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Conserved domains on  [gi|30017397|ref|NP_835186|]
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ELKS/Rab6-interacting/CAST family member 1 isoform 2 [Mus musculus]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
Cast super family cl37807
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ...
3-347 1.97e-171

RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.


The actual alignment was detected with superfamily member pfam10174:

Pssm-ID: 431111 [Multi-domain]  Cd Length: 766  Bit Score: 496.65  E-value: 1.97e-171
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30017397     3 LQTQLKEVLRENDLLRKDVEVKESKLSSSMNSIKTFWSPELKKERALRKDEASKITIWKEQYRVVQEENQHMQMTIQALQ 82
Cdd:pfam10174   1 LQAQLRDLQRENELLRRELDIKESKLGSSMNSIKTFWSPELKKERALRKEEAARISVLKEQYRVTQEENQHLQLTIQALQ 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30017397    83 DELRIQRDLNQLFQQD--SSSRTGEPCVA--ELTEENFQRLHAEHERQAKELFLLRKTLEEMELRIETQKQTLNARDESI 158
Cdd:pfam10174  81 DELRAQRDLNQLLQQDftTSPVDGEDKFStpELTEENFRRLQSEHERQAKELFLLRKTLEEMELRIETQKQTLGARDESI 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30017397   159 KKLLEMLQSKGLSAKATEEDHERTRRLAEAEMHVHHLESLLEQKEKENNMLREEMHRRFENAPDSAKTKALQTVIEMKDS 238
Cdd:pfam10174 161 KKLLEMLQSKGLPKKSGEEDWERTRRIAEAEMQLGHLEVLLDQKEKENIHLREELHRRNQLQPDPAKTKALQTVIEMKDT 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30017397   239 KISSMERGLRDLEEEIQMLKSNGALSSEEREEEMKQMEVYRSHSKFMKNKIGQVKQELSRKDTELLALQTKLETLTNQFS 318
Cdd:pfam10174 241 KISSLERNIRDLEDEVQMLKTNGLLHTEDREEEIKQMEVYKSHSKFMKNKIDQLKQELSKKESELLALQTKLETLTNQNS 320
                         330       340
                  ....*....|....*....|....*....
gi 30017397   319 DSKQHIEVLKESLTAKEQRAAILQTEVKS 347
Cdd:pfam10174 321 DCKQHIEVLKESLTAKEQRAAILQTEVDA 349
 
Name Accession Description Interval E-value
Cast pfam10174
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ...
3-347 1.97e-171

RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.


Pssm-ID: 431111 [Multi-domain]  Cd Length: 766  Bit Score: 496.65  E-value: 1.97e-171
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30017397     3 LQTQLKEVLRENDLLRKDVEVKESKLSSSMNSIKTFWSPELKKERALRKDEASKITIWKEQYRVVQEENQHMQMTIQALQ 82
Cdd:pfam10174   1 LQAQLRDLQRENELLRRELDIKESKLGSSMNSIKTFWSPELKKERALRKEEAARISVLKEQYRVTQEENQHLQLTIQALQ 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30017397    83 DELRIQRDLNQLFQQD--SSSRTGEPCVA--ELTEENFQRLHAEHERQAKELFLLRKTLEEMELRIETQKQTLNARDESI 158
Cdd:pfam10174  81 DELRAQRDLNQLLQQDftTSPVDGEDKFStpELTEENFRRLQSEHERQAKELFLLRKTLEEMELRIETQKQTLGARDESI 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30017397   159 KKLLEMLQSKGLSAKATEEDHERTRRLAEAEMHVHHLESLLEQKEKENNMLREEMHRRFENAPDSAKTKALQTVIEMKDS 238
Cdd:pfam10174 161 KKLLEMLQSKGLPKKSGEEDWERTRRIAEAEMQLGHLEVLLDQKEKENIHLREELHRRNQLQPDPAKTKALQTVIEMKDT 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30017397   239 KISSMERGLRDLEEEIQMLKSNGALSSEEREEEMKQMEVYRSHSKFMKNKIGQVKQELSRKDTELLALQTKLETLTNQFS 318
Cdd:pfam10174 241 KISSLERNIRDLEDEVQMLKTNGLLHTEDREEEIKQMEVYKSHSKFMKNKIDQLKQELSKKESELLALQTKLETLTNQNS 320
                         330       340
                  ....*....|....*....|....*....
gi 30017397   319 DSKQHIEVLKESLTAKEQRAAILQTEVKS 347
Cdd:pfam10174 321 DCKQHIEVLKESLTAKEQRAAILQTEVDA 349
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
79-347 3.52e-08

