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Conserved domains on  [gi|21313054|ref|NP_083684|]
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dynein regulatory complex protein 10 [Mus musculus]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
Smc super family cl34174
Chromosome segregation ATPase [Cell cycle control, cell division, chromosome partitioning];
201-394 8.60e-06

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


The actual alignment was detected with superfamily member COG1196:

Pssm-ID: 224117 [Multi-domain]  Cd Length: 1163  Bit Score: 48.17  E-value: 8.60e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21313054  201 EVREKNQFIQDISRRSERNQEVIDDLQAELANVLKNKESEVEKENFVIQELKNHLHQVFKFSENslLRTKQEAEKQQKVD 280
Cdd:COG1196  731 ELEQLQSRLEELEEELEELEEELEELQERLEELEEELESLEEALAKLKEEIEELEEKRQALQEE--LEELEEELEEAERR 808
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21313054  281 FRASQVRLAKTQQDILALRAQYHNLVMENREAEQALRKKKYKVEtEIENWIQKYDMEMGEKQDEYEDLESIHKEEKLQLE 360
Cdd:COG1196  809 LDALERELESLEQRRERLEQEIEELEEEIEELEEKLDELEEELE-ELEKELEELKEELEELEAEKEELEDELKELEEEKE 887
                        170       180       190
                 ....*....|....*....|....*....|....
gi 21313054  361 ELRERHAVLVEEFSQIRAESEINSKKRVEAEREM 394
Cdd:COG1196  888 ELEEELRELESELAELKEEIEKLRERLEELEAKL 921
Adgb_C_mid-like super family cl41701
C-terminal middle region of Androglobins (Adgbs) and related proteins; including permuted ...
371-419 3.84e-05

C-terminal middle region of Androglobins (Adgbs) and related proteins; including permuted globin domain and IQ motif; Androglobin (Adgb, also known as Calpain-7-like protein, CAPN7L) is a large multidomain protein consisting of an N-terminal peptidase C2 family calpain-like domain, an IQ calmodulin-binding motif, and an internal, circularly permuted globin domain. The canonical secondary structure of hemoglobins is an 3-over-3 alpha-helical sandwich structure, where the eight alpha-helical segments are conventionally labeled, A-H, according to their sequential order; Adgbs differ from this in having helices C-H followed by A-B. Adgbs and other phylogenetically ancient globins, such as neuroglobins and globin X, form hexacoordinated heme iron complexes. Globins contain various highly conserved residues of the heme pocket: including a Phe in the interhelical position CD1 (Phe CD1, first position in the loop between the helices C and D) that is packed against the heme, a His at the 7th position of the E-helix (His E7) that binds the heme iron distally, and a His at the 8th position of the F-helix (His F8) that binds the heme iron proximally. Unlike other hexacoordinated globins, Adgbs have an E7 Gln; their hexacoordination scheme is [Gln]-Fe-[His]. In mammals, Adgb is mainly expressed in the testes and may play an important role in spermatogenesis. Arthropod Adgbs have degenerate globin domains (DOI:10.3389/fgene.2020.00858). This model spans the permuted globin domain, the IQ motif, and a conserved region of about 200 amino acid residues located C-terminal to the globin domain; it does not include the N-terminal protease domain or the large uncharacterized C-terminal domain of approximately 500 residues.


The actual alignment was detected with superfamily member cd22307:

Pssm-ID: 412094  Cd Length: 416  Bit Score: 45.62  E-value: 3.84e-05
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*....
gi 21313054 371 EEFSQIRAESEINSKKRVEAEREMVRMVRAATLIQAVWKGYLVRSILRS 419
Cdd:cd22307 120 ESPSSSLREIVEPDECDCRTREPTIEEHEAATKIQAFFRGTLVRKLLKA 168
 
Name Accession Description Interval E-value
Smc COG1196
Chromosome segregation ATPase [Cell cycle control, cell division, chromosome partitioning];
201-394 8.60e-06

