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Conserved domains on  [gi|19920317|ref|NP_006816|]
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cytoskeleton-associated protein 4 [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

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List of domain hits

Name Accession Description Interval E-value
Smc super family cl34174
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
146-550 1.49e-06

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


The actual alignment was detected with superfamily member COG1196:

Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 51.48  E-value: 1.49e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19920317 146 RQREELGQGLQGVEQKVQSLQATFGTFESILRSSQHKQDLTEKAVKQGESEVSRISEVLQKLQNEILKDLSDGIHVVKDA 225
Cdd:COG1196 225 LEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDI 304
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19920317 226 RERdfTSLENTVEERLTELTKSIndniaiftevqKRSQKEINDMKAKVASLEEsegnkqDLKALKEAVKEIQTSAKSREW 305
Cdd:COG1196 305 ARL--EERRRELEERLEELEEEL-----------AELEEELEELEEELEELEE------ELEEAEEELEEAEAELAEAEE 365
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19920317 306 DMEALRSTLQTMESDIYTEVRELVSLKQEQQAFKEAADTERLALQALTEKLLRSEESVSRLPEEIRRLEEELRQLKsdsh 385
Cdd:COG1196 366 ALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEE---- 441
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19920317 386 gpkedggfrhsEAFEALQQKSQGLDSRLQHVEDGVLSMQVASARQTESLESLLSKSQEHEQR---LAALQGRLEGLGSSE 462
Cdd:COG1196 442 -----------EALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARlllLLEAEADYEGFLEGV 510
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19920317 463 ADQDGLASTVRSLGETQLVL-----YGDVEELKRSVGELPSTVESLQKVQEQVHTLLSQDQAQAARLPPQDFLDRLSSLD 537
Cdd:COG1196 511 KAALLLAGLRGLAGAVAVLIgveaaYEAALEAALAAALQNIVVEDDEVAAAAIEYLKAAKAGRATFLPLDKIRARAALAA 590
                       410
                ....*....|...
gi 19920317 538 NLKASVSQVEADL 550
Cdd:COG1196 591 ALARGAIGAAVDL 603
 
Name Accession Description Interval E-value
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
146-550 1.49e-06

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 51.48  E-value: 1.49e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19920317 146 RQREELGQGLQGVEQKVQSLQATFGTFESILRSSQHKQDLTEKAVKQGESEVSRISEVLQKLQNEILKDLSDGIHVVKDA 225
Cdd:COG1196 225 LEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDI 304
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19920317 226 RERdfTSLENTVEERLTELTKSIndniaiftevqKRSQKEINDMKAKVASLEEsegnkqDLKALKEAVKEIQTSAKSREW 305
Cdd:COG1196 305 ARL--EERRRELEERLEELEEEL-----------AELEEELEELEEELEELEE------ELEEAEEELEEAEAELAEAEE 365
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19920317 306 DMEALRSTLQTMESDIYTEVRELVSLKQEQQAFKEAADTERLALQALTEKLLRSEESVSRLPEEIRRLEEELRQLKsdsh 385
Cdd:COG1196 366 ALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEE---- 441
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19920317 386 gpkedggfrhsEAFEALQQKSQGLDSRLQHVEDGVLSMQVASARQTESLESLLSKSQEHEQR---LAALQGRLEGLGSSE 462
Cdd:COG1196 442 -----------EALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARlllLLEAEADYEGFLEGV 510
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19920317 463 ADQDGLASTVRSLGETQLVL-----YGDVEELKRSVGELPSTVESLQKVQEQVHTLLSQDQAQAARLPPQDFLDRLSSLD 537
Cdd:COG1196 511 KAALLLAGLRGLAGAVAVLIgveaaYEAALEAALAAALQNIVVEDDEVAAAAIEYLKAAKAGRATFLPLDKIRARAALAA 590
                       410
                ....*....|...
gi 19920317 538 NLKASVSQVEADL 550
Cdd:COG1196 591 ALARGAIGAAVDL 603
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
130-509 4.56e-06

