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Conserved domains on  [gi|568922526|ref|XP_006501415|]
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pre-B-cell leukemia transcription factor-interacting protein 1 isoform X1 [Mus musculus]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
EnvC super family cl34844
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 251-351 7.55e-06

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


The actual alignment was detected with superfamily member COG4942:

Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 48.99  E-value: 7.55e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568922526 251 NRQDEIEHLQASSVPPDSVPSLQSMGFLLDKLAKENQDIRLLQAQLQAQKEELQSLLHQPKGLEEENARLREALQQGKTS 330
Cdd:COG4942  117 GRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAE 196

                         90       100
                 ....*....|....*....|....*
gi 568922526 331 HQA----LESELQQLRARLQGLEAN 351
Cdd:COG4942  197 RQKllarLEKELAELAAELAELQQE 221
SMC_prok_B super family cl37069
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 281-466 9.55e-04

chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


The actual alignment was detected with superfamily member TIGR02168:

Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 42.74  E-value: 9.55e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568922526   281 KLAKENQDIRLLQAQLQAQKEELQSLLHQPKGLEEENARLREALQQGKTSHQALESELQQLRARLQGLEANCVRgvdgvc 360
Cdd:TIGR02168  678 EIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQ------ 751

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568922526   361 lnWGGDPQDGKATKEQGHKGQEPDPSLLEQHKQLEAEAKALRQELQRQWQLLGSVHWDLQRGLRDagrgapahpgLAELG 440
Cdd:TIGR02168  752 --LSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTL----------LNEEA 819

                          170       180
                   ....*....|....*....|....*.
gi 568922526   441 HMLAQTLQDLENQGINTGRSPNDSEA 466
Cdd:TIGR02168  820 ANLRERLESLERRIAATERRLEDLEE 845
U2AF_lg super family cl36941
U2 snRNP auxilliary factor, large subunit, splicing factor; These splicing factors consist of ...
 483-583 1.28e-03

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: 42.19  E-value: 1.28e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568922526  483 KEKWRGGQRDQKAEHWKPRKEESGQERQRS-WRDEGREhtgRWREDRLRADESGSRKDSKRQDPKvhpRKDGNSHSVERQ 561
Cdd:TIGR01642   1 RDEEPDREREKSRGRDRDRSSERPRRRSRDrSRFRDRH---RRSRERSYREDSRPRDRRRYDSRS---PRSLRYSSVRRS 74

                          90       100
                  ....*....|....*....|..
gi 568922526  562 KHSWGKDNSPdaLSSWEELLRR 583
Cdd:TIGR01642  75 RDRPRRRSRS--VRSIEQHRRR 94
 
Name Accession Description Interval E-value
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 251-351 7.55e-06

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: 48.99  E-value: 7.55e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568922526 251 NRQDEIEHLQASSVPPDSVPSLQSMGFLLDKLAKENQDIRLLQAQLQAQKEELQSLLHQPKGLEEENARLREALQQGKTS 330
Cdd:COG4942  117 GRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAE 196

                         90       100
                 ....*....|....*....|....*
gi 568922526 331 HQA----LESELQQLRARLQGLEAN 351
Cdd:COG4942  197 RQKllarLEKELAELAAELAELQQE 221
SH3_and_anchor TIGR04211
SH3 domain protein; Members of this protein family have a signal peptide, a strongly conserved ...
 290-413 7.42e-05

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: 44.23  E-value: 7.42e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568922526  290 RLLQAQLQAQKEELQSllhQPKGLEEENARLREALQQGKTSHQALESELQQLRARLQGLEAncvrgvdgvclnwggDPQD 369
Cdd:TIGR04211  65 RERLPELQQELAELQE---ELAELQEQLAELRQENQELKQQLSTLEAELEELQKELERIKQ---------------ISAN 126