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


Pssm-ID: 224117 [Multi-domain]  Cd Length: 1163  Bit Score: 48.17  E-value: 8.60e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21313054  201 EVREKNQFIQDISRRSERNQEVIDDLQAELANVLKNKESEVEKENFVIQELKNHLHQVFKFSENslLRTKQEAEKQQKVD 280
Cdd:COG1196  731 ELEQLQSRLEELEEELEELEEELEELQERLEELEEELESLEEALAKLKEEIEELEEKRQALQEE--LEELEEELEEAERR 808
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21313054  281 FRASQVRLAKTQQDILALRAQYHNLVMENREAEQALRKKKYKVEtEIENWIQKYDMEMGEKQDEYEDLESIHKEEKLQLE 360
Cdd:COG1196  809 LDALERELESLEQRRERLEQEIEELEEEIEELEEKLDELEEELE-ELEKELEELKEELEELEAEKEELEDELKELEEEKE 887
                        170       180       190
                 ....*....|....*....|....*....|....
gi 21313054  361 ELRERHAVLVEEFSQIRAESEINSKKRVEAEREM 394
Cdd:COG1196  888 ELEEELRELESELAELKEEIEKLRERLEELEAKL 921
Adgb_C_mid-like cd22307
C-terminal middle region of Androglobins (Adgbs) and related proteins; including permuted ...
371-419 3.84e-05

C-terminal middle region of Androglobins (Adgbs) and related proteins; including permuted globin domain and IQ motif; Androglobin (Adgb, also known as Calpain-7-like protein, CAPN7L) is a large multidomain protein consisting of an N-terminal peptidase C2 family calpain-like domain, an IQ calmodulin-binding motif, and an internal, circularly permuted globin domain. The canonical secondary structure of hemoglobins is an 3-over-3 alpha-helical sandwich structure, where the eight alpha-helical segments are conventionally labeled, A-H, according to their sequential order; Adgbs differ from this in having helices C-H followed by A-B. Adgbs and other phylogenetically ancient globins, such as neuroglobins and globin X, form hexacoordinated heme iron complexes. Globins contain various highly conserved residues of the heme pocket: including a Phe in the interhelical position CD1 (Phe CD1, first position in the loop between the helices C and D) that is packed against the heme, a His at the 7th position of the E-helix (His E7) that binds the heme iron distally, and a His at the 8th position of the F-helix (His F8) that binds the heme iron proximally. Unlike other hexacoordinated globins, Adgbs have an E7 Gln; their hexacoordination scheme is [Gln]-Fe-[His]. In mammals, Adgb is mainly expressed in the testes and may play an important role in spermatogenesis. Arthropod Adgbs have degenerate globin domains (DOI:10.3389/fgene.2020.00858). This model spans the permuted globin domain, the IQ motif, and a conserved region of about 200 amino acid residues located C-terminal to the globin domain; it does not include the N-terminal protease domain or the large uncharacterized C-terminal domain of approximately 500 residues.


Pssm-ID: 412094  Cd Length: 416  Bit Score: 45.62  E-value: 3.84e-05
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*....
gi 21313054 371 EEFSQIRAESEINSKKRVEAEREMVRMVRAATLIQAVWKGYLVRSILRS 419
Cdd:cd22307 120 ESPSSSLREIVEPDECDCRTREPTIEEHEAATKIQAFFRGTLVRKLLKA 168
PTZ00121 PTZ00121
MAEBL; Provisional
214-393 8.85e-05

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 45.13  E-value: 8.85e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21313054   214 RRSERNQEVIDDLQAELANVLKNKESEVEKenfviQELKNHLHQVFKFSENSLLRTKQEAEKQQKVDFRASQVRLA---- 289
Cdd:PTZ00121 1558 KKAEEKKKAEEAKKAEEDKNMALRKAEEAK-----KAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAeeek 1632
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21313054   290 KTQQDILALRAQYHNLVMENREAEQALRKKKYKVETEIENWIQKYDMEMGEKQDEYEDLESIHK--EEKLQLEELRERHA 367
Cdd:PTZ00121 1633 KKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKeaEEAKKAEELKKKEA 1712
                         170       180
                  ....*....|....*....|....*.
gi 21313054   368 VLVEEFSQIRAESEINSKKRVEAERE 393
Cdd:PTZ00121 1713 EEKKKAEELKKAEEENKIKAEEAKKE 1738
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
201-393 1.89e-03