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: 50.07  E-value: 4.56e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19920317    130 VLEEVQQVRRSHQDFSRQREELGQGLQGVE------QKVQSLQATFGTFESILRSSQHKQDLTEKavKQGESEVSRISEV 203
Cdd:TIGR02169  175 ALEELEEVEENIERLDLIIDEKRQQLERLRrerekaERYQALLKEKREYEGYELLKEKEALERQK--EAIERQLASLEEE 252
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19920317    204 LQKLQNEIlKDLSDGIHVVKDARE------RDFTSLE-NTVEERLTELTKSI---NDNIAIFTEVQKRSQKEINDMKAKV 273
Cdd:TIGR02169  253 LEKLTEEI-SELEKRLEEIEQLLEelnkkiKDLGEEEqLRVKEKIGELEAEIaslERSIAEKERELEDAEERLAKLEAEI 331
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19920317    274 ----ASLEESEGNKQDLKALKEAVKEIqtsAKSREWDMEALRSTLQTMESDIYTEVRELVSLKQEqqafkeaadterlaL 349
Cdd:TIGR02169  332 dkllAEIEELEREIEEERKRRDKLTEE---YAELKEELEDLRAELEEVDKEFAETRDELKDYREK--------------L 394
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19920317    350 QALTEKLLRSEESVSRLpeeirrlEEELRQLksdshgpkedggfrhSEAFEALQQKSQGLDSRLQHVEDGVLSMQVASAR 429
Cdd:TIGR02169  395 EKLKREINELKRELDRL-------QEELQRL---------------SEELADLNAAIAGIEAKINELEEEKEDKALEIKK 452
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19920317    430 QTESLESLLSKSQEHEQRLAALQGRLEG----LGSSEADQDGLASTVRSLGETQLVLYGDVEELKRSVGELPSTVESLQK 505
Cdd:TIGR02169  453 QEWKLEQLAADLSKYEQELYDLKEEYDRvekeLSKLQRELAEAEAQARASEERVRGGRAVEEVLKASIQGVHGTVAQLGS 532

                   ....
gi 19920317    506 VQEQ 509
Cdd:TIGR02169  533 VGER 536
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
145-507 1.69e-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: 41.64  E-value: 1.69e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19920317    145 SRQREELGQGLQGVEQKVQSLQATFgtfesILRSSQHKQDLTEKavKQGESEVSRISEVLQKL----------------Q 208
Cdd:pfam15921  327 SQLRSELREAKRMYEDKIEELEKQL-----VLANSELTEARTER--DQFSQESGNLDDQLQKLladlhkrekelslekeQ 399
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19920317    209 NEILKDLSDGIHVVKDARERDFTSlENTVEERLTELTKSINDNIAIFTEVQKRSQKEINDMKAKVASL------------ 276
Cdd:pfam15921  400 NKRLWDRDTGNSITIDHLRRELDD-RNMEVQRLEALLKAMKSECQGQMERQMAAIQGKNESLEKVSSLtaqlestkemlr 478
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19920317    277 ---EESEGNKQDLKALKEAVKEIQTSAKSREWDMEALRSTLQTMESDIYTEVRELVSLKQEQQAFKEA-ADTERLALQaL 352
Cdd:pfam15921  479 kvvEELTAKKMTLESSERTVSDLTASLQEKERAIEATNAEITKLRSRVDLKLQELQHLKNEGDHLRNVqTECEALKLQ-M 557
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19920317    353 TEK-----LLRSE-ESVSRLPEEIRRLEEELRQLKSDSHGPKEDGGFRHSEaFEALQQKSqglDSRLQHVEDGVLSMQVA 426
Cdd:pfam15921  558 AEKdkvieILRQQiENMTQLVGQHGRTAGAMQVEKAQLEKEINDRRLELQE-FKILKDKK---DAKIRELEARVSDLELE 633
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19920317    427 SAR----QTESLESLLSKSQEHEQRLAALQGRLEGLGSSEADQDGLASTVRSLGETQLVLYGDVE-ELKRSVGELPSTVE 501
Cdd:pfam15921  634 KVKlvnaGSERLRAVKDIKQERDQLLNEVKTSRNELNSLSEDYEVLKRNFRNKSEEMETTTNKLKmQLKSAQSELEQTRN 713

