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Conserved domains on  [gi|2066300676|ref|NP_001382425|]
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testis-expressed protein 9 isoform 1 [Homo sapiens]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
SMC_prok_B super family cl37069
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
190-348 1.80e-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]


The actual alignment was detected with superfamily member TIGR02168:

Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 56.60  E-value: 1.80e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066300676  190 TEAQIRFLKAKLHVMQEELDNVVCECNKKEDEIQNLKSQVKNFEEDFMRQQRTINMQQSQVEKYKTLFEEANKKYDGLQQ 269
Cdd:TIGR02168  272 LRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKE 351
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2066300676  270 QLSSVERELENKRRLQKQAASSQSATEVRLNRAleeAEKYKLELSKLRQNNKDIANEEhKKIEVLKSENKKLEKQKGEL 348
Cdd:TIGR02168  352 ELESLEAELEELEAELEELESRLEELEEQLETL---RSKVAQLELQIASLNNEIERLE-ARLERLEDRRERLQQEIEEL 426
 
Name Accession Description Interval E-value
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
190-348 1.80e-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: 56.60  E-value: 1.80e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066300676  190 TEAQIRFLKAKLHVMQEELDNVVCECNKKEDEIQNLKSQVKNFEEDFMRQQRTINMQQSQVEKYKTLFEEANKKYDGLQQ 269
Cdd:TIGR02168  272 LRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKE 351
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2066300676  270 QLSSVERELENKRRLQKQAASSQSATEVRLNRAleeAEKYKLELSKLRQNNKDIANEEhKKIEVLKSENKKLEKQKGEL 348
Cdd:TIGR02168  352 ELESLEAELEELEAELEELESRLEELEEQLETL---RSKVAQLELQIASLNNEIERLE-ARLERLEDRRERLQQEIEEL 426
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
191-348 9.00e-05

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 44.54  E-value: 9.00e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066300676 191 EAQIRFLKAKLHVMQEELdnvvcecNKKEDEIQNLKSQVKNFEEDFMRQQRTINMQQSQVEKYKTLFEEANKKYDGLQQQ 270
Cdd:COG1196   266 EAELEELRLELEELELEL-------EEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEE 338
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2066300676 271 LSSVERELENKRRLQKQAASSQSATEVRLNRALEEAEKYKLELSKLRQNNKDIANEEHKKIEVLKSENKKLEKQKGEL 348
Cdd:COG1196   339 LEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERL 416
PRK12704 PRK12704
phosphodiesterase; Provisional
191-330 4.35e-04

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 42.07  E-value: 4.35e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066300676 191 EAQIRFLKAKlhvmqEELDNvvcECNKKEDEIQNLKSQVKNFEEDFMRQQRTINMQQSQVEKYKtlfeeanKKYDGLQQQ 270
Cdd:PRK12704   61 EAKEEIHKLR-----NEFEK---ELRERRNELQKLEKRLLQKEENLDRKLELLEKREEELEKKE-------KELEQKQQE 125
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2066300676 271 LSSVERELENKRRLQKQA---ASSQSATEVRlNRALEEAE-KYKLELSKLRQNNKDIANEEHKK 330
Cdd:PRK12704  126 LEKKEEELEELIEEQLQElerISGLTAEEAK-EILLEKVEeEARHEAAVLIKEIEEEAKEEADK 188
Spc7 smart00787
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ...
197-282 5.59e-03

Spc7 kinetochore protein; This domain is found in cell division proteins which are required for kinetochore-spindle association.


Pssm-ID: 197874 [Multi-domain]  Cd Length: 312  Bit Score: 38.46  E-value: 5.59e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066300676  197 LKAKLHVMQEELD---NVVCECNK-KEDEIQNLKSQVKNFEEDFMRQQRTINMQQSQVEKYKTLFEEANKKYDGLQQQLS 272
Cdd:smart00787 177 LRDRKDALEEELRqlkQLEDELEDcDPTELDRAKEKLKKLLQEIMIKVKKLEELEEELQELESKIEDLTNKKSELNTEIA 256
                           90
                   ....*....|
gi 2066300676  273 SVERELENKR 282
Cdd:smart00787 257 EAEKKLEQCR 266
 