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 568922526  370 GKATKEQGHKGQEPDPSLLEQHKQLEAEAKALRQELQRQWQLLG 413
Cdd:TIGR04211 127 AIELDEENRELREELAELKQENEALEAENERLQENEQRRWFLYG 170
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 281-466 9.55e-04

chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 42.74  E-value: 9.55e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568922526   281 KLAKENQDIRLLQAQLQAQKEELQSLLHQPKGLEEENARLREALQQGKTSHQALESELQQLRARLQGLEANCVRgvdgvc 360
Cdd:TIGR02168  678 EIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQ------ 751

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568922526   361 lnWGGDPQDGKATKEQGHKGQEPDPSLLEQHKQLEAEAKALRQELQRQWQLLGSVHWDLQRGLRDagrgapahpgLAELG 440
Cdd:TIGR02168  752 --LSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTL----------LNEEA 819

                          170       180
                   ....*....|....*....|....*.
gi 568922526   441 HMLAQTLQDLENQGINTGRSPNDSEA 466
Cdd:TIGR02168  820 ANLRERLESLERRIAATERRLEDLEE 845
U2AF_lg TIGR01642
U2 snRNP auxilliary factor, large subunit, splicing factor; These splicing factors consist of ...
 483-583 1.28e-03

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: 42.19  E-value: 1.28e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568922526  483 KEKWRGGQRDQKAEHWKPRKEESGQERQRS-WRDEGREhtgRWREDRLRADESGSRKDSKRQDPKvhpRKDGNSHSVERQ 561
Cdd:TIGR01642   1 RDEEPDREREKSRGRDRDRSSERPRRRSRDrSRFRDRH---RRSRERSYREDSRPRDRRRYDSRS---PRSLRYSSVRRS 74

                          90       100
                  ....*....|....*....|..
gi 568922526  562 KHSWGKDNSPdaLSSWEELLRR 583
Cdd:TIGR01642  75 RDRPRRRSRS--VRSIEQHRRR 94
ADIP pfam11559
Afadin- and alpha -actinin-Binding; This family is found in mammals where it is localized at ...
 242-345 2.90e-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: 38.84  E-value: 2.90e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568922526  242 ETELVETLGNRQDEIEHLQASsvppdsVPSLQsmgfllDKLAKENQDIRLLQAQLQAQKEELQSLLHQPKGLEEENARLR 321
Cdd:pfam11559  54 RESLNETIRTLEAEIERLQSK------IERLK------TQLEDLERELALLQAKERQLEKKLKTLEQKLKNEKEELQRLK 121

                          90       100
                  ....*....|....*....|....*...
gi 568922526  322 EALQQGKTSH----QALESELQQLRARL 345
Cdd:pfam11559 122 NALQQIKTQFahevKKRDREIEKLKERL 149
PRK13922 PRK13922
rod shape-determining protein MreC; Provisional
 279-325 8.00e-03

rod shape-determining protein MreC; Provisional


Pssm-ID: 237560  Cd Length: 276  Bit Score: 38.81  E-value: 8.00e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*..
gi 568922526 279 LDKLAKENQDIRLLQAQLQAQKEELQSLlhqpkglEEENARLREALQ 325
Cdd:PRK13922  71 LFDLREENEELKKELLELESRLQELEQL-------EAENARLRELLN 110
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
276-428 9.22e-03

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 39.37  E-value: 9.22e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568922526 276 GFLLDKLAKENQDI--------RLLQAQLQAQKEELQSLLHQpkglEEENARLREALQQGKTSHQALESELQQLRARLQG 347
Cdd:COG4717   45 AMLLERLEKEADELfkpqgrkpELNLKELKELEEELKEAEEK----EEEYAELQEELEELEEELEELEAELEELREELEK 120

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568922526 348 LEANcvrgvdgvcLNWGGDPQDGKATK----------EQGHKGQEPDPSLLEQHKQLEAEAKALRQELQRQWQLLG-SVH 416
Cdd:COG4717  121 LEKL---------LQLLPLYQELEALEaelaelperlEELEERLEELRELEEELEELEAELAELQEELEELLEQLSlATE 191