                   ....*.
gi 19920317    502 SLQKVQ 507
Cdd:pfam15921  714 TLKSME 719
 
Name Accession Description Interval E-value
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
146-550 1.49e-06

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 51.48  E-value: 1.49e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19920317 146 RQREELGQGLQGVEQKVQSLQATFGTFESILRSSQHKQDLTEKAVKQGESEVSRISEVLQKLQNEILKDLSDGIHVVKDA 225
Cdd:COG1196 225 LEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDI 304
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19920317 226 RERdfTSLENTVEERLTELTKSIndniaiftevqKRSQKEINDMKAKVASLEEsegnkqDLKALKEAVKEIQTSAKSREW 305
Cdd:COG1196 305 ARL--EERRRELEERLEELEEEL-----------AELEEELEELEEELEELEE------ELEEAEEELEEAEAELAEAEE 365
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19920317 306 DMEALRSTLQTMESDIYTEVRELVSLKQEQQAFKEAADTERLALQALTEKLLRSEESVSRLPEEIRRLEEELRQLKsdsh 385
Cdd:COG1196 366 ALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEE---- 441
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19920317 386 gpkedggfrhsEAFEALQQKSQGLDSRLQHVEDGVLSMQVASARQTESLESLLSKSQEHEQR---LAALQGRLEGLGSSE 462
Cdd:COG1196 442 -----------EALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARlllLLEAEADYEGFLEGV 510
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19920317 463 ADQDGLASTVRSLGETQLVL-----YGDVEELKRSVGELPSTVESLQKVQEQVHTLLSQDQAQAARLPPQDFLDRLSSLD 537
Cdd:COG1196 511 KAALLLAGLRGLAGAVAVLIgveaaYEAALEAALAAALQNIVVEDDEVAAAAIEYLKAAKAGRATFLPLDKIRARAALAA 590
                       410
                ....*....|...
gi 19920317 538 NLKASVSQVEADL 550
Cdd:COG1196 591 ALARGAIGAAVDL 603
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
130-509 4.56e-06

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: 50.07  E-value: 4.56e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19920317    130 VLEEVQQVRRSHQDFSRQREELGQGLQGVE------QKVQSLQATFGTFESILRSSQHKQDLTEKavKQGESEVSRISEV 203
Cdd:TIGR02169  175 ALEELEEVEENIERLDLIIDEKRQQLERLRrerekaERYQALLKEKREYEGYELLKEKEALERQK--EAIERQLASLEEE 252
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19920317    204 LQKLQNEIlKDLSDGIHVVKDARE------RDFTSLE-NTVEERLTELTKSI---NDNIAIFTEVQKRSQKEINDMKAKV 273
Cdd:TIGR02169  253 LEKLTEEI-SELEKRLEEIEQLLEelnkkiKDLGEEEqLRVKEKIGELEAEIaslERSIAEKERELEDAEERLAKLEAEI 331
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19920317    274 ----ASLEESEGNKQDLKALKEAVKEIqtsAKSREWDMEALRSTLQTMESDIYTEVRELVSLKQEqqafkeaadterlaL 349
Cdd:TIGR02169  332 dkllAEIEELEREIEEERKRRDKLTEE---YAELKEELEDLRAELEEVDKEFAETRDELKDYREK--------------L 394
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19920317    350 QALTEKLLRSEESVSRLpeeirrlEEELRQLksdshgpkedggfrhSEAFEALQQKSQGLDSRLQHVEDGVLSMQVASAR 429
Cdd:TIGR02169  395 EKLKREINELKRELDRL-------QEELQRL---------------SEELADLNAAIAGIEAKINELEEEKEDKALEIKK 452
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19920317    430 QTESLESLLSKSQEHEQRLAALQGRLEG----LGSSEADQDGLASTVRSLGETQLVLYGDVEELKRSVGELPSTVESLQK 505
Cdd:TIGR02169  453 QEWKLEQLAADLSKYEQELYDLKEEYDRvekeLSKLQRELAEAEAQARASEERVRGGRAVEEVLKASIQGVHGTVAQLGS 532

