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Conserved domains on  [gi|2462631416|ref|XP_054183992|]
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centriole and centriolar satellite protein OFD1 isoform X16 [Homo sapiens]

Protein Classification

kinesin family protein; PEPP family PH domain-containing protein( domain architecture ID 13870895)

kinesin family protein is a microtubule-dependent molecular motor that plays an important role in intracellular transport and in cell division and has an ATPase-containing motor domain; similar to N-type kinesins that are (+) end-directed motors and have an N-terminal motor domain| PEPP (phosphoinositol 3-phosphate-binding protein) family PH (pleckstrin homology) domain-containing protein similar to PH domain region of vertebrate pleckstrin homology domain-containing family A member 4/5/6/7

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
LisH_2 pfam16045
LisH;
75-101 9.29e-11

LisH;


:

Pssm-ID: 464992  Cd Length: 28  Bit Score: 57.09  E-value: 9.29e-11
                          10        20
                  ....*....|....*....|....*..
gi 2462631416  75 NSLVADHLQRCGYEYSLSVFFPESGLA 101
Cdd:pfam16045   2 NSLIAEYLQSQGYNYTLSVFLPESGLA 28
Smc super family cl34174
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
205-516 8.80e-10

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: 62.26  E-value: 8.80e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462631416 205 REIEEQLRaemcqKLKffKDTEIAK----IKMEAKKkYEKELTMFQNDFEKACQAKSEALVLREKSTLERIHKHQEIETK 280
Cdd:COG1196   196 GELERQLE-----PLE--RQAEKAEryreLKEELKE-LEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEA 267
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462631416 281 EIYAQRQLLL---KDMDLLRGREAELKQRVEAFE---LYQLELKDDYIIRTNRLIEDERKNKEKAVHLQEELIAINSKKE 354
Cdd:COG1196   268 ELEELRLELEeleLELEEAQAEEYELLAELARLEqdiARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELE 347
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462631416 355 ELNQsvnRVKELELELESVKAQSLAITKQnhmLNEKVKEMSDYSLLKEEKLELLAQNKLLKQQLEESRNENLRLLNRLAQ 434
Cdd:COG1196   348 EAEE---ELEEAEAELAEAEEALLEAEAE---LAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEE 421
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462631416 435 papELAVFQKELRKAEKAIVVEHEEFESCRQALHKQLQDEIEH---SAQLKAQILGYKASVKSLTTQVADLKLQLKQTQT 511
Cdd:COG1196   422 ---ELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALlelLAELLEEAALLEAALAELLEELAEAAARLLLLLE 498

                  ....*
gi 2462631416 512 ALENE 516
Cdd:COG1196   499 AEADY 503
 
Name Accession Description Interval E-value
LisH_2 pfam16045
LisH;
75-101 9.29e-11

LisH;


Pssm-ID: 464992  Cd Length: 28  Bit Score: 57.09  E-value: 9.29e-11
                          10        20
                  ....*....|....*....|....*..
gi 2462631416  75 NSLVADHLQRCGYEYSLSVFFPESGLA 101
Cdd:pfam16045   2 NSLIAEYLQSQGYNYTLSVFLPESGLA 28
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
205-516 8.80e-10

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 62.26  E-value: 8.80e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462631416 205 REIEEQLRaemcqKLKffKDTEIAK----IKMEAKKkYEKELTMFQNDFEKACQAKSEALVLREKSTLERIHKHQEIETK 280
Cdd:COG1196   196 GELERQLE-----PLE--RQAEKAEryreLKEELKE-LEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEA 267
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462631416 281 EIYAQRQLLL---KDMDLLRGREAELKQRVEAFE---LYQLELKDDYIIRTNRLIEDERKNKEKAVHLQEELIAINSKKE 354
Cdd:COG1196   268 ELEELRLELEeleLELEEAQAEEYELLAELARLEqdiARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELE 347
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462631416 355 ELNQsvnRVKELELELESVKAQSLAITKQnhmLNEKVKEMSDYSLLKEEKLELLAQNKLLKQQLEESRNENLRLLNRLAQ 434
Cdd:COG1196   348 EAEE---ELEEAEAELAEAEEALLEAEAE---LAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEE 421
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462631416 435 papELAVFQKELRKAEKAIVVEHEEFESCRQALHKQLQDEIEH---SAQLKAQILGYKASVKSLTTQVADLKLQLKQTQT 511
Cdd:COG1196   422 ---ELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALlelLAELLEEAALLEAALAELLEELAEAAARLLLLLE 498