                        170
                 ....*....|..
gi 568922526 417 WDLQRGLRDAGR 428
Cdd:COG4717  192 EELQDLAEELEE 203
 
Name Accession Description Interval E-value
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 251-351 7.55e-06

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: 48.99  E-value: 7.55e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568922526 251 NRQDEIEHLQASSVPPDSVPSLQSMGFLLDKLAKENQDIRLLQAQLQAQKEELQSLLHQPKGLEEENARLREALQQGKTS 330
Cdd:COG4942  117 GRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAE 196

                         90       100
                 ....*....|....*....|....*
gi 568922526 331 HQA----LESELQQLRARLQGLEAN 351
Cdd:COG4942  197 RQKllarLEKELAELAAELAELQQE 221
SH3_and_anchor TIGR04211
SH3 domain protein; Members of this protein family have a signal peptide, a strongly conserved ...
 290-413 7.42e-05

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: 44.23  E-value: 7.42e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568922526  290 RLLQAQLQAQKEELQSllhQPKGLEEENARLREALQQGKTSHQALESELQQLRARLQGLEAncvrgvdgvclnwggDPQD 369
Cdd:TIGR04211  65 RERLPELQQELAELQE---ELAELQEQLAELRQENQELKQQLSTLEAELEELQKELERIKQ---------------ISAN 126

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 568922526  370 GKATKEQGHKGQEPDPSLLEQHKQLEAEAKALRQELQRQWQLLG 413
Cdd:TIGR04211 127 AIELDEENRELREELAELKQENEALEAENERLQENEQRRWFLYG 170
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 281-351 1.26e-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: 1.26e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568922526 281 KLAKENQDIRLLQAQLQAQKEELQSLLHQPKGLEEENARLREALQQGKTSHQALESELQQLRARLQGLEAN 351
Cdd:COG4942   28 ELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAE 98
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
279-412 2.51e-04

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 44.52  E-value: 2.51e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568922526  279 LDKLAKENQDIRLLQAQLQAQKEELQSllhqpkgLEEENARLREALQQGKTSHQALESELQQLRARLQGLEANCVRGvdg 358
Cdd:COG4913   677 LERLDASSDDLAALEEQLEELEAELEE-------LEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLE--- 746

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 568922526  359 vcLNWGGDPQDGKATKEQGHKgqepdpsllEQHKQLEAEAKALRQELQRQWQLL 412
Cdd:COG4913   747 --LRALLEERFAAALGDAVER---------ELRENLEERIDALRARLNRAEEEL 789
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 280-410 5.31e-04

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 43.39  E-value: 5.31e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568922526 280 DKLAKENQDIRLLQAQLQAQKEELQSLLHQPKGLEEENARLREALQQGKTSHQALESELQQLRARLQGLEAncvrgvdgv 359
Cdd:COG1196  274 LELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEE--------- 344

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 568922526 360 clnwggdpQDGKATKEQGHKGQEpdpslLEQHKQLEAEAKALRQELQRQWQ 410
Cdd:COG1196  345 --------ELEEAEEELEEAEAE-----LAEAEEALLEAEAELAEAEEELE 382
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 281-466 9.55e-04

chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 42.74  E-value: 9.55e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568922526   281 KLAKENQDIRLLQAQLQAQKEELQSLLHQPKGLEEENARLREALQQGKTSHQALESELQQLRARLQGLEANCVRgvdgvc 360
Cdd:TIGR02168  678 EIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQ------ 751

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568922526   361 lnWGGDPQDGKATKEQGHKGQEPDPSLLEQHKQLEAEAKALRQELQRQWQLLGSVHWDLQRGLRDagrgapahpgLAELG 440
Cdd:TIGR02168  752 --LSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTL----------LNEEA 819

