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Conserved domains on  [gi|755513899|ref|XP_011246549|]
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dynein regulatory complex protein 10 isoform X1 [Mus musculus]

Protein Classification

IQ calmodulin-binding motif-containing protein( domain architecture ID 19230579)

IQ calmodulin-binding motif-containing protein may be involved in cooperative interactions with calmodulins or calmodulin-like proteins

Gene Ontology:  GO:0005516

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
IQCD cd23767
IQ (isoleucine-glutamine) motif containing D (IQCD); IQCD, also called dynein regulatory ...
 390-419 1.61e-07

IQ (isoleucine-glutamine) motif containing D (IQCD); IQCD, also called dynein regulatory complex protein 10 (DRC10), belongs to the IQ motif-containing protein family which contains a C-terminal conserved IQ motif domain and two coiled-coil domains. The IQ motif ([ILV]QxxxRxxxx[RK]), where x stands for any amino-acid residue, interacts with calmodulin (CaM) in a calcium-independent manner and is present in proteins with a wide diversity of biological functions. The IQCD protein was found to primarily accumulate in the acrosome area of round and elongating spermatids of the testis during late stage of spermiogenesis and was then localized to the acrosome and tail regions of mature spermatozoa. The expression of IQCD follows the trajectory of acrosome development during spermatogenesis. IQCD is associated with neuroblastoma and neurodegenerative diseases, and is reported to interact with the nuclear retinoid X receptor in the presence of 9-cis-retinoic acid, thereby activating the transcriptional activity of the receptor.


:

Pssm-ID: 467745 [Multi-domain]  Cd Length: 37  Bit Score: 47.15  E-value: 1.61e-07
                         10        20        30
                 ....*....|....*....|....*....|
gi 755513899 390 AEREMVRMVRAATLIQAVWKGYLVRSILRS 419
Cdd:cd23767    1 EEEELQRMNRAATLIQALWRGYKVRKELKK 30
PTZ00121 super family cl31754
MAEBL; Provisional
 214-393 9.23e-05

MAEBL; Provisional


The actual alignment was detected with superfamily member PTZ00121:

Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 45.13  E-value: 9.23e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755513899  214 RRSERNQEVIDDLQAELANVLKNKESEVEKenfviQELKNHLHQVFKFSENSLLRTKQEAEKQQKVDFRASQVRLA---- 289
Cdd:PTZ00121 1558 KKAEEKKKAEEAKKAEEDKNMALRKAEEAK-----KAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAeeek 1632

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755513899  290 KTQQDILALRAQYHNLVMENREAEQALRKKKYKVETEIENWIQKYDMEMGEKQDEYEDLESIHK--EEKLQLEELRERHA 367
Cdd:PTZ00121 1633 KKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKeaEEAKKAEELKKKEA 1712

                         170       180
                  ....*....|....*....|....*.
gi 755513899  368 VLVEEFSQIRAESEINSKKRVEAERE 393
Cdd:PTZ00121 1713 EEKKKAEELKKAEEENKIKAEEAKKE 1738
 
Name Accession Description Interval E-value
IQCD cd23767
IQ (isoleucine-glutamine) motif containing D (IQCD); IQCD, also called dynein regulatory ...
 390-419 1.61e-07

IQ (isoleucine-glutamine) motif containing D (IQCD); IQCD, also called dynein regulatory complex protein 10 (DRC10), belongs to the IQ motif-containing protein family which contains a C-terminal conserved IQ motif domain and two coiled-coil domains. The IQ motif ([ILV]QxxxRxxxx[RK]), where x stands for any amino-acid residue, interacts with calmodulin (CaM) in a calcium-independent manner and is present in proteins with a wide diversity of biological functions. The IQCD protein was found to primarily accumulate in the acrosome area of round and elongating spermatids of the testis during late stage of spermiogenesis and was then localized to the acrosome and tail regions of mature spermatozoa. The expression of IQCD follows the trajectory of acrosome development during spermatogenesis. IQCD is associated with neuroblastoma and neurodegenerative diseases, and is reported to interact with the nuclear retinoid X receptor in the presence of 9-cis-retinoic acid, thereby activating the transcriptional activity of the receptor.