                   ....
gi 19920317    506 VQEQ 509
Cdd:TIGR02169  533 VGER 536
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
146-394 1.28e-04

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: 44.75  E-value: 1.28e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19920317 146 RQREELGQGLQGVEQKVQSLQATFGTFESILRSSQHKQDLTEKAVKQGESEVSRISEVLQKLQNEIlkdlsdgihvvkDA 225
Cdd:COG4942  27 AELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEI------------AE 94
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19920317 226 RERDFTSLENTVEERLTELTK-SINDNIAIFTevqkrSQKEINDMKAKVASLEE-SEGNKQDLKALKEAVKEIQTSAKsr 303
Cdd:COG4942  95 LRAELEAQKEELAELLRALYRlGRQPPLALLL-----SPEDFLDAVRRLQYLKYlAPARREQAEELRADLAELAALRA-- 167
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19920317 304 ewDMEALRSTLQTMESDIYTEVRELVSLKQEQQAFKEAADTERLALQALTEKLLRSEESVSRLPEEIRRLEEELRQLKSD 383
Cdd:COG4942 168 --ELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPA 245
                       250
                ....*....|.
gi 19920317 384 SHGPKEDGGFR 394
Cdd:COG4942 246 AGFAALKGKLP 256
235kDa-fam TIGR01612
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ...
146-320 2.27e-04

reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in plasmodium species alternately annotated as reticulocyte binding protein, 235-kDa family protein and rhoptry protein. Rhoptry protein is localized on the cell surface and is extremely large (although apparently lacking in repeat structure) and is important for the process of invasion of the RBCs by the parasite. These proteins are found in P. falciparum, P. vivax and P. yoelii.