                          170       180
                   ....*....|....*....|....*.
gi 568922526   441 HMLAQTLQDLENQGINTGRSPNDSEA 466
Cdd:TIGR02168  820 ANLRERLESLERRIAATERRLEDLEE 845
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 280-351 1.17e-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: 42.06  E-value: 1.17e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568922526 280 DKLAKENQDIRLLQAQLQAQKEELQSLLHQPKGLEEENARLREALQQGKTSHQALESELQQLRARLQGLEAN 351
Cdd:COG4942   20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKE 91
U2AF_lg TIGR01642
U2 snRNP auxilliary factor, large subunit, splicing factor; These splicing factors consist of ...
 483-583 1.28e-03

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: 42.19  E-value: 1.28e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568922526  483 KEKWRGGQRDQKAEHWKPRKEESGQERQRS-WRDEGREhtgRWREDRLRADESGSRKDSKRQDPKvhpRKDGNSHSVERQ 561
Cdd:TIGR01642   1 RDEEPDREREKSRGRDRDRSSERPRRRSRDrSRFRDRH---RRSRERSYREDSRPRDRRRYDSRS---PRSLRYSSVRRS 74

                          90       100
                  ....*....|....*....|..
gi 568922526  562 KHSWGKDNSPdaLSSWEELLRR 583
Cdd:TIGR01642  75 RDRPRRRSRS--VRSIEQHRRR 94
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
280-351 1.82e-03

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 41.43  E-value: 1.82e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568922526 280 DKLAKENQDIRLLQAQLQAQKEELQSLLHQPKGLEEENARLREALQQGKTSHQALESELQQLRARLQGLEAN 351
Cdd:COG4372  101 EELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQE 172
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 253-406 2.33e-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: 41.58  E-value: 2.33e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568922526   253 QDEIEHLQASSVPPDSVPSLQSMGFLLDKLAKENQDIRLLQAQLQAQKEELQSLLHQPKGLEEENARLREALQQGKTSHQ 332
Cdd:TIGR02168  219 KAELRELELALLVLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEIS 298

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568922526   333 ALESELQQLRARLQGLEANCVRgVDGVCLNWGGDPQDGKATKEQGHKGQEpdpSLLEQHKQLEAEAKALRQELQ 406
Cdd:TIGR02168  299 RLEQQKQILRERLANLERQLEE-LEAQLEELESKLDELAEELAELEEKLE---ELKEELESLEAELEELEAELE 368
ADIP pfam11559
Afadin- and alpha -actinin-Binding; This family is found in mammals where it is localized at ...
 242-345 2.90e-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: 38.84  E-value: 2.90e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568922526  242 ETELVETLGNRQDEIEHLQASsvppdsVPSLQsmgfllDKLAKENQDIRLLQAQLQAQKEELQSLLHQPKGLEEENARLR 321
Cdd:pfam11559  54 RESLNETIRTLEAEIERLQSK------IERLK------TQLEDLERELALLQAKERQLEKKLKTLEQKLKNEKEELQRLK 121

                          90       100
                  ....*....|....*....|....*...
gi 568922526  322 EALQQGKTSH----QALESELQQLRARL 345
Cdd:pfam11559 122 NALQQIKTQFahevKKRDREIEKLKERL 149
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 283-350 3.11e-03

chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 41.20  E-value: 3.11e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568922526   283 AKENQDIRLLQAQLQAQKEELQSLLHQPKGLEEENARLREALQQGKTSHQALESELQQLRARLQGLEA 350
Cdd:TIGR02168  429 KLEEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLER 496
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 289-408 3.76e-03

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 40.69  E-value: 3.76e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568922526 289 IRLLQAQLQAQKEELQSLLHQPKGLEEENARLREALQQGKTSHQALESELQQLRARLQGLEAncvrgvdgvclnwggdpq 368
Cdd:COG1196  234 LRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLA------------------ 295

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 568922526 369 dGKATKEQGHKgqepdpSLLEQHKQLEAEAKALRQELQRQ 408
Cdd:COG1196  296 -ELARLEQDIA------RLEERRRELEERLEELEEELAEL 328
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
278-408 3.82e-03

