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Conserved domains on  [gi|564337222|ref|XP_006232730|]
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pre-B-cell leukemia transcription factor-interacting protein 1 isoform X1 [Rattus norvegicus]

Protein Classification

splicing factor U2AF large subunit( domain architecture ID 1002097)

splicing factor U2AF large subunit such as U2AF65, also termed U2AF2, which is the large subunit of U2 small nuclear ribonucleoprotein (snRNP) auxiliary factor (U2AF), which has been implicated in the recruitment of U2 snRNP to pre-mRNAs

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
COG4913 super family cl25907
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
275-449 7.00e-05

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


The actual alignment was detected with superfamily member COG4913:

Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 46.45  E-value: 7.00e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564337222  275 LDKLAKENQDIRLLQAQLQAQKEELQSLLhqpkgLEEENARLREALQQGKTSHQALESELQQLRARLQGLEANcVRGVDG 354
Cdd:COG4913   264 YAAARERLAELEYLRAALRLWFAQRRLEL-----LEAELEELRAELARLEAELERLEARLDALREELDELEAQ-IRGNGG 337
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564337222  355 vclnwggspqggkatteqghkgqepdtsllEQHKQLEAEAKALRQELQKQWQLLGsvhrNLQRGLQDAGQGAPAHA-GLA 433
Cdd:COG4913   338 ------------------------------DRLEQLEREIERLERELEERERRRA----RLEALLAALGLPLPASAeEFA 383
                         170
                  ....*....|....*.
gi 564337222  434 ELGHMLAQTLQGLESQ 449
Cdd:COG4913   384 ALRAEAAALLEALEEE 399
U2AF_lg super family cl36941
U2 snRNP auxilliary factor, large subunit, splicing factor; These splicing factors consist of ...
479-599 6.68e-04

U2 snRNP auxilliary factor, large subunit, splicing factor; These splicing factors consist of an N-terminal arginine-rich low complexity domain followed by three tandem RNA recognition motifs (pfam00076). The well-characterized members of this family are auxilliary components of the U2 small nuclear ribonuclearprotein splicing factor (U2AF). These proteins are closely related to the CC1-like subfamily of splicing factors (TIGR01622). Members of this subfamily are found in plants, metazoa and fungi.


The actual alignment was detected with superfamily member TIGR01642:

Pssm-ID: 273727 [Multi-domain]  Cd Length: 509  Bit Score: 42.96  E-value: 6.68e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564337222  479 REKWRGGQRDQKAEHWKLKKEESGQDRKKS-WRDEGREftgHWKENRPRAEESGSRKDSKRQDPKVH------------- 544
Cdd:TIGR01642   1 RDEEPDREREKSRGRDRDRSSERPRRRSRDrSRFRDRH---RRSRERSYREDSRPRDRRRYDSRSPRslryssvrrsrdr 77
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 564337222  545 -PRKSGNSHSGERQKHSwGKDNSPDSVSWEELLRRKY--RPPQGCSGVADCARQEGLA 599
Cdd:TIGR01642  78 pRRRSRSVRSIEQHRRR-LRDRSPSNQWRKDDKKRSLwdIKPPGYELVTADQAKASQV 134
 
Name Accession Description Interval E-value
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
275-449 7.00e-05

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 46.45  E-value: 7.00e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564337222  275 LDKLAKENQDIRLLQAQLQAQKEELQSLLhqpkgLEEENARLREALQQGKTSHQALESELQQLRARLQGLEANcVRGVDG 354
Cdd:COG4913   264 YAAARERLAELEYLRAALRLWFAQRRLEL-----LEAELEELRAELARLEAELERLEARLDALREELDELEAQ-IRGNGG 337
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564337222  355 vclnwggspqggkatteqghkgqepdtsllEQHKQLEAEAKALRQELQKQWQLLGsvhrNLQRGLQDAGQGAPAHA-GLA 433
Cdd:COG4913   338 ------------------------------DRLEQLEREIERLERELEERERRRA----RLEALLAALGLPLPASAeEFA 383
                         170
                  ....*....|....*.
gi 564337222  434 ELGHMLAQTLQGLESQ 449
Cdd:COG4913   384 ALRAEAAALLEALEEE 399
SH3_and_anchor TIGR04211
SH3 domain protein; Members of this protein family have a signal peptide, a strongly conserved ...
286-409 3.73e-04

SH3 domain protein; Members of this protein family have a signal peptide, a strongly conserved SH3 domain, a variable region, and then a C-terminal hydrophobic transmembrane alpha helix region.