Pssm-ID: 467745 [Multi-domain]  Cd Length: 37  Bit Score: 47.15  E-value: 1.61e-07
                         10        20        30
                 ....*....|....*....|....*....|
gi 755513899 390 AEREMVRMVRAATLIQAVWKGYLVRSILRS 419
Cdd:cd23767    1 EEEELQRMNRAATLIQALWRGYKVRKELKK 30
PTZ00121 PTZ00121
MAEBL; Provisional
 214-393 9.23e-05

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 45.13  E-value: 9.23e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755513899  214 RRSERNQEVIDDLQAELANVLKNKESEVEKenfviQELKNHLHQVFKFSENSLLRTKQEAEKQQKVDFRASQVRLA---- 289
Cdd:PTZ00121 1558 KKAEEKKKAEEAKKAEEDKNMALRKAEEAK-----KAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAeeek 1632

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755513899  290 KTQQDILALRAQYHNLVMENREAEQALRKKKYKVETEIENWIQKYDMEMGEKQDEYEDLESIHK--EEKLQLEELRERHA 367
Cdd:PTZ00121 1633 KKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKeaEEAKKAEELKKKEA 1712

                         170       180
                  ....*....|....*....|....*.
gi 755513899  368 VLVEEFSQIRAESEINSKKRVEAERE 393
Cdd:PTZ00121 1713 EEKKKAEELKKAEEENKIKAEEAKKE 1738
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 214-401 2.93e-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: 2.93e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755513899 214 RRSERNQEVIDDLQAELANVLKN--KESEVEKENFVIQELKNHLHQVFKFSENSLLRTKQEAEKQQKVDFRASQVRLAKT 291
Cdd:COG1196  182 EATEENLERLEDILGELERQLEPleRQAEKAERYRELKEELKELEAELLLLKLRELEAELEELEAELEELEAELEELEAE 261

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755513899 292 QQDILALRAQYHNLVMENREAEQALRKKKYKVETEIENWIQKYDMEMGEKQDEYEDLESIHKEE----------KLQLEE 361
Cdd:COG1196  262 LAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELaeleeeleelEEELEE 341

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 755513899 362 LRERHAVLVEEFSQIRAESEINSKKRVEAEREMVRMVRAA 401
Cdd:COG1196  342 LEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEEL 381
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 201-393 1.97e-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: 1.97e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755513899  201 EVREKNQFIQDISRRSERNQEVIDDL---QAELANVLKNKESEVEKENFVIQELKNHLHQVfkFSENSLLRTKQEAE--- 274
Cdd:TIGR04523 233 NIEKKQQEINEKTTEISNTQTQLNQLkdeQNKIKKQLSEKQKELEQNNKKIKELEKQLNQL--KSEISDLNNQKEQDwnk 310

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755513899  275 ------KQQKVDFRASQVRLAKTQQ-------DILALRAQYHNLVMENREAEQALRKKKYKVETeIENWIQKYDMEMGEK 341
Cdd:TIGR04523 311 elkselKNQEKKLEEIQNQISQNNKiisqlneQISQLKKELTNSESENSEKQRELEEKQNEIEK-LKKENQSYKQEIKNL 389

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 755513899  342 QDEYEDLESIHKEEKLQLEELRERHAVLVEEFSQIRAESEINSKKRVEAERE 393
Cdd:TIGR04523 390 ESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSE 441
 
Name Accession Description Interval E-value
IQCD cd23767
IQ (isoleucine-glutamine) motif containing D (IQCD); IQCD, also called dynein regulatory ...
 390-419 1.61e-07

IQ (isoleucine-glutamine) motif containing D (IQCD); IQCD, also called dynein regulatory complex protein 10 (DRC10), belongs to the IQ motif-containing protein family which contains a C-terminal conserved IQ motif domain and two coiled-coil domains. The IQ motif ([ILV]QxxxRxxxx[RK]), where x stands for any amino-acid residue, interacts with calmodulin (CaM) in a calcium-independent manner and is present in proteins with a wide diversity of biological functions. The IQCD protein was found to primarily accumulate in the acrosome area of round and elongating spermatids of the testis during late stage of spermiogenesis and was then localized to the acrosome and tail regions of mature spermatozoa. The expression of IQCD follows the trajectory of acrosome development during spermatogenesis. IQCD is associated with neuroblastoma and neurodegenerative diseases, and is reported to interact with the nuclear retinoid X receptor in the presence of 9-cis-retinoic acid, thereby activating the transcriptional activity of the receptor.