                  ....*
gi 2462631416 512 ALENE 516
Cdd:COG1196   499 AEADY 503
PTZ00121 PTZ00121
MAEBL; Provisional
199-482 3.31e-06

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 50.91  E-value: 3.31e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462631416  199 KLNEYKREIEEQLRA-EMCQKLKFFKDTEIAKIKMEAKKKYEkELTMFQNDFEKACQAKSEALVLREKStlERIHKHQEI 277
Cdd:PTZ00121  1432 KADEAKKKAEEAKKAdEAKKKAEEAKKAEEAKKKAEEAKKAD-EAKKKAEEAKKADEAKKKAEEAKKKA--DEAKKAAEA 1508
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462631416  278 ETKEIYAQRQLLLKDMDLLRgrEAELKQRVEAFELYQLELKDDYIIRTNRLIEDERKNK-EKAVHLQEELIAINSKKEEL 356
Cdd:PTZ00121  1509 KKKADEAKKAEEAKKADEAK--KAEEAKKADEAKKAEEKKKADELKKAEELKKAEEKKKaEEAKKAEEDKNMALRKAEEA 1586
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462631416  357 NQS----VNRVKELELELESVKAQSLAITKQNHMLNEKVKEMSDYSLLKEEKLELLAQNKLLKQQLEESRNENLRLLNRL 432
Cdd:PTZ00121  1587 KKAeearIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEE 1666
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 2462631416  433 AQPAPELAVFQKELRKAE----KAIVVEHEEFESCRQA--LHKQLQDEIEHSAQLK 482
Cdd:PTZ00121  1667 AKKAEEDKKKAEEAKKAEedekKAAEALKKEAEEAKKAeeLKKKEAEEKKKAEELK 1722
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
196-514 1.89e-05

chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 48.53  E-value: 1.89e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462631416  196 LEIKLNEYKREIEEQLRAEMCQKLKFFKDTEIAKIKMEAKKKYEKELTMFQNDFEKACQAKsealvlrEKSTLERIHKHQ 275
Cdd:TIGR02169  193 IDEKRQQLERLRREREKAERYQALLKEKREYEGYELLKEKEALERQKEAIERQLASLEEEL-------EKLTEEISELEK 265
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462631416  276 EIETKEIyAQRQLLLKDMDLLRGREAELKQRVEAFELYqlelkddyIIRTNRLIEDERKNKEKAVHLQEELIA-INSKKE 354
Cdd:TIGR02169  266 RLEEIEQ-LLEELNKKIKDLGEEEQLRVKEKIGELEAE--------IASLERSIAEKERELEDAEERLAKLEAeIDKLLA 336
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462631416  355 ELNQSVNRVKELELELESVKAqslAITKQNHMLNEKVKEMSDYSLLKEEKLELLAQNKLLKQQLEESRNENLRLLNRLAQ 434
Cdd:TIGR02169  337 EIEELEREIEEERKRRDKLTE---EYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQE 413
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462631416  435 PAPELAVFQKELRKAEKAIVVEHEEFESCRQALHKQLQDEIEHSAQLKAQILGYKASVKSLTTQVADLKLQLKQTQTALE 514
Cdd:TIGR02169  414 ELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELA 493
SMC_N pfam02463
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...
191-516 8.19e-03

RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.