Name Accession Description Interval E-value
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
190-348 1.80e-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: 56.60  E-value: 1.80e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066300676  190 TEAQIRFLKAKLHVMQEELDNVVCECNKKEDEIQNLKSQVKNFEEDFMRQQRTINMQQSQVEKYKTLFEEANKKYDGLQQ 269
Cdd:TIGR02168  272 LRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKE 351
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2066300676  270 QLSSVERELENKRRLQKQAASSQSATEVRLNRAleeAEKYKLELSKLRQNNKDIANEEhKKIEVLKSENKKLEKQKGEL 348
Cdd:TIGR02168  352 ELESLEAELEELEAELEELESRLEELEEQLETL---RSKVAQLELQIASLNNEIERLE-ARLERLEDRRERLQQEIEEL 426
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
155-348 5.09e-06

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: 48.90  E-value: 5.09e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066300676  155 FSLAKTISKIEGQLEEeglpeyIDDIFSGVSNDIG-TEAQIRFLKAKLHVMQEELdnvvcecNKKEDEIQNLKSQVKNFE 233
Cdd:TIGR02168  291 YALANEISRLEQQKQI------LRERLANLERQLEeLEAQLEELESKLDELAEEL-------AELEEKLEELKEELESLE 357
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066300676  234 EDFMRQQRTINMQQSQVEKYKTLFEEANKKYDGLQQQLSSVERELENKRRLQKQAASSQSATEVRLNRALEEAEkyKLEL 313
Cdd:TIGR02168  358 AELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLE--EAEL 435
                          170       180       190
                   ....*....|....*....|....*....|....*
gi 2066300676  314 SKLRQNNKDIANEEHKKIEVLKSENKKLEKQKGEL 348
Cdd:TIGR02168  436 KELQAELEELEEELEELQEELERLEEALEELREEL 470
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
190-374 8.92e-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: 8.92e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066300676  190 TEAQIRFLKAKLHVMQEELDNVVCECNKKEDEIQNLKSQVKNFEEDFMRQ-QRTINMQQSQVEKYKTLFEEANKKYDGLQ 268
Cdd:TIGR02169  242 IERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQLRvKEKIGELEAEIASLERSIAEKERELEDAE 321
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066300676  269 QQLSSVERELENKRRLQKQAASSQSATEVRLNRALEEAEKYKLELSKLRQNNKDIANEEHKKIEVLKSENKKLEKQKGEL 348
Cdd:TIGR02169  322 ERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREI 401
                          170       180
                   ....*....|....*....|....*.
gi 2066300676  349 MIGFKKQLKLIDVLKRQKMHIEAAKM 374
Cdd:TIGR02169  402 NELKRELDRLQEELQRLSEELADLNA 427
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
191-348 9.00e-05

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 44.54  E-value: 9.00e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066300676 191 EAQIRFLKAKLHVMQEELdnvvcecNKKEDEIQNLKSQVKNFEEDFMRQQRTINMQQSQVEKYKTLFEEANKKYDGLQQQ 270
Cdd:COG1196   266 EAELEELRLELEELELEL-------EEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEE 338
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2066300676 271 LSSVERELENKRRLQKQAASSQSATEVRLNRALEEAEKYKLELSKLRQNNKDIANEEHKKIEVLKSENKKLEKQKGEL 348
Cdd:COG1196   339 LEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERL 416
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
192-366 1.69e-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: 43.21  E-value: 1.69e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066300676 192 AQIRFLKAKLHVMQEELDNVVCECNKKEDEIQNLKSQVKNFEEDFMRQQRTINMQQSQVEKYKTLFEEANKKYDGLQQQL 271
Cdd:COG4942    20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAEL 99
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066300676 272 SSVERELenKRRLQK-QAASSQSATEVRLN-RALEEAEKYKLELSKLRQNNKDIANEEHKKIEVLKSENKKLEKQKGELM 349
Cdd:COG4942   100 EAQKEEL--AELLRAlYRLGRQPPLALLLSpEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELE 177
                         170
                  ....*....|....*..
gi 2066300676 350 IGFKKQLKLIDVLKRQK 366
Cdd:COG4942   178 ALLAELEEERAALEALK 194
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
190-344 1.71e-04

Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 43.28  E-value: 1.71e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066300676 190 TEAQIRFLKAKLHVMQEELDNVVCECNKKEDEIQNLKSQVKNFEEDFMRQQRTINMQQSQVEK-----YKTL-------- 256
Cdd:COG3883    28 LQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGEraralYRSGgsvsyldv 107
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066300676 257 ------FEEANKKYDGLQQ----------QLSSVERELENKRRLQKQAASSQSATEVRLNRALEEAEKYKLELSKLRQNN 320
Cdd:COG3883   108 llgsesFSDFLDRLSALSKiadadadlleELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQL 187
                         170       180
                  ....*....|....*....|....
gi 2066300676 321 KDIANEEHKKIEVLKSENKKLEKQ 344
Cdd:COG3883   188 SAEEAAAEAQLAELEAELAAAEAA 211
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
217-373 1.82e-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: 43.21  E-value: 1.82e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066300676 217 KKEDEIQNLKSQVKNFEEDFMRQQRTINMQQSQVEKYKTLFEEANKKYDGLQQQLSSVERELENKRRLQKQAASSQSATE 296
Cdd:COG4942    24 EAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQK 103
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066300676 297 VRLNRALEEAEKYK--------------LELSKLRQNNKDIANEEHKKIEVLKSENKKLEKQKGELMIGFKKQLKLIDVL 362
Cdd:COG4942   104 EELAELLRALYRLGrqpplalllspedfLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAEL 183
                         170
                  ....*....|.
gi 2066300676 363 KRQKMHIEAAK 373
Cdd:COG4942   184 EEERAALEALK 194
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
191-373 2.83e-04

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 43.00  E-value: 2.83e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066300676 191 EAQIRFLKAKLHVMQEELDnvvcecnKKEDEIQNLKSQVKNFEEDFMRQQRTINMQQSQVEKYKTLFEEANKKYDGLQQQ 270
Cdd:COG1196   224 ELEAELLLLKLRELEAELE-------ELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAE 296
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066300676 271 LSSVERELENKRRLQKQAASSQSATEVRLNRALEEAEKYKLELSKLRQNNKDIANEEHKKIEVLKSENKKLEKQKGELmi 350
Cdd:COG1196   297 LARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAEL-- 374
                         170       180
                  ....*....|....*....|...
gi 2066300676 351 gfKKQLKLIDVLKRQKMHIEAAK 373
Cdd:COG1196   375 --AEAEEELEELAEELLEALRAA 395
PRK12704 PRK12704
phosphodiesterase; Provisional
191-330 4.35e-04

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 42.07  E-value: 4.35e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066300676 191 EAQIRFLKAKlhvmqEELDNvvcECNKKEDEIQNLKSQVKNFEEDFMRQQRTINMQQSQVEKYKtlfeeanKKYDGLQQQ 270
Cdd:PRK12704   61 EAKEEIHKLR-----NEFEK---ELRERRNELQKLEKRLLQKEENLDRKLELLEKREEELEKKE-------KELEQKQQE 125
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2066300676 271 LSSVERELENKRRLQKQA---ASSQSATEVRlNRALEEAE-KYKLELSKLRQNNKDIANEEHKK 330
Cdd:PRK12704  126 LEKKEEELEELIEEQLQElerISGLTAEEAK-EILLEKVEeEARHEAAVLIKEIEEEAKEEADK 188
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
221-360 6.68e-04

Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];


Pssm-ID: 441187 [Multi-domain]  Cd Length: 236  Bit Score: 40.68  E-value: 6.68e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066300676 221 EIQNLKSQVKNFEEDFMRQQRTINMQQSQVEKYKTLFEEANKKYDGLQQQLSSV--ERELENkrrLQKQ---AASSQSAT 295
Cdd:COG1579    32 ELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVrnNKEYEA---LQKEiesLKRRISDL 108
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2066300676 296 EVRLNRALEEAEKYKLELSKLRQNNKDIANEEHKKIEVLKSENKKLEKQKGELMIGFKKQLKLID 360
Cdd:COG1579   109 EDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAEREELAAKIP 173
PRK00409 PRK00409
recombination and DNA strand exchange inhibitor protein; Reviewed
258-373 8.92e-04

recombination and DNA strand exchange inhibitor protein; Reviewed


Pssm-ID: 234750 [Multi-domain]  Cd Length: 782  Bit Score: 41.35  E-value: 8.92e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066300676 258 EEANKKYDGLQQQLSSVERELENKRRLQKQAASsqsatevRLNRALEEAEKYKLELSKLRQNNKDIANEE--------HK 329
Cdd:PRK00409  505 EEAKKLIGEDKEKLNELIASLEELERELEQKAE-------EAEALLKEAEKLKEELEEKKEKLQEEEDKLleeaekeaQQ 577
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 2066300676 330 KIEVLKSENKKLEKQKGELMIGFKKQLK---LIDVLKRQKMHIEAAK 373
Cdd:PRK00409  578 AIKEAKKEADEIIKELRQLQKGGYASVKaheLIEARKRLNKANEKKE 624
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
193-348 9.66e-04

helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.