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


Pssm-ID: 275316 [Multi-domain]  Cd Length: 745  Bit Score: 40.77  E-value: 1.89e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21313054   201 EVREKNQFIQDISRRSERNQEVIDDL---QAELANVLKNKESEVEKENFVIQELKNHLHQVfkFSENSLLRTKQEAE--- 274
Cdd:TIGR04523 233 NIEKKQQEINEKTTEISNTQTQLNQLkdeQNKIKKQLSEKQKELEQNNKKIKELEKQLNQL--KSEISDLNNQKEQDwnk 310
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21313054   275 ------KQQKVDFRASQVRLAKTQQ-------DILALRAQYHNLVMENREAEQALRKKKYKVETeIENWIQKYDMEMGEK 341
Cdd:TIGR04523 311 elkselKNQEKKLEEIQNQISQNNKiisqlneQISQLKKELTNSESENSEKQRELEEKQNEIEK-LKKENQSYKQEIKNL 389
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 21313054   342 QDEYEDLESIHKEEKLQLEELRERHAVLVEEFSQIRAESEINSKKRVEAERE 393
Cdd:TIGR04523 390 ESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSE 441
 
Name Accession Description Interval E-value
Smc COG1196
Chromosome segregation ATPase [Cell cycle control, cell division, chromosome partitioning];
201-394 8.60e-06

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


Pssm-ID: 224117 [Multi-domain]  Cd Length: 1163  Bit Score: 48.17  E-value: 8.60e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21313054  201 EVREKNQFIQDISRRSERNQEVIDDLQAELANVLKNKESEVEKENFVIQELKNHLHQVFKFSENslLRTKQEAEKQQKVD 280
Cdd:COG1196  731 ELEQLQSRLEELEEELEELEEELEELQERLEELEEELESLEEALAKLKEEIEELEEKRQALQEE--LEELEEELEEAERR 808
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21313054  281 FRASQVRLAKTQQDILALRAQYHNLVMENREAEQALRKKKYKVEtEIENWIQKYDMEMGEKQDEYEDLESIHKEEKLQLE 360
Cdd:COG1196  809 LDALERELESLEQRRERLEQEIEELEEEIEELEEKLDELEEELE-ELEKELEELKEELEELEAEKEELEDELKELEEEKE 887
                        170       180       190
                 ....*....|....*....|....*....|....
gi 21313054  361 ELRERHAVLVEEFSQIRAESEINSKKRVEAEREM 394
Cdd:COG1196  888 ELEEELRELESELAELKEEIEKLRERLEELEAKL 921
Adgb_C_mid-like cd22307
C-terminal middle region of Androglobins (Adgbs) and related proteins; including permuted ...
371-419 3.84e-05

C-terminal middle region of Androglobins (Adgbs) and related proteins; including permuted globin domain and IQ motif; Androglobin (Adgb, also known as Calpain-7-like protein, CAPN7L) is a large multidomain protein consisting of an N-terminal peptidase C2 family calpain-like domain, an IQ calmodulin-binding motif, and an internal, circularly permuted globin domain. The canonical secondary structure of hemoglobins is an 3-over-3 alpha-helical sandwich structure, where the eight alpha-helical segments are conventionally labeled, A-H, according to their sequential order; Adgbs differ from this in having helices C-H followed by A-B. Adgbs and other phylogenetically ancient globins, such as neuroglobins and globin X, form hexacoordinated heme iron complexes. Globins contain various highly conserved residues of the heme pocket: including a Phe in the interhelical position CD1 (Phe CD1, first position in the loop between the helices C and D) that is packed against the heme, a His at the 7th position of the E-helix (His E7) that binds the heme iron distally, and a His at the 8th position of the F-helix (His F8) that binds the heme iron proximally. Unlike other hexacoordinated globins, Adgbs have an E7 Gln; their hexacoordination scheme is [Gln]-Fe-[His]. In mammals, Adgb is mainly expressed in the testes and may play an important role in spermatogenesis. Arthropod Adgbs have degenerate globin domains (DOI:10.3389/fgene.2020.00858). This model spans the permuted globin domain, the IQ motif, and a conserved region of about 200 amino acid residues located C-terminal to the globin domain; it does not include the N-terminal protease domain or the large uncharacterized C-terminal domain of approximately 500 residues.