Pssm-ID: 426784 [Multi-domain]  Cd Length: 1161  Bit Score: 39.95  E-value: 8.19e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462631416  191 IKFESLEIKLNEYKREIEEQLRAEMCQKLKFFKDTEIAKIKMEAKKKYEKELTMFQNDFEKACQAKSEALVLREKSTLEr 270
Cdd:pfam02463  158 IEEEAAGSRLKRKKKEALKKLIEETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEYLLYLDYLKLNE- 236
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462631416  271 ihKHQEIETKEIYAQRQLLLKDMDLLRgREAELKQRVEAFELYQLELKDDYIIRTNRLIEDERKNKEKAVHLQEELIAIN 350
Cdd:pfam02463  237 --ERIDLLQELLRDEQEEIESSKQEIE-KEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDE 313
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462631416  351 SKKEELNQSVNRV-KELELELESVKAQSLAITKQNHMLNEKVKEMSDYSLLKEEKLELLAQNKLLKQQLEESRNENLRLL 429
Cdd:pfam02463  314 EKLKESEKEKKKAeKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLK 393
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462631416  430 NRLAQPAPELA----VFQKELRKAEKAIVVEHEEFESCRQALHKQLQDEIEHSAQLKAQILGYKASVKSLTTQVADLKLQ 505
Cdd:pfam02463  394 EEELELKSEEEkeaqLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKLLKDELELKKSEDL 473
                          330
                   ....*....|.
gi 2462631416  506 LKQTQTALENE 516
Cdd:pfam02463  474 LKETQLVKLQE 484
 
Name Accession Description Interval E-value
LisH_2 pfam16045
LisH;
75-101 9.29e-11

LisH;


Pssm-ID: 464992  Cd Length: 28  Bit Score: 57.09  E-value: 9.29e-11
                          10        20
                  ....*....|....*....|....*..
gi 2462631416  75 NSLVADHLQRCGYEYSLSVFFPESGLA 101
Cdd:pfam16045   2 NSLIAEYLQSQGYNYTLSVFLPESGLA 28
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
205-516 8.80e-10

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 62.26  E-value: 8.80e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462631416 205 REIEEQLRaemcqKLKffKDTEIAK----IKMEAKKkYEKELTMFQNDFEKACQAKSEALVLREKSTLERIHKHQEIETK 280
Cdd:COG1196   196 GELERQLE-----PLE--RQAEKAEryreLKEELKE-LEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEA 267
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462631416 281 EIYAQRQLLL---KDMDLLRGREAELKQRVEAFE---LYQLELKDDYIIRTNRLIEDERKNKEKAVHLQEELIAINSKKE 354
Cdd:COG1196   268 ELEELRLELEeleLELEEAQAEEYELLAELARLEqdiARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELE 347
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462631416 355 ELNQsvnRVKELELELESVKAQSLAITKQnhmLNEKVKEMSDYSLLKEEKLELLAQNKLLKQQLEESRNENLRLLNRLAQ 434
Cdd:COG1196   348 EAEE---ELEEAEAELAEAEEALLEAEAE---LAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEE 421
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462631416 435 papELAVFQKELRKAEKAIVVEHEEFESCRQALHKQLQDEIEH---SAQLKAQILGYKASVKSLTTQVADLKLQLKQTQT 511
Cdd:COG1196   422 ---ELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALlelLAELLEEAALLEAALAELLEELAEAAARLLLLLE 498

                  ....*
gi 2462631416 512 ALENE 516
Cdd:COG1196   499 AEADY 503
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
192-483 5.01e-07