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 55.33  E-value: 3.52e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30017397  79 QALQDELRiQRDLNQLFQQDsssrtgepcvaELTEENFQRLHAEHERQAKELFLLRKTLEEMELRIETQKQTLNARDESI 158
Cdd:COG1196 216 RELKEELK-ELEAELLLLKL-----------RELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELEL 283
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30017397 159 KKLLEMLQSKGLSAKATEEDHERTR-RLAEAEMHVHHLESLLEQKEKENNMLREEMHRRFENApdsaktKALQTVIEMKD 237
Cdd:COG1196 284 EEAQAEEYELLAELARLEQDIARLEeRRRELEERLEELEEELAELEEELEELEEELEELEEEL------EEAEEELEEAE 357
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30017397 238 SKISSMERGLRDLEEEIQMLKSNGALSSEEREEEMKQMEVYRSHSKFMKNKIGQVKQELSRKDTELLALQTKLETLTNQF 317
Cdd:COG1196 358 AELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEE 437
                       250       260       270
                ....*....|....*....|....*....|
gi 30017397 318 SDSKQHIEVLKESLTAKEQRAAILQTEVKS 347
Cdd:COG1196 438 EEEEEALEEAAEEEAELEEEEEALLELLAE 467
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
42-336 3.62e-08

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: 55.45  E-value: 3.62e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30017397     42 ELKKERALRKDEASKITIWKEQYRVVQEENQHMQ-MTIQALQDELRIQRDLNQLFQQDSSSRTGEpcvaELTEENFQRLH 120
Cdd:TIGR02168  678 EIEELEEKIEELEEKIAELEKALAELRKELEELEeELEQLRKELEELSRQISALRKDLARLEAEV----EQLEERIAQLS 753
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30017397    121 AEHERQAKELFLLRKTLEEMELRIETQKQTLNARDESIKKLLEMLQSKGLSAKATEEDHERTR-RLAEAEMHVHHLESLL 199
Cdd:TIGR02168  754 KELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNeEAANLRERLESLERRI 833
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30017397    200 EQKEKENNMLREEmhrrfenapdsakTKALQTVIEMKDSKISSMERGLRDLEEEIQMLksngalsSEEREEEMKQMEVYR 279
Cdd:TIGR02168  834 AATERRLEDLEEQ-------------IEELSEDIESLAAEIEELEELIEELESELEAL-------LNERASLEEALALLR 893
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 30017397    280 SHSKFMKNKIGQVKQELSRKDTELLALQTKLETLTNQFSDSKQHIEVLKESLTAKEQ 336
Cdd:TIGR02168  894 SELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLSEEYS 950
46 PHA02562
endonuclease subunit; Provisional
58-270 2.78e-04

endonuclease subunit; Provisional


Pssm-ID: 222878 [Multi-domain]  Cd Length: 562  Bit Score: 42.69  E-value: 2.78e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30017397   58 TIWKEQYRVVQEENQHMQMTIQALQDELRIQRDlnqlFQQDSSSRTGEPcVAELTE------ENFQRLHAEHERQAKELF 131
Cdd:PHA02562 170 KLNKDKIRELNQQIQTLDMKIDHIQQQIKTYNK----NIEEQRKKNGEN-IARKQNkydelvEEAKTIKAEIEELTDELL 244
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30017397  132 LLRKTLEEME---LRIETQKQTLNARDESIKKLLEMLQSKGLSAKATEEDHERTRRLAEAEMHVHHLESLLEQKEKENNM 208
Cdd:PHA02562 245 NLVMDIEDPSaalNKLNTAAAKIKSKIEQFQKVIKMYEKGGVCPTCTQQISEGPDRITKIKDKLKELQHSLEKLDTAIDE 324
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 30017397  209 LREEMHRRFENapdSAKTKALQTVIEMKDSKISSMERGLRDLEEEIQMLKSNGALSSEEREE 270
Cdd:PHA02562 325 LEEIMDEFNEQ---SKKLLELKNKISTNKQSLITLVDKAKKVKAAIEELQAEFVDNAEELAK 383
 
Name Accession Description Interval E-value
Cast pfam10174
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ...
3-347 1.97e-171

RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.