Pssm-ID: 275316 [Multi-domain]  Cd Length: 745  Bit Score: 41.16  E-value: 9.66e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066300676 193 QIRFLKAKLHVMQEELDNVVCECNKKEDEIQNLKSQVKNFEEDFMRQQRTINMQQSQVEKYKTLFEEANKKYDGLQQQLS 272
Cdd:TIGR04523 315 ELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQIN 394
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2066300676 273 SVERELENKRRLQKQAASSQSATEVRLNRALEEAEKYKLELSKLRQNNKDIANEEHKKIEVLKSENKKLEKQKGEL 348
Cdd:TIGR04523 395 DLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQL 470
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
219-355 2.14e-03

Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 40.28  E-value: 2.14e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066300676  219 EDEIQNLKSQVKNFEEDfmrqQRTINMQQSQVEKYKTLFEEANKKYDGLQQQLSSVERELENKRRLQKQAASSQSATEVR 298
Cdd:COG4913    667 EREIAELEAELERLDAS----SDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDL 742
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 2066300676  299 LNRAL-EEAEKYKLELSkLRQNNKDIANEEHKKIEVLKSENKKLEKQKGELMIGFKKQ 355
Cdd:COG4913    743 ARLELrALLEERFAAAL-GDAVERELRENLEERIDALRARLNRAEEELERAMRAFNRE 799
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
192-365 2.66e-03

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 39.92  E-value: 2.66e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066300676 192 AQIRFLKAKLHVMQEELDNVVCECNKKEDEIQNLKSQVKNFEEDFMRQQRTINMQQSQVEKYKTLFEEANKKYDGLQQQL 271
Cdd:COG1196   232 LKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERR 311
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066300676 272 SSVER---ELENKRRLQKQAASSQSATEVRLNRALEEAEKYKLELSKLRQNNKDIANEEHKKIEVLKSENKKLEKQKGEL 348
Cdd:COG1196   312 RELEErleELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEA 391
                         170
                  ....*....|....*..
gi 2066300676 349 MIGFKKQLKLIDVLKRQ 365
Cdd:COG1196   392 LRAAAELAAQLEELEEA 408
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
250-371 4.16e-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: 39.27  E-value: 4.16e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066300676  250 VEKYKTLFEEANKKYDGLQQQLSSVE---RELE-NKRRLQKQAASSQSATEV--------------RLNRALEEAEKYKL 311
Cdd:TIGR02168  167 ISKYKERRKETERKLERTRENLDRLEdilNELErQLKSLERQAEKAERYKELkaelrelelallvlRLEELREELEELQE 246
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2066300676  312 ELSKLRQNNKDIA---NEEHKKIEVLKSENKKLEKQKGELMIGFKKQLKLIDVLKRQKMHIEA 371
Cdd:TIGR02168  247 ELKEAEEELEELTaelQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRE 309
Spc7 smart00787
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ...
197-282 5.59e-03

Spc7 kinetochore protein; This domain is found in cell division proteins which are required for kinetochore-spindle association.


Pssm-ID: 197874 [Multi-domain]  Cd Length: 312  Bit Score: 38.46  E-value: 5.59e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066300676  197 LKAKLHVMQEELD---NVVCECNK-KEDEIQNLKSQVKNFEEDFMRQQRTINMQQSQVEKYKTLFEEANKKYDGLQQQLS 272
Cdd:smart00787 177 LRDRKDALEEELRqlkQLEDELEDcDPTELDRAKEKLKKLLQEIMIKVKKLEELEEELQELESKIEDLTNKKSELNTEIA 256
                           90
                   ....*....|
gi 2066300676  273 SVERELENKR 282
Cdd:smart00787 257 EAEKKLEQCR 266
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
182-343 6.68e-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: 38.90  E-value: 6.68e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066300676  182 SGVSNDIGTEAQIRFLKAKLHVMQEELDNVVCECNKKEDEIQNLKSQVKNFEEDFMRQQRTINMQQSQVEKYKTLFEEan 261
Cdd:TIGR02169  664 GGILFSRSEPAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEE-- 741
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066300676  262 kkydgLQQQLSSVERELENKRrlqkqaaSSQSATEVRLNRALEEAEKYKLELSKLR-----------QNNKDIANEEHKK 330
Cdd:TIGR02169  742 -----LEEDLSSLEQEIENVK-------SELKELEARIEELEEDLHKLEEALNDLEarlshsripeiQAELSKLEEEVSR 809
                          170
                   ....*....|....
gi 2066300676  331 IE-VLKSENKKLEK 343
Cdd:TIGR02169  810 IEaRLREIEQKLNR 823
 
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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