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 53.40  E-value: 5.01e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462631416 192 KFESLEIKLNEYKREIEE-QLRAEMCQKLKFFKDTEIAKIKMEAKKKyEKELTMFQNDfekacqaksEALVLREKSTLER 270
Cdd:COG1196   233 KLRELEAELEELEAELEElEAELEELEAELAELEAELEELRLELEEL-ELELEEAQAE---------EYELLAELARLEQ 302
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462631416 271 IHKHQEIETKEIYAQRQLLLKDMDLLRGREAELKQRVEAFELYQLELKDDYIIRTNRLIEDERKNKEKAVHLQEELIAIN 350
Cdd:COG1196   303 DIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELE 382
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462631416 351 SKKEELNQSVNRVKELELELESVKAQSLAITKQNHMLNEKVKEmsdyslLKEEKLELLAQNKLLKQQLEESRNENLRLLN 430
Cdd:COG1196   383 ELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEE------LEEALAELEEEEEEEEEALEEAAEEEAELEE 456
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2462631416 431 RLAQPAPELAVFQKELRKAEKAIVVEHEEFESCRQALHKQLQDEIEHSAQLKA 483
Cdd:COG1196   457 EEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEG 509
PTZ00121 PTZ00121
MAEBL; Provisional
199-482 3.31e-06

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 50.91  E-value: 3.31e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462631416  199 KLNEYKREIEEQLRA-EMCQKLKFFKDTEIAKIKMEAKKKYEkELTMFQNDFEKACQAKSEALVLREKStlERIHKHQEI 277
Cdd:PTZ00121  1432 KADEAKKKAEEAKKAdEAKKKAEEAKKAEEAKKKAEEAKKAD-EAKKKAEEAKKADEAKKKAEEAKKKA--DEAKKAAEA 1508
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462631416  278 ETKEIYAQRQLLLKDMDLLRgrEAELKQRVEAFELYQLELKDDYIIRTNRLIEDERKNK-EKAVHLQEELIAINSKKEEL 356
Cdd:PTZ00121  1509 KKKADEAKKAEEAKKADEAK--KAEEAKKADEAKKAEEKKKADELKKAEELKKAEEKKKaEEAKKAEEDKNMALRKAEEA 1586
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462631416  357 NQS----VNRVKELELELESVKAQSLAITKQNHMLNEKVKEMSDYSLLKEEKLELLAQNKLLKQQLEESRNENLRLLNRL 432
Cdd:PTZ00121  1587 KKAeearIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEE 1666
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 2462631416  433 AQPAPELAVFQKELRKAE----KAIVVEHEEFESCRQA--LHKQLQDEIEHSAQLK 482
Cdd:PTZ00121  1667 AKKAEEDKKKAEEAKKAEedekKAAEALKKEAEEAKKAeeLKKKEAEEKKKAEELK 1722
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
196-514 1.89e-05

chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 48.53  E-value: 1.89e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462631416  196 LEIKLNEYKREIEEQLRAEMCQKLKFFKDTEIAKIKMEAKKKYEKELTMFQNDFEKACQAKsealvlrEKSTLERIHKHQ 275
Cdd:TIGR02169  193 IDEKRQQLERLRREREKAERYQALLKEKREYEGYELLKEKEALERQKEAIERQLASLEEEL-------EKLTEEISELEK 265
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462631416  276 EIETKEIyAQRQLLLKDMDLLRGREAELKQRVEAFELYqlelkddyIIRTNRLIEDERKNKEKAVHLQEELIA-INSKKE 354
Cdd:TIGR02169  266 RLEEIEQ-LLEELNKKIKDLGEEEQLRVKEKIGELEAE--------IASLERSIAEKERELEDAEERLAKLEAeIDKLLA 336
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462631416  355 ELNQSVNRVKELELELESVKAqslAITKQNHMLNEKVKEMSDYSLLKEEKLELLAQNKLLKQQLEESRNENLRLLNRLAQ 434
Cdd:TIGR02169  337 EIEELEREIEEERKRRDKLTE---EYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQE 413
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462631416  435 PAPELAVFQKELRKAEKAIVVEHEEFESCRQALHKQLQDEIEHSAQLKAQILGYKASVKSLTTQVADLKLQLKQTQTALE 514
Cdd:TIGR02169  414 ELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELA 493
sbcc TIGR00618
exonuclease SbcC; All proteins in this family for which functions are known are part of an ...
134-513 4.00e-05

exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]