Pssm-ID: 275056 [Multi-domain]  Cd Length: 198  Bit Score: 42.30  E-value: 3.73e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564337222  286 RLLQAQLQAQKEELQSllhQPKGLEEENARLREALQQGKTSHQALESELQQLRARLQGLEAncvrgvdgvclnwggSPQG 365
Cdd:TIGR04211  65 RERLPELQQELAELQE---ELAELQEQLAELRQENQELKQQLSTLEAELEELQKELERIKQ---------------ISAN 126
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 564337222  366 GKATTEQGHKGQEPDTSLLEQHKQLEAEAKALRQELQKQWQLLG 409
Cdd:TIGR04211 127 AIELDEENRELREELAELKQENEALEAENERLQENEQRRWFLYG 170
U2AF_lg TIGR01642
U2 snRNP auxilliary factor, large subunit, splicing factor; These splicing factors consist of ...
479-599 6.68e-04

U2 snRNP auxilliary factor, large subunit, splicing factor; These splicing factors consist of an N-terminal arginine-rich low complexity domain followed by three tandem RNA recognition motifs (pfam00076). The well-characterized members of this family are auxilliary components of the U2 small nuclear ribonuclearprotein splicing factor (U2AF). These proteins are closely related to the CC1-like subfamily of splicing factors (TIGR01622). Members of this subfamily are found in plants, metazoa and fungi.


Pssm-ID: 273727 [Multi-domain]  Cd Length: 509  Bit Score: 42.96  E-value: 6.68e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564337222  479 REKWRGGQRDQKAEHWKLKKEESGQDRKKS-WRDEGREftgHWKENRPRAEESGSRKDSKRQDPKVH------------- 544
Cdd:TIGR01642   1 RDEEPDREREKSRGRDRDRSSERPRRRSRDrSRFRDRH---RRSRERSYREDSRPRDRRRYDSRSPRslryssvrrsrdr 77
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 564337222  545 -PRKSGNSHSGERQKHSwGKDNSPDSVSWEELLRRKY--RPPQGCSGVADCARQEGLA 599
Cdd:TIGR01642  78 pRRRSRSVRSIEQHRRR-LRDRSPSNQWRKDDKKRSLwdIKPPGYELVTADQAKASQV 134
ZapB pfam06005
Cell division protein ZapB; ZapB is a non-essential, abundant cell division factor that is ...
267-342 4.44e-03

Cell division protein ZapB; ZapB is a non-essential, abundant cell division factor that is required for proper Z-ring formation.


Pssm-ID: 428718 [Multi-domain]  Cd Length: 71  Bit Score: 36.48  E-value: 4.44e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 564337222  267 SLQSMGLLLDKLAKENQDIRLLQAQLQAQKEELQSLlhqpkglEEENARLREALQQGKTSHQALESELQQLRARLQ 342
Cdd:pfam06005   2 SLELLEQLETKIQAAVDTIALLQMENEELKEENEEL-------KEEANELEEENQQLKQERNQWQERIRGLLGKLD 70
PRK13922 PRK13922
rod shape-determining protein MreC; Provisional
275-321 7.93e-03

rod shape-determining protein MreC; Provisional


Pssm-ID: 237560  Cd Length: 276  Bit Score: 38.81  E-value: 7.93e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*..
gi 564337222 275 LDKLAKENQDIRLLQAQLQAQKEELQSLlhqpkglEEENARLREALQ 321
Cdd:PRK13922  71 LFDLREENEELKKELLELESRLQELEQL-------EAENARLRELLN 110
 
Name Accession Description Interval E-value
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
275-449 7.00e-05