Pssm-ID: 431111 [Multi-domain]  Cd Length: 766  Bit Score: 496.65  E-value: 1.97e-171
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30017397     3 LQTQLKEVLRENDLLRKDVEVKESKLSSSMNSIKTFWSPELKKERALRKDEASKITIWKEQYRVVQEENQHMQMTIQALQ 82
Cdd:pfam10174   1 LQAQLRDLQRENELLRRELDIKESKLGSSMNSIKTFWSPELKKERALRKEEAARISVLKEQYRVTQEENQHLQLTIQALQ 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30017397    83 DELRIQRDLNQLFQQD--SSSRTGEPCVA--ELTEENFQRLHAEHERQAKELFLLRKTLEEMELRIETQKQTLNARDESI 158
Cdd:pfam10174  81 DELRAQRDLNQLLQQDftTSPVDGEDKFStpELTEENFRRLQSEHERQAKELFLLRKTLEEMELRIETQKQTLGARDESI 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30017397   159 KKLLEMLQSKGLSAKATEEDHERTRRLAEAEMHVHHLESLLEQKEKENNMLREEMHRRFENAPDSAKTKALQTVIEMKDS 238
Cdd:pfam10174 161 KKLLEMLQSKGLPKKSGEEDWERTRRIAEAEMQLGHLEVLLDQKEKENIHLREELHRRNQLQPDPAKTKALQTVIEMKDT 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30017397   239 KISSMERGLRDLEEEIQMLKSNGALSSEEREEEMKQMEVYRSHSKFMKNKIGQVKQELSRKDTELLALQTKLETLTNQFS 318
Cdd:pfam10174 241 KISSLERNIRDLEDEVQMLKTNGLLHTEDREEEIKQMEVYKSHSKFMKNKIDQLKQELSKKESELLALQTKLETLTNQNS 320
                         330       340
                  ....*....|....*....|....*....
gi 30017397   319 DSKQHIEVLKESLTAKEQRAAILQTEVKS 347
Cdd:pfam10174 321 DCKQHIEVLKESLTAKEQRAAILQTEVDA 349
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
79-347 3.52e-08

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 55.33  E-value: 3.52e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30017397  79 QALQDELRiQRDLNQLFQQDsssrtgepcvaELTEENFQRLHAEHERQAKELFLLRKTLEEMELRIETQKQTLNARDESI 158
Cdd:COG1196 216 RELKEELK-ELEAELLLLKL-----------RELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELEL 283
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30017397 159 KKLLEMLQSKGLSAKATEEDHERTR-RLAEAEMHVHHLESLLEQKEKENNMLREEMHRRFENApdsaktKALQTVIEMKD 237
Cdd:COG1196 284 EEAQAEEYELLAELARLEQDIARLEeRRRELEERLEELEEELAELEEELEELEEELEELEEEL------EEAEEELEEAE 357
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30017397 238 SKISSMERGLRDLEEEIQMLKSNGALSSEEREEEMKQMEVYRSHSKFMKNKIGQVKQELSRKDTELLALQTKLETLTNQF 317
Cdd:COG1196 358 AELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEE 437
                       250       260       270
                ....*....|....*....|....*....|
gi 30017397 318 SDSKQHIEVLKESLTAKEQRAAILQTEVKS 347
Cdd:COG1196 438 EEEEEALEEAAEEEAELEEEEEALLELLAE 467
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
42-336 3.62e-08