Pssm-ID: 129705 [Multi-domain]  Cd Length: 1042  Bit Score: 47.27  E-value: 4.00e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462631416  134 ENQKGFLMHFLKELAEYHQAKEScnMETQTSSTFNRDSLAEKLQLIDDQFADAYPQRIKFESLEIKLNEYKREIEEQLRA 213
Cdd:TIGR00618  362 EVATSIREISCQQHTLTQHIHTL--QQQKTTLTQKLQSLCKELDILQREQATIDTRTSAFRDLQGQLAHAKKQQELQQRY 439
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462631416  214 EMCQKLKFFKDTEIAKIK----MEAKKKYeKELTMFQNDFEKACQAKSEALVLREKSTLEriHKHQEIETKEIYAQRQLL 289
Cdd:TIGR00618  440 AELCAAAITCTAQCEKLEkihlQESAQSL-KEREQQLQTKEQIHLQETRKKAVVLARLLE--LQEEPCPLCGSCIHPNPA 516
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462631416  290 LKDMDLLRGREAELKQRVEAFELYQLELKDDY---IIRTNRLIEDERKNKEKAVHLQEELIAINSKKEELNQSVNRVKEL 366
Cdd:TIGR00618  517 RQDIDNPGPLTRRMQRGEQTYAQLETSEEDVYhqlTSERKQRASLKEQMQEIQQSFSILTQCDNRSKEDIPNLQNITVRL 596
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462631416  367 ELELESVKAQSLAITKQNHMLNEKVKEmsdysllkeeklellAQNKLLKQQLEESRNENLRLLnRLAQPAPELAVFQKEL 446
Cdd:TIGR00618  597 QDLTEKLSEAEDMLACEQHALLRKLQP---------------EQDLQDVRLHLQQCSQELALK-LTALHALQLTLTQERV 660
                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2462631416  447 RKAEKAIVVEHEEFESCRQALHKQLQDEIEHSAQLKAQILGYKASVKSLTTQVADLKLQLKQTQTAL 513
Cdd:TIGR00618  661 REHALSIRVLPKELLASRQLALQKMQSEKEQLTYWKEMLAQCQTLLRELETHIEEYDREFNEIENAS 727
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
205-514 6.90e-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: 46.59  E-value: 6.90e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462631416  205 REIEEQLR-----AEMCQKLKFFKDTE------IAKIKMEAKKKYEKELTMFQNDFEKACQAKSEALVLREKSTLERIHK 273
Cdd:TIGR02168  196 NELERQLKslerqAEKAERYKELKAELrelelaLLVLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLE 275
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462631416  274 HQEIETKEIYAQRQLLLkdmdlLRGREAELKQRVEAFELYQLELKDDYIIRTNRLIEDERKNKEKAVHLQEELIAINSKK 353
Cdd:TIGR02168  276 VSELEEEIEELQKELYA-----LANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELK 350
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462631416  354 EELNQSVNRVKELELELESVKAQSLAITKQNHMLNEKVKEmsdysllkeeklellaqnklLKQQLEESRNENLRLLNRLA 433
Cdd:TIGR02168  351 EELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQ--------------------LELQIASLNNEIERLEARLE 410
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462631416  434 QPAPELAVFQKELRKAEKAIVVE-----HEEFESCRQALHKQLQDEIEHSAQLKAQilgyKASVKSLTTQVADLKLQLKQ 508
Cdd:TIGR02168  411 RLEDRRERLQQEIEELLKKLEEAelkelQAELEELEEELEELQEELERLEEALEEL----REELEEAEQALDAAERELAQ 486

                   ....*.
gi 2462631416  509 TQTALE 514
Cdd:TIGR02168  487 LQARLD 492
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
192-516 7.78e-05