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 46.45  E-value: 7.00e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564337222  275 LDKLAKENQDIRLLQAQLQAQKEELQSLLhqpkgLEEENARLREALQQGKTSHQALESELQQLRARLQGLEANcVRGVDG 354
Cdd:COG4913   264 YAAARERLAELEYLRAALRLWFAQRRLEL-----LEAELEELRAELARLEAELERLEARLDALREELDELEAQ-IRGNGG 337
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564337222  355 vclnwggspqggkatteqghkgqepdtsllEQHKQLEAEAKALRQELQKQWQLLGsvhrNLQRGLQDAGQGAPAHA-GLA 433
Cdd:COG4913   338 ------------------------------DRLEQLEREIERLERELEERERRRA----RLEALLAALGLPLPASAeEFA 383
                         170
                  ....*....|....*.
gi 564337222  434 ELGHMLAQTLQGLESQ 449
Cdd:COG4913   384 ALRAEAAALLEALEEE 399
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
256-347 1.21e-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: 45.14  E-value: 1.21e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564337222 256 LQASVPPDSVPSLQSMGLLLDKLAKENQDIRLLQAQLQAQKEELQSLLHQPKGLEEENARLREALQQGKTSHQA----LE 331
Cdd:COG4942  126 LSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKllarLE 205
                         90
                 ....*....|....*.
gi 564337222 332 SELQQLRARLQGLEAN 347
Cdd:COG4942  206 KELAELAAELAELQQE 221
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
277-347 1.71e-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: 44.37  E-value: 1.71e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 564337222 277 KLAKENQDIRLLQAQLQAQKEELQSLLHQPKGLEEENARLREALQQGKTSHQALESELQQLRARLQGLEAN 347
Cdd:COG4942   28 ELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAE 98
SH3_and_anchor TIGR04211
SH3 domain protein; Members of this protein family have a signal peptide, a strongly conserved ...
286-409 3.73e-04

SH3 domain protein; Members of this protein family have a signal peptide, a strongly conserved SH3 domain, a variable region, and then a C-terminal hydrophobic transmembrane alpha helix region.


Pssm-ID: 275056 [Multi-domain]  Cd Length: 198  Bit Score: 42.30  E-value: 3.73e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564337222  286 RLLQAQLQAQKEELQSllhQPKGLEEENARLREALQQGKTSHQALESELQQLRARLQGLEAncvrgvdgvclnwggSPQG 365
Cdd:TIGR04211  65 RERLPELQQELAELQE---ELAELQEQLAELRQENQELKQQLSTLEAELEELQKELERIKQ---------------ISAN 126
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 564337222  366 GKATTEQGHKGQEPDTSLLEQHKQLEAEAKALRQELQKQWQLLG 409
Cdd:TIGR04211 127 AIELDEENRELREELAELKQENEALEAENERLQENEQRRWFLYG 170
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
275-404 6.45e-04

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 43.37  E-value: 6.45e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564337222  275 LDKLAKENQDIRLLQAQLQAQKEELQSllhqpkgLEEENARLREALQQGKTSHQALESELQQLRARLQGLEANCVRGvdg 354
Cdd:COG4913   677 LERLDASSDDLAALEEQLEELEAELEE-------LEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLE--- 746
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 564337222  355 vcLNWGGSPQGGKATTEQghKGQEPDTSLLEQHKQLEAEAKALRQELQKQ 404
Cdd:COG4913   747 --LRALLEERFAAALGDA--VERELRENLEERIDALRARLNRAEEELERA 792
U2AF_lg TIGR01642
U2 snRNP auxilliary factor, large subunit, splicing factor; These splicing factors consist of ...
479-599 6.68e-04

U2 snRNP auxilliary factor, large subunit, splicing factor; These splicing factors consist of an N-terminal arginine-rich low complexity domain followed by three tandem RNA recognition motifs (pfam00076). The well-characterized members of this family are auxilliary components of the U2 small nuclear ribonuclearprotein splicing factor (U2AF). These proteins are closely related to the CC1-like subfamily of splicing factors (TIGR01622). Members of this subfamily are found in plants, metazoa and fungi.


Pssm-ID: 273727 [Multi-domain]  Cd Length: 509  Bit Score: 42.96  E-value: 6.68e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564337222  479 REKWRGGQRDQKAEHWKLKKEESGQDRKKS-WRDEGREftgHWKENRPRAEESGSRKDSKRQDPKVH------------- 544
Cdd:TIGR01642   1 RDEEPDREREKSRGRDRDRSSERPRRRSRDrSRFRDRH---RRSRERSYREDSRPRDRRRYDSRSPRslryssvrrsrdr 77
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 564337222  545 -PRKSGNSHSGERQKHSwGKDNSPDSVSWEELLRRKY--RPPQGCSGVADCARQEGLA 599
Cdd:TIGR01642  78 pRRRSRSVRSIEQHRRR-LRDRSPSNQWRKDDKKRSLwdIKPPGYELVTADQAKASQV 134
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
273-449 7.65e-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: 7.65e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564337222 273 LLLDKLAKENQDIRLLQAQLQAQKEELQSllhqpkgLEEENARLREALQQGKTSHQALESELQQLRARLQGLEAncvrgv 352
Cdd:COG1196  229 LLLLKLRELEAELEELEAELEELEAELEE-------LEAELAELEAELEELRLELEELELELEEAQAEEYELLA------ 295
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564337222 353 dgvclnwggspqgGKATTEQGHKgqepdtSLLEQHKQLEAEAKALRQELQKQWQLLGSVHRNLQRGLQDAGQGAPAHAGL 432
Cdd:COG1196  296 -------------ELARLEQDIA------RLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEA 356
                        170
                 ....*....|....*..
gi 564337222 433 AELGHMLAQTLQGLESQ 449
Cdd:COG1196  357 EAELAEAEEALLEAEAE 373
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
249-345 9.78e-04