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: 55.45  E-value: 3.62e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30017397     42 ELKKERALRKDEASKITIWKEQYRVVQEENQHMQ-MTIQALQDELRIQRDLNQLFQQDSSSRTGEpcvaELTEENFQRLH 120
Cdd:TIGR02168  678 EIEELEEKIEELEEKIAELEKALAELRKELEELEeELEQLRKELEELSRQISALRKDLARLEAEV----EQLEERIAQLS 753
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30017397    121 AEHERQAKELFLLRKTLEEMELRIETQKQTLNARDESIKKLLEMLQSKGLSAKATEEDHERTR-RLAEAEMHVHHLESLL 199
Cdd:TIGR02168  754 KELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNeEAANLRERLESLERRI 833
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30017397    200 EQKEKENNMLREEmhrrfenapdsakTKALQTVIEMKDSKISSMERGLRDLEEEIQMLksngalsSEEREEEMKQMEVYR 279
Cdd:TIGR02168  834 AATERRLEDLEEQ-------------IEELSEDIESLAAEIEELEELIEELESELEAL-------LNERASLEEALALLR 893
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 30017397    280 SHSKFMKNKIGQVKQELSRKDTELLALQTKLETLTNQFSDSKQHIEVLKESLTAKEQ 336
Cdd:TIGR02168  894 SELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLSEEYS 950
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
52-351 1.41e-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: 46.97  E-value: 1.41e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30017397     52 DEASKITIWKEQYRVVQEENQHMQMTIQALQDELR-IQRDLNQLFQQDSSSRTGEPCVAELTEENFQRLHAEHERQAKEL 130
Cdd:TIGR02168  162 EEAAGISKYKERRKETERKLERTRENLDRLEDILNeLERQLKSLERQAEKAERYKELKAELRELELALLVLRLEELREEL 241
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30017397    131 FLLRKTLEEMELRIETQKQTLNARDESIKKL-LEMLQSKGLSAKATEEDHERTRRLAEAEMHVHHLESLLEQKEKENNML 209
Cdd:TIGR02168  242 EELQEELKEAEEELEELTAELQELEEKLEELrLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEEL 321
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30017397    210 REEMhRRFENAPDSAKTKA---------LQTVIEMKDSKISS-------MERGLRDLEEEIQMLKSNGALSSEEREEEMK 273
Cdd:TIGR02168  322 EAQL-EELESKLDELAEELaeleekleeLKEELESLEAELEEleaeleeLESRLEELEEQLETLRSKVAQLELQIASLNN 400
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30017397    274 QMEVYRSH-------------------SKFMKNKIGQVKQELSRKDTELLALQTKLETLTNQFSDSKQHIEVLKESLTAK 334
Cdd:TIGR02168  401 EIERLEARlerledrrerlqqeieellKKLEEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAA 480
                          330
                   ....*....|....*..
gi 30017397    335 EQRAAILQTEVKSFCDL 351
Cdd:TIGR02168  481 ERELAQLQARLDSLERL 497
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
122-346 2.34e-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: 46.60  E-value: 2.34e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30017397    122 EHERQAKELFLLRKTLEEMELRIETQKQTLNARDESIKKLLEMLQSKgLSAKATEEDHERTRRLAEAEMHVHHLESLLEQ 201
Cdd:TIGR02169  234 ALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKK-IKDLGEEEQLRVKEKIGELEAEIASLERSIAE 312
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30017397    202 KEKENNMLREEMhrrfenAPDSAKTKALQTVIEMKDSKISSMERGLRDLEEEIQMLKSNGALSSEEREEEMKQMEVYRSH 281
Cdd:TIGR02169  313 KERELEDAEERL------AKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDE 386
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 30017397    282 SKFMKNKIGQVKQELSRKDTELLALQTKLETLTNQFSDSKQHIEVLKESLTAKEQRAAILQTEVK 346
Cdd:TIGR02169  387 LKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIK 451
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
61-343 9.42e-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: 44.67  E-value: 9.42e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30017397     61 KEQYRVVQEENQHMQMTIQALQDEL-RIQRDLNQLFQ--QDSSSRTGEpcvaelTEENFQRLHAEHERQAKELfllrktl 137
Cdd:TIGR02169  673 PAELQRLRERLEGLKRELSSLQSELrRIENRLDELSQelSDASRKIGE------IEKEIEQLEQEEEKLKERL------- 739
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30017397    138 EEMELRIETQKQTLNARDESIKKLLEMLQSKGLSAKATEEdhertrrlAEAEMHVHHLESLLEQKEKENNMLREEmHRRF 217
Cdd:TIGR02169  740 EELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEE--------ALNDLEARLSHSRIPEIQAELSKLEEE-VSRI 810
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30017397    218 ENAPDSAktkalqtviemkDSKISSMERGLRDLEEEIQMLKSNGALSSEEREEEMKQMEVYRSHSKFMKNKIGQVKQELS 297
Cdd:TIGR02169  811 EARLREI------------EQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALR 878
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*.
gi 30017397    298 RKDTELLALQTKLETLTNQFSDSKQHIEVLKESLTAKEQRAAILQT 343
Cdd:TIGR02169  879 DLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKA 924
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
42-271 1.31e-04