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 40.67  E-value: 3.82e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568922526  278 LLDKLAKENQDIRLLQAQLQAQKEELQSLLHQPKGLE-EENARLREALQQGKTSHQALESELQQLRARLQGLEancvrgv 356
Cdd:COG4913   300 LRAELARLEAELERLEARLDALREELDELEAQIRGNGgDRLEQLEREIERLERELEERERRRARLEALLAALG------- 372

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 568922526  357 dgvcLNWGGDPQDGKATKEQGHKGQEPDPSLLEQHKQLEAEAKALRQELQRQ 408
Cdd:COG4913   373 ----LPLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRE 420
MreC COG1792
Cell shape-determining protein MreC [Cell cycle control, cell division, chromosome ...
 279-325 4.50e-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: 4.50e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*..
gi 568922526 279 LDKLAKENQDIRLLQAQLQAQKEELQSLlhqpkglEEENARLREALQ 325
Cdd:COG1792   70 LFNLREENERLKEENAELRAELQRLEEL-------EAENARLRELLD 109
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
279-407 6.87e-03

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 39.90  E-value: 6.87e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568922526  279 LDKLAKENQDIRLLQAQLQAQKEELQSLLHQpkgLEEENARLREALQQ-GKTSHQALESELQQLRARLQGLEANCVR--- 354
Cdd:COG4913   290 LELLEAELEELRAELARLEAELERLEARLDA---LREELDELEAQIRGnGGDRLEQLEREIERLERELEERERRRARlea 366

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568922526  355 GVDGVCLNWGGDPQDGKATKEQGHKGQEPDPSLLE-----------QHKQLEAEAKALRQELQR 407
Cdd:COG4913   367 LLAALGLPLPASAEEFAALRAEAAALLEALEEELEaleealaeaeaALRDLRRELRELEAEIAS 430
ZapB pfam06005
Cell division protein ZapB; ZapB is a non-essential, abundant cell division factor that is ...
 271-346 7.91e-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: 35.70  E-value: 7.91e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568922526  271 SLQSMGFLLDKLAKENQDIRLLQAQLQAQKEELQSLlhqpkglEEENARLREALQQGKTSHQALESELQQLRARLQ 346
Cdd:pfam06005   2 SLELLEQLETKIQAAVDTIALLQMENEELKEENEEL-------KEEANELEEENQQLKQERNQWQERIRGLLGKLD 70
PRK13922 PRK13922
rod shape-determining protein MreC; Provisional
 279-325 8.00e-03

rod shape-determining protein MreC; Provisional


Pssm-ID: 237560  Cd Length: 276  Bit Score: 38.81  E-value: 8.00e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*..
gi 568922526 279 LDKLAKENQDIRLLQAQLQAQKEELQSLlhqpkglEEENARLREALQ 325
Cdd:PRK13922  71 LFDLREENEELKKELLELESRLQELEQL-------EAENARLRELLN 110
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
276-428 9.22e-03

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 39.37  E-value: 9.22e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568922526 276 GFLLDKLAKENQDI--------RLLQAQLQAQKEELQSLLHQpkglEEENARLREALQQGKTSHQALESELQQLRARLQG 347
Cdd:COG4717   45 AMLLERLEKEADELfkpqgrkpELNLKELKELEEELKEAEEK----EEEYAELQEELEELEEELEELEAELEELREELEK 120

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568922526 348 LEANcvrgvdgvcLNWGGDPQDGKATK----------EQGHKGQEPDPSLLEQHKQLEAEAKALRQELQRQWQLLG-SVH 416
Cdd:COG4717  121 LEKL---------LQLLPLYQELEALEaelaelperlEELEERLEELRELEEELEELEAELAELQEELEELLEQLSlATE 191

                        170
                 ....*....|..
gi 568922526 417 WDLQRGLRDAGR 428
Cdd:COG4717  192 EELQDLAEELEE 203
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
278-351 9.58e-03

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 39.12  E-value: 9.58e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568922526 278 LLDKLAKENQDIRLLQAQLQAQKEELQSLLHQPKGLEEENARLREALQQGKTSHQALESELQQLRARLQGLEAN 351
Cdd:COG4372   92 AQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEE 165
 
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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