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 42.45  E-value: 9.78e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564337222 249 RQDEVEQLQASVPPDSVPSLQSMGLLLDKLAKENQDIRLLQAQLQAQKEELQSLL--HQPKGLEEENARLREALQQGKTS 326
Cdd:COG4717  368 LEQEIAALLAEAGVEDEEELRAALEQAEEYQELKEELEELEEQLEELLGELEELLeaLDEEELEEELEELEEELEELEEE 447
                         90
                 ....*....|....*....
gi 564337222 327 HQALESELQQLRARLQGLE 345
Cdd:COG4717  448 LEELREELAELEAELEQLE 466
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
250-536 1.01e-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: 42.74  E-value: 1.01e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564337222   250 QDEVEQLQASVPPDSVPSLQS-MGLLLDKLAKENQDIRLLQAQLQAQKEELQSLLHQPKGLEEENARLREALQQGKTSHQ 328
Cdd:TIGR02168  219 KAELRELELALLVLRLEELREeLEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEIS 298
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564337222   329 ALESELQQLRARLQGLEANCVRgVDGVCLNWGGSPQGGKATTEQGHKGQEPDTSLLEQHKQLEAEAKALRQELQKQWQLL 408
Cdd:TIGR02168  299 RLEQQKQILRERLANLERQLEE-LEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEEL 377
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564337222   409 GSVHRNLQRGLQDAGQGAPAHAglAELGHMLAQtLQGLESQGINTGRSSNDSEAWHQKKPRFQHPREWSGREkwrggqrd 488
Cdd:TIGR02168  378 EEQLETLRSKVAQLELQIASLN--NEIERLEAR-LERLEDRRERLQQEIEELLKKLEEAELKELQAELEELE-------- 446
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*...
gi 564337222   489 qKAEHWKLKKEESGQDRKKSWRDEGREFTGHWKENRPRAEESGSRKDS 536
Cdd:TIGR02168  447 -EELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDS 493
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
277-449 1.54e-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: 41.97  E-value: 1.54e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564337222   277 KLAKENQDIRLLQAQLQAQKEELQSLLHQPKGLEEENARLREALQQGKTSHQALESELQQLRARLQGLEANcvrgVDGVC 356
Cdd:TIGR02168  678 EIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEER----IAQLS 753
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564337222   357 LNWGGSPQGGKATTEQGHKGQEPDTSLLEQHKQLEAEAKALRQELQKQWQLLGSVHRNLQRGLQDAGQGAPAHAGLAELG 436
Cdd:TIGR02168  754 KELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRI 833
                          170
                   ....*....|...
gi 564337222   437 HMLAQTLQGLESQ 449
Cdd:TIGR02168  834 AATERRLEDLEEQ 846
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
276-347 1.55e-03

Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 41.67  E-value: 1.55e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 564337222 276 DKLAKENQDIRLLQAQLQAQKEELQSLLHQPKGLEEENARLREALQQGKTSHQALESELQQLRARLQGLEAN 347
Cdd:COG4942   20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKE 91
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
276-449 2.07e-03

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 41.46  E-value: 2.07e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564337222 276 DKLAKENQDIRLLQAQLQAQKEELQSLLHQPKGLEEENARLREALQQGKTSHQALESELQQLRARLQGLEAncvrgvdgv 355
Cdd:COG1196  274 LELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEE--------- 344
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564337222 356 clnwggspQGGKATTEQGHKGQEpdtslLEQHKQLEAEAKALRQELQKQWQllgsvhRNLQRGLQDAGQGAPAHAGLAEL 435
Cdd:COG1196  345 --------ELEEAEEELEEAEAE-----LAEAEEALLEAEAELAEAEEELE------ELAEELLEALRAAAELAAQLEEL 405
                        170
                 ....*....|....
gi 564337222 436 GHMLAQTLQGLESQ 449
Cdd:COG1196  406 EEAEEALLERLERL 419
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
234-414 3.06e-03