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 44.16  E-value: 1.31e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30017397  42 ELKKERALRKDEASKITIWKEQYRVVQEENQHMQMTIQALQDELR-IQRDLNQLFQQDSSSRTGepcvAELTEENFQRLH 120
Cdd:COG1196 247 ELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYeLLAELARLEQDIARLEER----RRELEERLEELE 322
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30017397 121 AEHERQAKELFLLRKTLEEMELRIETQKQTLNARDESIKKLLEMLQSKGLSAKATEED-HERTRRLAEAEMHVHHLESLL 199
Cdd:COG1196 323 EELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEElEELAEELLEALRAAAELAAQL 402
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 30017397 200 EQKEK--ENNMLREEMHRRFENAPDSAKTKALQTVIEMKDSKISSMERGLRDLEEEIQMLKSNGALSSEEREEE 271
Cdd:COG1196 403 EELEEaeEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLE 476
46 PHA02562
endonuclease subunit; Provisional
58-270 2.78e-04

endonuclease subunit; Provisional


Pssm-ID: 222878 [Multi-domain]  Cd Length: 562  Bit Score: 42.69  E-value: 2.78e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30017397   58 TIWKEQYRVVQEENQHMQMTIQALQDELRIQRDlnqlFQQDSSSRTGEPcVAELTE------ENFQRLHAEHERQAKELF 131
Cdd:PHA02562 170 KLNKDKIRELNQQIQTLDMKIDHIQQQIKTYNK----NIEEQRKKNGEN-IARKQNkydelvEEAKTIKAEIEELTDELL 244
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30017397  132 LLRKTLEEME---LRIETQKQTLNARDESIKKLLEMLQSKGLSAKATEEDHERTRRLAEAEMHVHHLESLLEQKEKENNM 208
Cdd:PHA02562 245 NLVMDIEDPSaalNKLNTAAAKIKSKIEQFQKVIKMYEKGGVCPTCTQQISEGPDRITKIKDKLKELQHSLEKLDTAIDE 324
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 30017397  209 LREEMHRRFENapdSAKTKALQTVIEMKDSKISSMERGLRDLEEEIQMLKSNGALSSEEREE 270
Cdd:PHA02562 325 LEEIMDEFNEQ---SKKLLELKNKISTNKQSLITLVDKAKKVKAAIEELQAEFVDNAEELAK 383
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
126-347 6.66e-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: 41.97  E-value: 6.66e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30017397    126 QAKELFLLRKTLEEMELRIETQKQTLNARDESIKKLLEMLQSKGLSAKATEEDHERTR-RLAEAEMHVHHLESLLEQKEK 204
Cdd:TIGR02168  675 RRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRkDLARLEAEVEQLEERIAQLSK 754
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30017397    205 ENNMLREEMHR--------RFENAPDSAKTKALQTVIEMKDSKISSMERGLRDLEEEIQMLKSNGALSSEEREEEMKQME 276
Cdd:TIGR02168  755 ELTELEAEIEEleerleeaEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIA 834
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 30017397    277 VYRSHSKFMKNKIGQVKQELSRKDTELLALQTKLETLTNQFSDSKQHIEVLKESLTAKEQRAAILQTEVKS 347
Cdd:TIGR02168  835 ATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRE 905
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
126-347 1.46e-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: 40.13  E-value: 1.46e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30017397 126 QAKELFLLRKTLEEMELRIETQKQTLNARDESIKKLLEMLQskglsaKATEEDHERTRRLAEAEMHVHHLESLLEQKEKE 205
Cdd:COG4942  18 QADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLA------ALERRIAALARRIRALEQELAALEAELAELEKE 91
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30017397 206 NNMLREEMHRRFENApdsaktkALQTVIEMKDSKISSMERGLR--DLEEEIQMLKSNGALSSEEREeemkQMEVYRSHSK 283
Cdd:COG4942  92 IAELRAELEAQKEEL-------AELLRALYRLGRQPPLALLLSpeDFLDAVRRLQYLKYLAPARRE----QAEELRADLA 160
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 30017397 284 FMKNKIGQVKQELSRKDTELLALQTKLETLTNQFSDSKQHIEVLKESLTAKEQRAAILQTEVKS 347
Cdd:COG4942 161 ELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEE 224
COG5022 COG5022
Myosin heavy chain [General function prediction only];
77-314 5.02e-03