Pssm-ID: 130673 [Multi-domain]  Cd Length: 2757  Bit Score: 44.66  E-value: 2.27e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19920317    146 RQREELGQGLQGVEQKVQSLQATFGTFESILRSS-------------QHKQDLTEKAVKQGESEVSRISEVLQKLQneiL 212
Cdd:TIGR01612 1019 HQFDEKEKATNDIEQKIEDANKNIPNIEIAIHTSiyniideiekeigKNIELLNKEILEEAEINITNFNEIKEKLK---H 1095
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19920317    213 KDLSDgihVVKDARERdFTSLENTVEERLTELTKSINDNIAIFTEVQKRSQKEINDMKAKVASLEESEGN---KQDLKAL 289
Cdd:TIGR01612 1096 YNFDD---FGKEENIK-YADEINKIKDDIKNLDQKIDHHIKALEEIKKKSENYIDEIKAQINDLEDVADKaisNDDPEEI 1171
                          170       180       190
                   ....*....|....*....|....*....|....
gi 19920317    290 KEAVKEIQTSAKSREW---DMEALRSTLQTMESD 320
Cdd:TIGR01612 1172 EKKIENIVTKIDKKKNiydEIKKLLNEIAEIEKD 1205
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
263-553 1.04e-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: 1.04e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19920317    263 QKEINDMKAKVASLE-ESEGNKQDLKALKEAVKEIQTSAKSREWDMEALRSTLQTMESDIYTEVRELVSLKQEQQAFKEA 341
Cdd:TIGR02169  687 KRELSSLQSELRRIEnRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEAR 766
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19920317    342 ADTERLALQALTEKL--LRSEESVSRLPEEIRRLEEELRQLKsdshgpKEDGGFRHSEA-FEALQQKSQGLDSRLQHVED 418
Cdd:TIGR02169  767 IEELEEDLHKLEEALndLEARLSHSRIPEIQAELSKLEEEVS------RIEARLREIEQkLNRLTLEKEYLEKEIQELQE 840
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19920317    419 GV--LSMQVASARQTES-----LESLLSKSQEHEQRLAALQGRLEGLgssEADQDGLASTVRSLGETQLVLYGDVEELKR 491
Cdd:TIGR02169  841 QRidLKEQIKSIEKEIEnlngkKEELEEELEELEAALRDLESRLGDL---KKERDELEAQLRELERKIEELEAQIEKKRK 917
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 19920317    492 SVGELPSTVESLQKVQEQVHTLLSQDQAQAARLPpqdfldrlsSLDNLKASVSQVEADLKML 553
Cdd:TIGR02169  918 RLSELKAKLEALEEELSEIEDPKGEDEEIPEEEL---------SLEDVQAELQRVEEEIRAL 970
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
145-507 1.69e-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: 41.64  E-value: 1.69e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19920317    145 SRQREELGQGLQGVEQKVQSLQATFgtfesILRSSQHKQDLTEKavKQGESEVSRISEVLQKL----------------Q 208
Cdd:pfam15921  327 SQLRSELREAKRMYEDKIEELEKQL-----VLANSELTEARTER--DQFSQESGNLDDQLQKLladlhkrekelslekeQ 399
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19920317    209 NEILKDLSDGIHVVKDARERDFTSlENTVEERLTELTKSINDNIAIFTEVQKRSQKEINDMKAKVASL------------ 276
Cdd:pfam15921  400 NKRLWDRDTGNSITIDHLRRELDD-RNMEVQRLEALLKAMKSECQGQMERQMAAIQGKNESLEKVSSLtaqlestkemlr 478
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19920317    277 ---EESEGNKQDLKALKEAVKEIQTSAKSREWDMEALRSTLQTMESDIYTEVRELVSLKQEQQAFKEA-ADTERLALQaL 352
Cdd:pfam15921  479 kvvEELTAKKMTLESSERTVSDLTASLQEKERAIEATNAEITKLRSRVDLKLQELQHLKNEGDHLRNVqTECEALKLQ-M 557
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19920317    353 TEK-----LLRSE-ESVSRLPEEIRRLEEELRQLKSDSHGPKEDGGFRHSEaFEALQQKSqglDSRLQHVEDGVLSMQVA 426
Cdd:pfam15921  558 AEKdkvieILRQQiENMTQLVGQHGRTAGAMQVEKAQLEKEINDRRLELQE-FKILKDKK---DAKIRELEARVSDLELE 633
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19920317    427 SAR----QTESLESLLSKSQEHEQRLAALQGRLEGLGSSEADQDGLASTVRSLGETQLVLYGDVE-ELKRSVGELPSTVE 501
Cdd:pfam15921  634 KVKlvnaGSERLRAVKDIKQERDQLLNEVKTSRNELNSLSEDYEVLKRNFRNKSEEMETTTNKLKmQLKSAQSELEQTRN 713

                   ....*.
gi 19920317    502 SLQKVQ 507
Cdd:pfam15921  714 TLKSME 719
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
149-486 2.01e-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: 41.20  E-value: 2.01e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19920317    149 EELGQGLQGVEQKVQSLQATFGTFESILRSSQHKQDLTEKAVKQGESEVSRISEVLQKLQNEIlKDLSDGIHVVKDARER 228
Cdd:TIGR02168  235 EELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEI-SRLEQQKQILRERLAN 313
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19920317    229 DFTSLENTVEERLTELTKSINDniaiftevqkrsQKEINDMKAKVASLEEsegNKQDLKALkeavkeiqtsAKSREWDME 308
Cdd:TIGR02168  314 LERQLEELEAQLEELESKLDEL------------AEELAELEEKLEELKE---ELESLEAE----------LEELEAELE 368
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19920317    309 ALRSTLQTMESDIYTEVRELVSLKQEQQAfkeaadtERLALQALTEKLLRSEESVSRLPEEIRRLEEElrqlksdshgpk 388
Cdd:TIGR02168  369 ELESRLEELEEQLETLRSKVAQLELQIAS-------LNNEIERLEARLERLEDRRERLQQEIEELLKK------------ 429
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19920317    389 edggfRHSEAFEALQQKSQGLDSRLQHVEDGVLSMQVASARQTESLESLLSKSQEHEQRLAALQGRLEGLGSSEADQDGL 468
Cdd:TIGR02168  430 -----LEEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLEGF 504
                          330
                   ....*....|....*...
gi 19920317    469 ASTVRSLGETQLVLYGDV 486
Cdd:TIGR02168  505 SEGVKALLKNQSGLSGIL 522
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
131-521 2.04e-03