Pssm-ID: 412094  Cd Length: 416  Bit Score: 45.62  E-value: 3.84e-05
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*....
gi 21313054 371 EEFSQIRAESEINSKKRVEAEREMVRMVRAATLIQAVWKGYLVRSILRS 419
Cdd:cd22307 120 ESPSSSLREIVEPDECDCRTREPTIEEHEAATKIQAFFRGTLVRKLLKA 168
PTZ00121 PTZ00121
MAEBL; Provisional
214-393 8.85e-05

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 45.13  E-value: 8.85e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21313054   214 RRSERNQEVIDDLQAELANVLKNKESEVEKenfviQELKNHLHQVFKFSENSLLRTKQEAEKQQKVDFRASQVRLA---- 289
Cdd:PTZ00121 1558 KKAEEKKKAEEAKKAEEDKNMALRKAEEAK-----KAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAeeek 1632
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21313054   290 KTQQDILALRAQYHNLVMENREAEQALRKKKYKVETEIENWIQKYDMEMGEKQDEYEDLESIHK--EEKLQLEELRERHA 367
Cdd:PTZ00121 1633 KKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKeaEEAKKAEELKKKEA 1712
                         170       180
                  ....*....|....*....|....*.
gi 21313054   368 VLVEEFSQIRAESEINSKKRVEAERE 393
Cdd:PTZ00121 1713 EEKKKAEELKKAEEENKIKAEEAKKE 1738
Smc COG1196
Chromosome segregation ATPase [Cell cycle control, cell division, chromosome partitioning];
201-406 2.43e-04

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


Pssm-ID: 224117 [Multi-domain]  Cd Length: 1163  Bit Score: 43.55  E-value: 2.43e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21313054  201 EVREKNQFIQDISRRSERNQEVIDDLQAELANVLKNKESEVEKENFVIQELKNHLHQVFK--FSENSLLRTKQEAEKQQK 278
Cdd:COG1196  713 ELERQLEELKRELAALEEELEQLQSRLEELEEELEELEEELEELQERLEELEEELESLEEalAKLKEEIEELEEKRQALQ 792
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21313054  279 VDFRASQVRLAKTQQDILALRAQYHNLVMENREAEQALRKKKYKVEtEIENWIQKYDMEMGEKQDEYEDLESIHKEEKLQ 358
Cdd:COG1196  793 EELEELEEELEEAERRLDALERELESLEQRRERLEQEIEELEEEIE-ELEEKLDELEEELEELEKELEELKEELEELEAE 871
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 21313054  359 LEELRERHAVLVEEFSQIRAESEINSKKRVEAEREMVRMVRAATLIQA 406
Cdd:COG1196  872 KEELEDELKELEEEKEELEEELRELESELAELKEEIEKLRERLEELEA 919
Smc COG1196
Chromosome segregation ATPase [Cell cycle control, cell division, chromosome partitioning];
201-406 5.55e-04

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


Pssm-ID: 224117 [Multi-domain]  Cd Length: 1163  Bit Score: 42.39  E-value: 5.55e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21313054  201 EVREKNQFIQDISRRSERNQEVIDDLQAELANVLKNKESEVEKENFVIQELKNHLHQVFKF--SENSLLRTKQEAEKQQK 278
Cdd:COG1196  299 ELEGEISLLRERLEELENELEELEERLEELKEKIEALKEELEERETLLEELEQLLAELEEAkeELEEKLSALLEELEELF 378
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21313054  279 VDFRASQVRLAKTQQDILA----LRAQYHNLVMENREAEQALRKKKYKVEtEIENWIQKYDMEMGEKQDEYEDLESIHKE 354
Cdd:COG1196  379 EALREELAELEAELAEIRNeleeLKREIESLEERLERLSERLEDLKEELK-ELEAELEELQTELEELNEELEELEEQLEE 457
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 21313054  355 EKLQLEELRERHAVLVEEFSQIRAESEINSKK--RVEAEREMVRMVRAATLIQA 406
Cdd:COG1196  458 LRDRLKELERELAELQEELQRLEKELSSLEARldRLEAEQRASQGVRAVLEALE 511
Smc COG1196
Chromosome segregation ATPase [Cell cycle control, cell division, chromosome partitioning];
201-393 1.56e-03