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 46.21  E-value: 7.78e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462631416 192 KFESLEIKLNEYKREIEEQL--------RAEMCQKLKFFKDTEIAKIKMEAKK------KYEKELTMFQNDFEKACQAKS 257
Cdd:PRK03918  159 DYENAYKNLGEVIKEIKRRIerlekfikRTENIEELIKEKEKELEEVLREINEisselpELREELEKLEKEVKELEELKE 238
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462631416 258 EALVL-REKSTLERIHKHQEIETKEIYAQRQLLLKDMDLLRGREAELKQRVEAFELYQL--ELKDDYIIRTNRLIEDERK 334
Cdd:PRK03918  239 EIEELeKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKELKEKAEEYIKlsEFYEEYLDELREIEKRLSR 318
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462631416 335 NKEKAVHLQEELIAINSKKEELNQSVNRVKELELELESVKAQSLAItkqnHMLNEKVKEMSDYSLLKEEKLELLAQNKLL 414
Cdd:PRK03918  319 LEEEINGIEERIKELEEKEERLEELKKKLKELEKRLEELEERHELY----EEAKAKKEELERLKKRLTGLTPEKLEKELE 394
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462631416 415 -----KQQLEESRNENLRLLNRLAQPAPELAVFQKELRKAEKAIVVeheefesCRQALHKQLQDEIehSAQLKAQILGYK 489
Cdd:PRK03918  395 elekaKEEIEEEISKITARIGELKKEIKELKKAIEELKKAKGKCPV-------CGRELTEEHRKEL--LEEYTAELKRIE 465
                         330       340
                  ....*....|....*....|....*..
gi 2462631416 490 ASVKSLTTQVADLKLQLKQTQTALENE 516
Cdd:PRK03918  466 KELKEIEEKERKLRKELRELEKVLKKE 492
sbcc TIGR00618
exonuclease SbcC; All proteins in this family for which functions are known are part of an ...
181-508 1.35e-04

exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]


Pssm-ID: 129705 [Multi-domain]  Cd Length: 1042  Bit Score: 45.73  E-value: 1.35e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462631416  181 DQFADAYPQRIKfeslEIKLNEYKREIEEQLRAEMcqklkfFKDTEIAKIKMEAKKKYEKELTMFQNDFEKACQAKSEAL 260
Cdd:TIGR00618  155 AQFLKAKSKEKK----ELLMNLFPLDQYTQLALME------FAKKKSLHGKAELLTLRSQLLTLCTPCMPDTYHERKQVL 224
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462631416  261 VLREKSTLERIHkhQEIETKEIYAQRQLLLKDMDllrGREAELKQRVEAFELYQLELKDdyIIRTNRLIEDERKnKEKAV 340
Cdd:TIGR00618  225 EKELKHLREALQ--QTQQSHAYLTQKREAQEEQL---KKQQLLKQLRARIEELRAQEAV--LEETQERINRARK-AAPLA 296
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462631416  341 HLQEELIAINSKKEELNQSVN-RVKELELEL---ESVKAQSLAITKQNHMLNE----------------KVKEMSDYSLL 400
Cdd:TIGR00618  297 AHIKAVTQIEQQAQRIHTELQsKMRSRAKLLmkrAAHVKQQSSIEEQRRLLQTlhsqeihirdahevatSIREISCQQHT 376
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462631416  401 KEEKLELLAQNK-LLKQQLEESRNENLRLLNRLAQPAPELAVF---QKELRKAEKAIVVEHEEFESCRQALHKQLQDEIE 476
Cdd:TIGR00618  377 LTQHIHTLQQQKtTLTQKLQSLCKELDILQREQATIDTRTSAFrdlQGQLAHAKKQQELQQRYAELCAAAITCTAQCEKL 456
                          330       340       350
                   ....*....|....*....|....*....|..
gi 2462631416  477 HSAQLKAQILGYKAsvksLTTQVADLKLQLKQ 508
Cdd:TIGR00618  457 EKIHLQESAQSLKE----REQQLQTKEQIHLQ 484
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
202-469 1.46e-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: 42.35  E-value: 1.46e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462631416  202 EYKREIEEqLRaemcQKLKFFKDtEIAKIKMEAKKkYEKELTMFQNDFEKAcqaksealvLREKSTLERIHKHQEIETKE 281
Cdd:TIGR02168  674 ERRREIEE-LE----EKIEELEE-KIAELEKALAE-LRKELEELEEELEQL---------RKELEELSRQISALRKDLAR 737
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462631416  282 IYAQRQLLLKDMDLLRGREAELKQRVEafelyqlELKDDYIIRTNRLIEDERK---NKEKAVHLQEELIAINSKKEELNQ 358
Cdd:TIGR02168  738 LEAEVEQLEERIAQLSKELTELEAEIE-------ELEERLEEAEEELAEAEAEieeLEAQIEQLKEELKALREALDELRA 810
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462631416  359 SVNRVKE----LELELESVKAQSLAITKQNHMLNEKVKEMS-DYSLLKEEKLELLAQNKLLKQQLEESRNENLRLLNRLA 433
Cdd:TIGR02168  811 ELTLLNEeaanLRERLESLERRIAATERRLEDLEEQIEELSeDIESLAAEIEELEELIEELESELEALLNERASLEEALA 890
                          250       260       270
                   ....*....|....*....|....*....|....*.
gi 2462631416  434 QPAPELAVFQKELRKAEKAIVVEHEEFESCRQALHK 469
Cdd:TIGR02168  891 LLRSELEELSEELRELESKRSELRRELEELREKLAQ 926
PRK12704 PRK12704
phosphodiesterase; Provisional
299-454 2.21e-03