Pssm-ID: 467745 [Multi-domain]  Cd Length: 37  Bit Score: 47.15  E-value: 1.61e-07
                         10        20        30
                 ....*....|....*....|....*....|
gi 755513899 390 AEREMVRMVRAATLIQAVWKGYLVRSILRS 419
Cdd:cd23767    1 EEEELQRMNRAATLIQALWRGYKVRKELKK 30
IQCG-IQCD cd21098
IQ (isoleucine-glutamine) motif containing G and D (IQCG and IQCD); IQCG and IQCD belong to ...
 391-415 1.46e-05

IQ (isoleucine-glutamine) motif containing G and D (IQCG and IQCD); IQCG and IQCD belong to the IQ motif-containing protein family which contain a C-terminal conserved IQ (isoleucine-glutamine) motif and a coiled-coil domain. The IQCG protein (also known as DRC9 and CFAP122) is essential for sperm flagellum formation in mice. The IQCD protein (also known as DRC10) is involved in sperm fertilization and the acrosome reaction. Both proteins are components of the nexin-dynein regulatory complex (N-DRC), a key regulator of ciliary/flagellar motility. IQCG and IQCD proteins contain a central coiled-coil domain and a C-terminal IQ (isoleucine-glutamine) motif ([ILV]QxxxRxxxx[RK]), where x stands for any amino-acid residue, that interacts with calmodulin (CaM) in a calcium-independent manner. IQ motif-containing proteins that are known to bind calmodulin (CaM) have a wide diversity of biological functions, and they include neuronal growth proteins, myosins, voltage-operated channels, phosphatases, Ras exchange proteins, sperm surface proteins, Ras Gap-like proteins, spindle-associated proteins, and several proteins in plants.


Pssm-ID: 467743  Cd Length: 25  Bit Score: 41.59  E-value: 1.46e-05
                         10        20
                 ....*....|....*....|....*
gi 755513899 391 EREMVRMVRAATLIQAVWKGYLVRS 415
Cdd:cd21098    1 QSEDERELWAATKIQALWRGYMVRR 25
Adgb_C_mid-like cd22307
C-terminal middle region of Androglobins (Adgbs) and related proteins; including permuted ...
 371-419 4.00e-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: 4.00e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 755513899 371 EEFSQIRAESEINSKKRVEAEREMVRMVRAATLIQAVWKGYLVRSILRS 419
Cdd:cd22307  120 ESPSSSLREIVEPDECDCRTREPTIEEHEAATKIQAFFRGTLVRKLLKA 168
PTZ00121 PTZ00121
MAEBL; Provisional
 214-393 9.23e-05

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 45.13  E-value: 9.23e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755513899  214 RRSERNQEVIDDLQAELANVLKNKESEVEKenfviQELKNHLHQVFKFSENSLLRTKQEAEKQQKVDFRASQVRLA---- 289
Cdd:PTZ00121 1558 KKAEEKKKAEEAKKAEEDKNMALRKAEEAK-----KAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAeeek 1632

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755513899  290 KTQQDILALRAQYHNLVMENREAEQALRKKKYKVETEIENWIQKYDMEMGEKQDEYEDLESIHK--EEKLQLEELRERHA 367
Cdd:PTZ00121 1633 KKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKeaEEAKKAEELKKKEA 1712

                         170       180
                  ....*....|....*....|....*.
gi 755513899  368 VLVEEFSQIRAESEINSKKRVEAERE 393
Cdd:PTZ00121 1713 EEKKKAEELKKAEEENKIKAEEAKKE 1738
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 214-401 2.93e-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: 2.93e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755513899 214 RRSERNQEVIDDLQAELANVLKN--KESEVEKENFVIQELKNHLHQVFKFSENSLLRTKQEAEKQQKVDFRASQVRLAKT 291
Cdd:COG1196  182 EATEENLERLEDILGELERQLEPleRQAEKAERYRELKEELKELEAELLLLKLRELEAELEELEAELEELEAELEELEAE 261