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


Pssm-ID: 224117 [Multi-domain]  Cd Length: 1163  Bit Score: 41.24  E-value: 1.56e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21313054  201 EVREKNQFIQDISRRSERNQEVIDDLQAELANvLKNKESEVEKEnfviqelKNHLHQVFKFSENSLLRtKQEAEKQQKVD 280
Cdd:COG1196  261 ELEEAEKEIEELKSELEELREELEELQEELLE-LKEEIEELEGE-------ISLLRERLEELENELEE-LEERLEELKEK 331
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21313054  281 FRASQVRLAKTQQDILALRAQYHNLVMENREAEQALRKKKYKVETEIENWIQKYD---MEMGEKQDEYEDLESIHKEEKL 357
Cdd:COG1196  332 IEALKEELEERETLLEELEQLLAELEEAKEELEEKLSALLEELEELFEALREELAeleAELAEIRNELEELKREIESLEE 411
                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 21313054  358 QLEELRERHAVLVEEFSQIRAESEINSKKRVEAERE 393
Cdd:COG1196  412 RLERLSERLEDLKEELKELEAELEELQTELEELNEE 447
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
201-393 1.89e-03

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


Pssm-ID: 275316 [Multi-domain]  Cd Length: 745  Bit Score: 40.77  E-value: 1.89e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21313054   201 EVREKNQFIQDISRRSERNQEVIDDL---QAELANVLKNKESEVEKENFVIQELKNHLHQVfkFSENSLLRTKQEAE--- 274
Cdd:TIGR04523 233 NIEKKQQEINEKTTEISNTQTQLNQLkdeQNKIKKQLSEKQKELEQNNKKIKELEKQLNQL--KSEISDLNNQKEQDwnk 310
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21313054   275 ------KQQKVDFRASQVRLAKTQQ-------DILALRAQYHNLVMENREAEQALRKKKYKVETeIENWIQKYDMEMGEK 341
Cdd:TIGR04523 311 elkselKNQEKKLEEIQNQISQNNKiisqlneQISQLKKELTNSESENSEKQRELEEKQNEIEK-LKKENQSYKQEIKNL 389
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 21313054   342 QDEYEDLESIHKEEKLQLEELRERHAVLVEEFSQIRAESEINSKKRVEAERE 393
Cdd:TIGR04523 390 ESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSE 441
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
209-397 2.55e-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: 2.55e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21313054    209 IQDISRRSERNQEVIDDLQAELANVLKNKESEVEKEnfvIQELKnhlhqvfkfSENSLLRTKQEAEKQQKVDfraSQVRL 288
Cdd:TIGR02169  260 ISELEKRLEEIEQLLEELNKKIKDLGEEEQLRVKEK---IGELE---------AEIASLERSIAEKERELED---AEERL 324
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21313054    289 AKTQQDILALRAQYHNLvmenREAEQALRKKKYKVETEIEnwiqkydmemgEKQDEYEDLESihkeeklQLEELRERHAV 368
Cdd:TIGR02169  325 AKLEAEIDKLLAEIEEL----EREIEEERKRRDKLTEEYA-----------ELKEELEDLRA-------ELEEVDKEFAE 382
                          170       180
                   ....*....|....*....|....*....
gi 21313054    369 LVEEFSQIRAESEINSKKRVEAEREMVRM 397
Cdd:TIGR02169  383 TRDELKDYREKLEKLKREINELKRELDRL 411
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
201-394 6.03e-03