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 41.30  E-value: 2.21e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462631416 299 REAELKQRVEAFELyQLELKDDYIIRTNRLIEDERKNKEKAVHLQEELIAINSKKEELNQSVNRVKELELELESVKAqsl 378
Cdd:PRK12704   56 KEALLEAKEEIHKL-RNEFEKELRERRNELQKLEKRLLQKEENLDRKLELLEKREEELEKKEKELEQKQQELEKKEE--- 131
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2462631416 379 aitKQNHMLNEKVKEMSDYSllkeEKLELLAQNKLLKQQLEESRNENLRLLNRLAQPAPELAVfqkelRKAEKAIV 454
Cdd:PRK12704  132 ---ELEELIEEQLQELERIS----GLTAEEAKEILLEKVEEEARHEAAVLIKEIEEEAKEEAD-----KKAKEILA 195
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
307-517 3.29e-03

Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 40.77  E-value: 3.29e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462631416 307 VEAFELYQLELKDDYIIRTNRLIEDERKNKEKAVHLQEELIA-------INSKKEELNQSVNRVKELELELESVKAQSLA 379
Cdd:COG3206   158 AEAYLEQNLELRREEARKALEFLEEQLPELRKELEEAEAALEefrqkngLVDLSEEAKLLLQQLSELESQLAEARAELAE 237
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462631416 380 ITKQNHMLNEKVKEMSDYSLLKEEKLELLAqnklLKQQLEESRNENLRLLNRLAQPAPELAVFQKELrkaekaivvehee 459
Cdd:COG3206   238 AEARLAALRAQLGSGPDALPELLQSPVIQQ----LRAQLAELEAELAELSARYTPNHPDVIALRAQI------------- 300
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2462631416 460 fescrQALHKQLQDEIEHS-AQLKAQILGYKASVKSLTTQVADLKLQLK------QTQTALENEV 517
Cdd:COG3206   301 -----AALRAQLQQEAQRIlASLEAELEALQAREASLQAQLAQLEARLAelpeleAELRRLEREV 360
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
169-380 5.48e-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: 40.44  E-value: 5.48e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462631416  169 RDSLAEKLQliddQFADAYPQRIKFESLEIKLNEYKREIEEQLRAEMCQKlkffkdteiAKIKMEAKKKYEKELTMFQND 248
Cdd:TIGR02169  307 ERSIAEKER----ELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRR---------DKLTEEYAELKEELEDLRAEL 373
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462631416  249 FEKAcqAKSEALVLREKSTLERIHKHQEiETKEIYAQRQLLLKDMDLLRGREAELKQRVEAFELYQLELKDDYIIRTNRL 328
Cdd:TIGR02169  374 EEVD--KEFAETRDELKDYREKLEKLKR-EINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEI 450
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|..
gi 2462631416  329 IEDERKNKEKAVHLQEELIAINSKKEELNQSVNRVKELELELESVKAQSLAI 380
Cdd:TIGR02169  451 KKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQARAS 502
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