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 41.29  E-value: 2.04e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19920317 131 LEEVQQVRRSHQDFSRQREELGQGLQGVEQKVQSLQATFGTFESILRSSQHKQDLTE--KAVKQGESEVSRISEVLQKLQ 208
Cdd:COG4717  73 LKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPlyQELEALEAELAELPERLEELE 152
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19920317 209 NEI---------LKDLSDGIHVVKDARERDFTSLENTVEERLTELTKSIND---NIAIFTEVQKRSQKEINDMKAKVASL 276
Cdd:COG4717 153 ERLeelreleeeLEELEAELAELQEELEELLEQLSLATEEELQDLAEELEElqqRLAELEEELEEAQEELEELEEELEQL 232
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19920317 277 EESEGNKQDLKALKEA-------------VKEIQTSAKSREWDMEALRSTLQTMESDIYTEVRELVSLKQEQQAFKEAAD 343
Cdd:COG4717 233 ENELEAAALEERLKEArlllliaaallalLGLGGSLLSLILTIAGVLFLVLGLLALLFLLLAREKASLGKEAEELQALPA 312
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19920317 344 TERLALQALTEKLLRSEESVSRLPEEIRRLEEELRQLKSdshgpkedggfRHSEAFEALQQKSqgLDSRLQHVEDGVLSM 423
Cdd:COG4717 313 LEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQE-----------LLREAEELEEELQ--LEELEQEIAALLAEA 379
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19920317 424 QVASARQTESLESLLSKSQEHEQRLAALQGRLEGLGSSE------ADQDGLASTVRSLGETQLVLYGDVEELKRSVGELP 497
Cdd:COG4717 380 GVEDEEELRAALEQAEEYQELKEELEELEEQLEELLGELeelleaLDEEELEEELEELEEELEELEEELEELREELAELE 459
                       410       420
                ....*....|....*....|....
gi 19920317 498 STVESLQKVQEQVHTLLSQDQAQA 521
Cdd:COG4717 460 AELEQLEEDGELAELLQELEELKA 483
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
132-366 2.40e-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: 41.20  E-value: 2.40e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19920317    132 EEVQQVRRSHQDFSRQREELGQGLQGVEQKVQSLQATFGTFESILRSSQHKQDLTEKAVKQGESEVSRISEVLQKLQNEI 211
Cdd:TIGR02168  239 EELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQL 318
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19920317    212 lKDLSDGIHVVKDARERDFTSLeNTVEERLTELTKSINDNIAIFTEVQKRSQ----------KEINDMKAKVASLEESEG 281
Cdd:TIGR02168  319 -EELEAQLEELESKLDELAEEL-AELEEKLEELKEELESLEAELEELEAELEelesrleeleEQLETLRSKVAQLELQIA 396
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19920317    282 --------NKQDLKALKEAVKeiQTSAKSREWDMEALRSTLQTMESDIYTEVRELVSLKQEQQAFKEAADTERLALQALT 353
Cdd:TIGR02168  397 slnneierLEARLERLEDRRE--RLQQEIEELLKKLEEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAE 474
                          250
                   ....*....|...
gi 19920317    354 EKLLRSEESVSRL 366
Cdd:TIGR02168  475 QALDAAERELAQL 487
 
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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