Myosin heavy chain [General function prediction only];


Pssm-ID: 227355 [Multi-domain]  Cd Length: 1463  Bit Score: 38.91  E-value: 5.02e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30017397   77 TIQALQDELRIQRDLNQLFQQDSSsrtgepCVAELTEENFQRLHAEHERQakelfllrKTLEEMELRIETQKQTLNARDE 156
Cdd:COG5022  818 CIIKLQKTIKREKKLRETEEVEFS------LKAEVLIQKFGRSLKAKKRF--------SLLKKETIYLQSAQRVELAERQ 883
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30017397  157 SIKKLLEMLQSKGLSAKATEEDhertrrlaeaemhvhhlESLLEQKEKENNMLREEMHRRfenapdSAKTKALQTVIEMK 236
Cdd:COG5022  884 LQELKIDVKSISSLKLVNLELE-----------------SEIIELKKSLSSDLIENLEFK------TELIARLKKLLNNI 940
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 30017397  237 DSKI-SSMERGLRDLEEEIQMLKSNGALSSEEREEEMKQMEVYRSHSKFMKNKIGQVKQELSRKDTELLALQTKLETLT 314
Cdd:COG5022  941 DLEEgPSIEYVKLPELNKLHEVESKLKETSEEYEDLLKKSTILVREGNKANSELKNFKKELAELSKQYGALQESTKQLK 1019
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
5-258 7.21e-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: 38.50  E-value: 7.21e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30017397      5 TQLKEVLRENDLLRKDVEVKESKLSSSMNSIKTFWSpELKKERALRKDEASKIT-IWKEQYRVVQEENQHMQMTIQALQD 83
Cdd:TIGR02168  235 EELREELEELQEELKEAEEELEELTAELQELEEKLE-ELRLEVSELEEEIEELQkELYALANEISRLEQQKQILRERLAN 313
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30017397     84 ELRIQRDLNQLFQQDSSSRTGEPCVAELTEENFQRLHAEHERQAKELFLLRKTLEEMELRIET----------------- 146
Cdd:TIGR02168  314 LERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEEleeqletlrskvaqlel 393
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30017397    147 QKQTLNARDESIKKLLEMLQSKglSAKATEEDHERTRRLAEAEMHVHHLESLLEQKEKENNMLREEMHRRFENAPDSAKT 226
Cdd:TIGR02168  394 QIASLNNEIERLEARLERLEDR--RERLQQEIEELLKKLEEAELKELQAELEELEEELEELQEELERLEEALEELREELE 471
                          250       260       270
                   ....*....|....*....|....*....|....*...
gi 30017397    227 KALQTVIEMKD------SKISSMERGLRDLEEEIQMLK 258
Cdd:TIGR02168  472 EAEQALDAAERelaqlqARLDSLERLQENLEGFSEGVK 509
CCDC73 pfam15818
Coiled-coil domain-containing protein 73 family; CCDC73 is a family of eukaryotic coiled-coil ...
43-217 7.95e-03

Coiled-coil domain-containing protein 73 family; CCDC73 is a family of eukaryotic coiled-coil containing proteins. The function is not known. The alternative name is sarcoma antigen NY-SAR-79.


Pssm-ID: 464893 [Multi-domain]  Cd Length: 1048  Bit Score: 38.39  E-value: 7.95e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30017397     43 LKKERALRKDEASKITIWKEQYRVVQEENQHMQMTIQA-------LQDELRIQRDLNQLFQQDSSSRTGEpcvAELTEEN 115
Cdd:pfam15818  231 LNMELELNKKINEEITHIQEEKQDIIISFQHMQQLLQQqtqanteMEAELKALKENNQTLERDNELQREK---VKENEEK 307
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30017397    116 FQRLHAEHErqaKELFLLRKTLEEMELRIETQKQTLNARDESIKKLLEMlQSKGLSAKATEEDhERTRRLAE-----AEM 190
Cdd:pfam15818  308 FLNLQNEHE---KALGTWKKHVEELNGEINEIKNELSSLKETHIKLQEH-YNKLCNQKKFEED-KKFQNVPEvnnenSEM 382
                          170       180
                   ....*....|....*....|....*..
gi 30017397    191 HVHHLESLLEQKEKENNMLREEMHRRF 217
Cdd:pfam15818  383 STEKSENLIIQKYNSEQEIREENTKSF 409
 
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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