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 40.91  E-value: 3.06e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564337222 234 LQVFPETELVQTVGNRQDEVEQLQASVPPDSVPSLQSMGLLLDKLAKENQDIRLLQAQLQAQKEELQSLLHQPKGLEEEN 313
Cdd:COG4717   39 LLAFIRAMLLERLEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREEL 118
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564337222 314 ARLREALQqgktsHQALESELQQLRARLQGLEANcvrgvdgvclnwggspqggkatTEQGHKGQEPDTSLLEQHKQLEAE 393
Cdd:COG4717  119 EKLEKLLQ-----LLPLYQELEALEAELAELPER----------------------LEELEERLEELRELEEELEELEAE 171
                        170       180
                 ....*....|....*....|.
gi 564337222 394 AKALRQELQKQWQLLGSVHRN 414
Cdd:COG4717  172 LAELQEELEELLEQLSLATEE 192
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
251-346 3.25e-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: 40.81  E-value: 3.25e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564337222   251 DEVEQLQasvppDSVPSLQSMGLLLDKLAKENQdIRLLQAQLQAQKEELQSLLHQPKGLEEENARLREALQQGKTSHQAL 330
Cdd:TIGR02168  407 ARLERLE-----DRRERLQQEIEELLKKLEEAE-LKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAA 480
                           90
                   ....*....|....*.
gi 564337222   331 ESELQQLRARLQGLEA 346
Cdd:TIGR02168  481 ERELAQLQARLDSLER 496
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
276-347 3.47e-03

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 40.27  E-value: 3.47e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 564337222 276 DKLAKENQDIRLLQAQLQAQKEELQSLLHQPKGLEEENARLREALQQGKTSHQALESELQQLRARLQGLEAN 347
Cdd:COG4372  101 EELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQE 172
ZapB pfam06005
Cell division protein ZapB; ZapB is a non-essential, abundant cell division factor that is ...
267-342 4.44e-03

Cell division protein ZapB; ZapB is a non-essential, abundant cell division factor that is required for proper Z-ring formation.


Pssm-ID: 428718 [Multi-domain]  Cd Length: 71  Bit Score: 36.48  E-value: 4.44e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 564337222  267 SLQSMGLLLDKLAKENQDIRLLQAQLQAQKEELQSLlhqpkglEEENARLREALQQGKTSHQALESELQQLRARLQ 342
Cdd:pfam06005   2 SLELLEQLETKIQAAVDTIALLQMENEELKEENEEL-------KEEANELEEENQQLKQERNQWQERIRGLLGKLD 70
MreC COG1792
Cell shape-determining protein MreC [Cell cycle control, cell division, chromosome ...
275-321 4.47e-03

Cell shape-determining protein MreC [Cell cycle control, cell division, chromosome partitioning, Cytoskeleton];


Pssm-ID: 441397  Cd Length: 282  Bit Score: 39.86  E-value: 4.47e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*..
gi 564337222 275 LDKLAKENQDIRLLQAQLQAQKEELQSLlhqpkglEEENARLREALQ 321
Cdd:COG1792   70 LFNLREENERLKEENAELRAELQRLEEL-------EAENARLRELLD 109
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
274-402 4.73e-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: 4.73e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564337222  274 LLDKLAKENQDIRLLQAQLQAQKEELQSLLHQPKG--------LEEENARLREALQQgktshqaLESELQQLRARLQGLE 345
Cdd:COG4913   300 LRAELARLEAELERLEARLDALREELDELEAQIRGnggdrleqLEREIERLERELEE-------RERRRARLEALLAALG 372
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 564337222  346 ANCVRGVDGVCLNWGGSPQGGKATTEQGHKGQEPDTSLLEQHKQLEAEAKALRQELQ 402
Cdd:COG4913   373 LPLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIA 429
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
249-418 5.02e-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: 5.02e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564337222  249 RQDEVEQLQASVPPDSvpSLQSMGLLLDKLAKENQDIRLLQAQLQAQKEELQSllhqpkgLEEENARLREALQQ-GKTSH 327
Cdd:COG4913   270 RLAELEYLRAALRLWF--AQRRLELLEAELEELRAELARLEAELERLEARLDA-------LREELDELEAQIRGnGGDRL 340
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564337222  328 QALESELQQLRARLQGLEANCVR---GVDGVCLNWGGSPQGGKATTEQGHKGQEPDTSLLEQHKQLEAEAKALRQELQKQ 404
Cdd:COG4913   341 EQLEREIERLERELEERERRRARleaLLAALGLPLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRE 420
                         170
                  ....*....|....
gi 564337222  405 WQLLGSVHRNLQRG 418
Cdd:COG4913   421 LRELEAEIASLERR 434
ADIP pfam11559
Afadin- and alpha -actinin-Binding; This family is found in mammals where it is localized at ...
274-341 5.18e-03