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 39.27  E-value: 6.03e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21313054    201 EVREKNQFIQDISRRSERNQEVIDDLQAELANVlknkESEVEKENFVIQELKNHLHQVfKFSENSLLRTKQEAEKQqkvd 280
Cdd:TIGR02168  769 RLEEAEEELAEAEAEIEELEAQIEQLKEELKAL----REALDELRAELTLLNEEAANL-RERLESLERRIAATERR---- 839
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21313054    281 FRASQVRLAKTQQDILALRAQYHNLVMENREAEQALrKKKYKVETEIENWIQKYDMEMGEKQDEYEDLESIHKEEKLQLE 360
Cdd:TIGR02168  840 LEDLEEQIEELSEDIESLAAEIEELEELIEELESEL-EALLNERASLEEALALLRSELEELSEELRELESKRSELRRELE 918
                          170       180       190
                   ....*....|....*....|....*....|....*
gi 21313054    361 ELRERHAVLVEEFSQIRAE-SEINSKKRVEAEREM 394
Cdd:TIGR02168  919 ELREKLAQLELRLEGLEVRiDNLQERLSEEYSLTL 953
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
217-395 7.67e-03

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 38.87  E-value: 7.67e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21313054  217 ERNQEVIDDLQAELANvLKNKESEVEKENFVIQELKNHLHQVFKFSENSLLRTKQEAEKQQKVDFRASQVRLAKTQQDIL 296
Cdd:PRK02224 471 EEDRERVEELEAELED-LEEEVEEVEERLERAEDLVEAEDRIERLEERREDLEELIAERRETIEEKRERAEELRERAAEL 549
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21313054  297 ALRAQ--------YHNLVMENREAEQALRKKKYKVETEIENW---------IQKYDMEMGEKQDEYEDLESIHKEEKLQL 359
Cdd:PRK02224 550 EAEAEekreaaaeAEEEAEEAREEVAELNSKLAELKERIESLerirtllaaIADAEDEIERLREKREALAELNDERRERL 629
                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 21313054  360 EELRERHAVLVEEFSQIRAESEINSKKRVEAEREMV 395
Cdd:PRK02224 630 AEKRERKRELEAEFDEARIEEAREDKERAEEYLEQV 665
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
204-379 8.35e-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: 38.88  E-value: 8.35e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21313054    204 EKNQFIQDISRRSERNQEVIDDLQAELANVLKNKES---EVEKENFVIQELKNHLHQVFKFSENslLRTKQeAEKQQKVD 280
Cdd:TIGR02168  320 ELEAQLEELESKLDELAEELAELEEKLEELKEELESleaELEELEAELEELESRLEELEEQLET--LRSKV-AQLELQIA 396
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21313054    281 FRASQVRLAKTQQDILALRAQyhNLVMENREAEQALRkkkykveteiENWIQKYDMEMGEKQDEYEDLESIHKEEKLQLE 360
Cdd:TIGR02168  397 SLNNEIERLEARLERLEDRRE--RLQQEIEELLKKLE----------EAELKELQAELEELEEELEELQEELERLEEALE 464
                          170
                   ....*....|....*....
gi 21313054    361 ELRERHAVLVEEFSQIRAE 379
Cdd:TIGR02168  465 ELREELEEAEQALDAAERE 483
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
160-397 8.42e-03

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 38.51  E-value: 8.42e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21313054    160 PQFTRLLQVQAPGRSPGAQCLLDGLVELRGFLFEKLLTSPMEVREKNQFIQDISRRS---ERNQEVIDDLQAELANVLKN 236
Cdd:TIGR02169  662 PRGGILFSRSEPAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIgeiEKEIEQLEQEEEKLKERLEE 741
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21313054    237 KESEVEKENFVIQELKNHLHQVFKFSENSLLRTKQEAEKQQKVDFRASQVRLAKTQQDILALRAQYHNLVMENREAEQAL 316
Cdd:TIGR02169  742 LEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARLSHSRIPEIQAELSKLEEEVSRIEARLREIEQKL 821
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21313054    317 RKKKYKVETEienwiqkyDMEMGEKQDEYEDLESIHKEEKLQLEELRERHAVLVEEFSQIRAESEINSKKRVEAEREMVR 396
Cdd:TIGR02169  822 NRLTLEKEYL--------EKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDE 893

                   .
gi 21313054    397 M 397
Cdd:TIGR02169  894 L 894
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.20
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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