQRLRERLEGLKRELSSLQSELRRIENRldeLSQELSDASRKIGEIEKEIEQLEQEEEKLKERL---EELEEDLSS 748
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838744807  110 MRKQKKERKQELKLLQEQEQELRDILcmppcdvdSTSVPTLEELK--LFRQRVATLRETKESRREEFVNIKKQIILCMEE 187
Cdd:TIGR02169  749 LEQEIENVKSELKELEARIEELEEDL--------HKLEEALNDLEarLSHSRIPEIQAELSKLEEEVSRIEARLREIEQK 820
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838744807  188 LEH-SPDTSFERDVVCEDESAFCLSLENIATLQKLLKQLEMKKSQNEAECEGLRTQIRELWDRLQIPEEEREPVEAIMTG 266
Cdd:TIGR02169  821 LNRlTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRE 900
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838744807  267 SKTKIrNALKLEVDRLEELkMQNIKQVIEKIRVELAQFWDQCFYSQEQRQAFAPYysEDYTENLLHLHdaeiVRLRNYYD 346
Cdd:TIGR02169  901 LERKI-EELEAQIEKKRKR-LSELKAKLEALEEELSEIEDPKGEDEEIPEEELSL--EDVQAELQRVE----EEIRALEP 972
                          330       340       350       360       370       380       390
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1838744807  347 VHkelFQGVQKWEESWKLFLEFERKAsdpgrftnrggNLLKEEKEraklqktlpkleeELKARIEQWEQEHSTAFV 422
Cdd:TIGR02169  973 VN---MLAIQEYEEVLKRLDELKEKR-----------AKLEEERK-------------AILERIEEYEKKKREVFM 1021
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
91-318 9.76e-05

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: 45.82  E-value: 9.76e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838744807   91 EKDTTILQLEKDLRTQVELMRKQKKERKQELKLLQEQEQELRDILCMPPcDVDSTSVPTLEELKLFRQRVATLRETKESR 170
Cdd:TIGR02168  674 ERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELE-ELSRQISALRKDLARLEAEVEQLEERIAQL 752
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838744807  171 REEFVNIKKQIILCMEELEhspdtsferdvvcEDESAFCLSLENIATLQKLLKQLEMKKSQNEAECEGLRTQIRELWDRL 250
Cdd:TIGR02168  753 SKELTELEAEIEELEERLE-------------EAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEA 819
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838744807  251 QIPEEEREpveaimtgsktKIRNALKLEVDRLEELKMQ--NIKQVIEKIRVELAQFWDQCFYSQEQRQAF 318
Cdd:TIGR02168  820 ANLRERLE-----------SLERRIAATERRLEDLEEQieELSEDIESLAAEIEELEELIEELESELEAL 878
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
50-258 5.56e-04

Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 42.83  E-value: 5.56e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838744807  50 LLDRMIAEEESLRERLLKSISICQKELSTLCSELQVKPFQEEKDTTILQLEKDLRTQVELMRKQKKERKQELKLLQEQEQ 129
Cdd:COG4717    47 LLERLEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQ 126
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838744807 130 ELRDILCMPPCDVDSTSVPT-LEELKLFRQRVATLRETKESRREEFVNIKKQIILCMEELEHSPDTSFERdvvcedesaf 208
Cdd:COG4717   127 LLPLYQELEALEAELAELPErLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQD---------- 196
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 1838744807 209 clSLENIATLQKLLKQLEMKKSQNEAECEGLRTQIRELWDRLQIPEEERE 258
Cdd:COG4717   197 --LAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEER 244
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
97-303 3.61e-03

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 40.31  E-value: 3.61e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838744807  97 LQLEKDLRtQVELMRKQKKERKQELKLLQEQEQELRDILcmppcDVDSTSVPTLE-ELKLFRQRVATLRETKESRREEFV 175
Cdd:COG1196   218 LKEELKEL-EAELLLLKLRELEAELEELEAELEELEAEL-----EELEAELAELEaELEELRLELEELELELEEAQAEEY 291
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838744807 176 NIKKQIilcmEELEHspdtsfERDVVCEDESAfclSLENIATLQKLLKQLEMKKSQNEAECEGLRTQIRELWDRLQIPEE 255
Cdd:COG1196   292 ELLAEL----ARLEQ------DIARLEERRRE---LEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEA 358
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 1838744807 256 EREPVEAIMTGSKTKIRNALKLEVDRLEELkmQNIKQVIEKIRVELAQ 303
Cdd:COG1196   359 ELAEAEEALLEAEAELAEAEEELEELAEEL--LEALRAAAELAAQLEE 404
CALCOCO1 pfam07888
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ...
2-137 7.62e-03

Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.


Pssm-ID: 462303 [Multi-domain]  Cd Length: 488  Bit Score: 39.11  E-value: 7.62e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838744807   2 RRSEVLADESITCLQKALTHLREIWELIGIPE--EQRLQRTEVVKKHIKDLLDRMIA---EEESLRERLLKSISICQKEL 76
Cdd:pfam07888 108 ASSEELSEEKDALLAQRAAHEARIRELEEDIKtlTQRVLERETELERMKERAKKAGAqrkEEEAERKQLQAKLQQTEEEL 187
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1838744807  77 STLCSELQV-KPFQEEKDTTILQLEKDLrTQVELMRKQKKERKQELKLLQEQEQELRDILCM 137
Cdd:pfam07888 188 RSLSKEFQElRNSLAQRDTQVLQLQDTI-TTLTQKLTTAHRKEAENEALLEELRSLQERLNA 248
 
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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