Afadin- and alpha -actinin-Binding; This family is found in mammals where it is localized at cell-cell adherens junctions, and in Sch. pombe and other fungi where it anchors spindle-pole bodies to spindle microtubules. It is a coiled-coil structure, and in pombe, it is required for anchoring the minus end of spindle microtubules to the centrosome equivalent, the spindle-pole body. The name ADIP derives from the family being composed of Afadin- and alpha -Actinin-Binding Proteins localized at Cell-Cell Adherens Junctions.


Pssm-ID: 463295 [Multi-domain]  Cd Length: 151  Bit Score: 38.07  E-value: 5.18e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 564337222  274 LLDKLAKENQDIRLLQAQLQAQKEELQSLLHQPKGLEEENARLREALQQGKTSH----QALESELQQLRARL 341
Cdd:pfam11559  78 LKTQLEDLERELALLQAKERQLEKKLKTLEQKLKNEKEELQRLKNALQQIKTQFahevKKRDREIEKLKERL 149
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
230-452 5.69e-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: 40.04  E-value: 5.69e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564337222   230 EEAELQVFPETELVQTVGNRQDEVEQLQASVPPDSVPSLQSMGLLLDKLAKEN-------QDIRLLQAQLQAQKEELQSL 302
Cdd:TIGR02168  722 EELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEeelaeaeAEIEELEAQIEQLKEELKAL 801
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564337222   303 LHQPKGLEEENARLREALQQGKTSHQALESELQQLRARLQGLEANCVRgvdgvclnwgGSPQGGKATTEQGHKGQEPDTS 382
Cdd:TIGR02168  802 REALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEE----------LSEDIESLAAEIEELEELIEEL 871
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 564337222   383 L--LEQHKQLEAEAKALRQELQKQWQLLGSVHRNLQRGLQDAGQgapahaGLAELGHMLAQ---TLQGLESQGIN 452
Cdd:TIGR02168  872 EseLEALLNERASLEEALALLRSELEELSEELRELESKRSELRR------ELEELREKLAQlelRLEGLEVRIDN 940
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
250-342 6.55e-03

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


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 40.00  E-value: 6.55e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564337222 250 QDEVEQLQASVppDSVPSLQSMGLLLDKLAKENQDIRLLQAQLQAQKEELQSLLHQPKGLEEENARLRE--ALQQGKTSH 327
Cdd:COG3206  195 EAALEEFRQKN--GLVDLSEEAKLLLQQLSELESQLAEARAELAEAEARLAALRAQLGSGPDALPELLQspVIQQLRAQL 272
                         90
                 ....*....|....*
gi 564337222 328 QALESELQQLRARLQ 342
Cdd:COG3206  273 AELEAELAELSARYT 287
PRK13922 PRK13922
rod shape-determining protein MreC; Provisional
275-321 7.93e-03

rod shape-determining protein MreC; Provisional


Pssm-ID: 237560  Cd Length: 276  Bit Score: 38.81  E-value: 7.93e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*..
gi 564337222 275 LDKLAKENQDIRLLQAQLQAQKEELQSLlhqpkglEEENARLREALQ 321
Cdd:PRK13922  71 LFDLREENEELKKELLELESRLQELEQL-------EAENARLRELLN 110
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
231-408 9.18e-03

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 39.51  E-value: 9.18e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564337222  231 EAELQvfpetELVQTVGNRQDEVEQLQASVppDSVPSLQSMGLLLDKLAKENQDIRLLQAQLQAQKEELQSLL------- 303
Cdd:COG4913   616 EAELA-----ELEEELAEAEERLEALEAEL--DALQERREALQRLAEYSWDEIDVASAEREIAELEAELERLDassddla 688
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564337222  304 ---HQPKGLEEENARLREALQQGKTSHQALESELQQLRARLQGLEANCVRGVDGVClnwggspQGGKATTEQGHKGQEPD 380
Cdd:COG4913   689 aleEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLAR-------LELRALLEERFAAALGD 761
                         170       180
                  ....*....|....*....|....*...
gi 564337222  381 TSLLEQHKQLEAEAKALRQELQKQWQLL 408
Cdd:COG4913   762 AVERELRENLEERIDALRARLNRAEEEL 789
 
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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