169-453 7.89e-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: 40.05  E-value: 7.89e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462631416  169 RDSLAEKLQLIDdQFADAYPQRIKFESLEIKLNEYKREIEEQLRAEMCQKLKFFKDtEIAKIKmEAKKKYEKELTmfqnD 248
Cdd:TIGR02169  690 LSSLQSELRRIE-NRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEE-DLSSLE-QEIENVKSELK----E 762
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462631416  249 FEKACQAKSEALV-LREK-STLERIHKHQEIEtkEIYAQRQLLLKDMDLLRGREAELKQRVEA--FELYQLELKDDYIIR 324
Cdd:TIGR02169  763 LEARIEELEEDLHkLEEAlNDLEARLSHSRIP--EIQAELSKLEEEVSRIEARLREIEQKLNRltLEKEYLEKEIQELQE 840
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462631416  325 TNRLIEDERKNKEKAVHLqeeliaINSKKEELNQSV----NRVKELELELESVKAQSLAITKQNHMLNEKVKEM-SDYSL 399
Cdd:TIGR02169  841 QRIDLKEQIKSIEKEIEN------LNGKKEELEEELeeleAALRDLESRLGDLKKERDELEAQLRELERKIEELeAQIEK 914
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....
gi 2462631416  400 LKEEKLELLAQNKLLKQQLEESrNENLRLLNRLAQPAPELAVFQKELRKAEKAI 453
Cdd:TIGR02169  915 KRKRLSELKAKLEALEEELSEI-EDPKGEDEEIPEEELSLEDVQAELQRVEEEI 967
SMC_N pfam02463
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...
191-516 8.19e-03

RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.


Pssm-ID: 426784 [Multi-domain]  Cd Length: 1161  Bit Score: 39.95  E-value: 8.19e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462631416  191 IKFESLEIKLNEYKREIEEQLRAEMCQKLKFFKDTEIAKIKMEAKKKYEKELTMFQNDFEKACQAKSEALVLREKSTLEr 270
Cdd:pfam02463  158 IEEEAAGSRLKRKKKEALKKLIEETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEYLLYLDYLKLNE- 236
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462631416  271 ihKHQEIETKEIYAQRQLLLKDMDLLRgREAELKQRVEAFELYQLELKDDYIIRTNRLIEDERKNKEKAVHLQEELIAIN 350
Cdd:pfam02463  237 --ERIDLLQELLRDEQEEIESSKQEIE-KEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDE 313
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462631416  351 SKKEELNQSVNRV-KELELELESVKAQSLAITKQNHMLNEKVKEMSDYSLLKEEKLELLAQNKLLKQQLEESRNENLRLL 429
Cdd:pfam02463  314 EKLKESEKEKKKAeKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLK 393
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462631416  430 NRLAQPAPELA----VFQKELRKAEKAIVVEHEEFESCRQALHKQLQDEIEHSAQLKAQILGYKASVKSLTTQVADLKLQ 505
Cdd:pfam02463  394 EEELELKSEEEkeaqLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKLLKDELELKKSEDL 473
                          330
                   ....*....|.
gi 2462631416  506 LKQTQTALENE 516
Cdd:pfam02463  474 LKETQLVKLQE 484
 
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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