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755513899 292 QQDILALRAQYHNLVMENREAEQALRKKKYKVETEIENWIQKYDMEMGEKQDEYEDLESIHKEE----------KLQLEE 361
Cdd:COG1196  262 LAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELaeleeeleelEEELEE 341

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 755513899 362 LRERHAVLVEEFSQIRAESEINSKKRVEAEREMVRMVRAA 401
Cdd:COG1196  342 LEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEEL 381
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 201-393 1.97e-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: 1.97e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755513899  201 EVREKNQFIQDISRRSERNQEVIDDL---QAELANVLKNKESEVEKENFVIQELKNHLHQVfkFSENSLLRTKQEAE--- 274
Cdd:TIGR04523 233 NIEKKQQEINEKTTEISNTQTQLNQLkdeQNKIKKQLSEKQKELEQNNKKIKELEKQLNQL--KSEISDLNNQKEQDwnk 310

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755513899  275 ------KQQKVDFRASQVRLAKTQQ-------DILALRAQYHNLVMENREAEQALRKKKYKVETeIENWIQKYDMEMGEK 341
Cdd:TIGR04523 311 elkselKNQEKKLEEIQNQISQNNKiisqlneQISQLKKELTNSESENSEKQRELEEKQNEIEK-LKKENQSYKQEIKNL 389

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 755513899  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 2.66e-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: 2.66e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755513899   209 IQDISRRSERNQEVIDDLQAELANVLKNKESEVEKEnfvIQELKnhlhqvfkfSENSLLRTKQEAEKQQKVDfraSQVRL 288
Cdd:TIGR02169  260 ISELEKRLEEIEQLLEELNKKIKDLGEEEQLRVKEK---IGELE---------AEIASLERSIAEKERELED---AEERL 324

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755513899   289 AKTQQDILALRAQYHNLvmenREAEQALRKKKYKVETEIEnwiqkydmemgEKQDEYEDLESihkeeklQLEELRERHAV 368
Cdd:TIGR02169  325 AKLEAEIDKLLAEIEEL----EREIEEERKRRDKLTEEYA-----------ELKEELEDLRA-------ELEEVDKEFAE 382

                          170       180
                   ....*....|....*....|....*....
gi 755513899   369 LVEEFSQIRAESEINSKKRVEAEREMVRM 397
Cdd:TIGR02169  383 TRDELKDYREKLEKLKREINELKRELDRL 411
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 202-393 2.99e-03

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 40.31  E-value: 2.99e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755513899 202 VREKNQFIQDISRRSERNQEVIDDLQaELANVLKNKESEVEKENFVIQELKNhlhqvfkfsENSLLRTKQEAEKQQKVDF 281
Cdd:COG1196  294 LAELARLEQDIARLEERRRELEERLE-ELEEELAELEEELEELEEELEELEE---------ELEEAEEELEEAEAELAEA 363

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755513899 282 RASQVRLAKTQQDILALRAQYHNLVMENREAEQALRKKKYKVETEIENWIQKYDMEMGEKQDEYEDLESIHKEEKLQLEE 361
Cdd:COG1196  364 EEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEA 443

                        170       180       190
                 ....*....|....*....|....*....|..
gi 755513899 362 LRERHAVLVEEFSQIRAESEINSKKRVEAERE 393
Cdd:COG1196  444 LEEAAEEEAELEEEEEALLELLAELLEEAALL 475
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 201-394 6.29e-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: 6.29e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755513899   201 EVREKNQFIQDISRRSERNQEVIDDLQAELANVlknkESEVEKENFVIQELKNHLHQVfKFSENSLLRTKQEAEKQqkvd 280
Cdd:TIGR02168  769 RLEEAEEELAEAEAEIEELEAQIEQLKEELKAL----REALDELRAELTLLNEEAANL-RERLESLERRIAATERR---- 839

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755513899   281 FRASQVRLAKTQQDILALRAQYHNLVMENREAEQALrKKKYKVETEIENWIQKYDMEMGEKQDEYEDLESIHKEEKLQLE 360
Cdd:TIGR02168  840 LEDLEEQIEELSEDIESLAAEIEELEELIEELESEL-EALLNERASLEEALALLRSELEELSEELRELESKRSELRRELE 918

                          170       180       190
                   ....*....|....*....|....*....|....*
gi 755513899   361 ELRERHAVLVEEFSQIRAE-SEINSKKRVEAEREM 394
Cdd:TIGR02168  919 ELREKLAQLELRLEGLEVRiDNLQERLSEEYSLTL 953
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
201-418 7.85e-03

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 38.60  E-value: 7.85e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755513899 201 EVREKNQFIQDISRRSERNQEVIDDLQAelanvLKNKESEVEKEnfvIQELKNHLHQVFKFSENSLLRTKQEAEKQQKVD 280
Cdd:COG4717   72 ELKELEEELKEAEEKEEEYAELQEELEE-----LEEELEELEAE---LEELREELEKLEKLLQLLPLYQELEALEAELAE 143

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755513899 281 FrasQVRLAKTQQDIlalrAQYHNLVMENREAEQALRKKKYKVETEIENWIQKYDMEMGEKQDEYEDLESIHKEEKLQLE 360
Cdd:COG4717  144 L---PERLEELEERL----EELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELE 216

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 755513899 361 ELRERHAVLVEEFSQIRAESEINSKKRVEAEREMVRMVRAATLIQAVWKGYLVRSILR 418
Cdd:COG4717  217 EAQEELEELEEELEQLENELEAAALEERLKEARLLLLIAAALLALLGLGGSLLSLILT 274
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
217-395 8.00e-03

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 38.87  E-value: 8.00e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755513899 217 ERNQEVIDDLQAELANvLKNKESEVEKENFVIQELKNHLHQVFKFSENSLLRTKQEAEKQQKVDFRASQVRLAKTQQDIL 296
Cdd:PRK02224 471 EEDRERVEELEAELED-LEEEVEEVEERLERAEDLVEAEDRIERLEERREDLEELIAERRETIEEKRERAEELRERAAEL 549

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755513899 297 ALRAQ--------YHNLVMENREAEQALRKKKYKVETEIENW---------IQKYDMEMGEKQDEYEDLESIHKEEKLQL 359
Cdd:PRK02224 550 EAEAEekreaaaeAEEEAEEAREEVAELNSKLAELKERIESLerirtllaaIADAEDEIERLREKREALAELNDERRERL 629

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 755513899 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 8.71e-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: 8.71e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755513899   204 EKNQFIQDISRRSERNQEVIDDLQAELANVLKNKES---EVEKENFVIQELKNHLHQVFKFSENslLRTKQeAEKQQKVD 280
Cdd:TIGR02168  320 ELEAQLEELESKLDELAEELAELEEKLEELKEELESleaELEELEAELEELESRLEELEEQLET--LRSKV-AQLELQIA 396

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755513899   281 FRASQVRLAKTQQDILALRAQyhNLVMENREAEQALRkkkykveteiENWIQKYDMEMGEKQDEYEDLESIHKEEKLQLE 360
Cdd:TIGR02168  397 SLNNEIERLEARLERLEDRRE--RLQQEIEELLKKLE----------EAELKELQAELEELEEELEELQEELERLEEALE 464

                          170
                   ....*....|....*....
gi 755513899   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 8.78e-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: 8.78e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755513899   160 PQFTRLLQVQAPGRSPGAQCLLDGLVELRGFLFEKLLTSPMEVREKNQFIQDISRRS---ERNQEVIDDLQAELANVLKN 236
Cdd:TIGR02169  662 PRGGILFSRSEPAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIgeiEKEIEQLEQEEEKLKERLEE 741

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755513899   237 KESEVEKENFVIQELKNHLHQVFKFSENSLLRTKQEAEKQQKVDFRASQVRLAKTQQDILALRAQYHNLVMENREAEQAL 316
Cdd:TIGR02169  742 LEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARLSHSRIPEIQAELSKLEEEVSRIEARLREIEQKL 821

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755513899   317 RKKKYKVETEienwiqkyDMEMGEKQDEYEDLESIHKEEKLQLEELRERHAVLVEEFSQIRAESEINSKKRVEAEREMVR 396
Cdd:TIGR02169  822 NRLTLEKEYL--------EKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDE 893


                   .
gi 755513899   397 M 397
Cdd:TIGR02169  894 L 894
 
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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