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Conserved domains on  [gi|2024358976|ref|XP_015150417|]
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dynein regulatory complex protein 10 isoform X1 [Gallus gallus]

Protein Classification

coiled-coil domain-containing protein( domain architecture ID 1000037)

coiled-coil domain-containing protein contains a region with alpha-helical coiled-coil sequence signatures that is being annotated by a variety of protein family models, not necessarily indicating family membership

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Smc super family cl34174
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 159-379 1.77e-04

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


The actual alignment was detected with superfamily member COG1196:

Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 43.77  E-value: 1.77e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024358976 159 LERLLTSPTKEEETVQLMEDISLRINKNTETITALQAELAAAIRAQDEEIQNKDNMIKDLKNSMEILDEccKDNILQVKW 238
Cdd:COG1196   290 EYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEA--ELAEAEEAL 367

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024358976 239 EGEKQQKEELRASQARCARLQQNIQQLEAQFNKLVLEHRASELALRKRKCRLETEILNwIQAYDTDMAEKQAEFEEVHAA 318
Cdd:COG1196   368 LEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEE-LEEALAELEEEEEEEEEALEE 446

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2024358976 319 YTKEKAELSLLMEKHAVLLQEYSQIEEERRINEEKKKQALEELAVLTLAATRIQAFWRGYL 379
Cdd:COG1196   447 AAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFL 507
 
Name Accession Description Interval E-value
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 159-379 1.77e-04

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 43.77  E-value: 1.77e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024358976 159 LERLLTSPTKEEETVQLMEDISLRINKNTETITALQAELAAAIRAQDEEIQNKDNMIKDLKNSMEILDEccKDNILQVKW 238
Cdd:COG1196   290 EYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEA--ELAEAEEAL 367

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024358976 239 EGEKQQKEELRASQARCARLQQNIQQLEAQFNKLVLEHRASELALRKRKCRLETEILNwIQAYDTDMAEKQAEFEEVHAA 318
Cdd:COG1196   368 LEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEE-LEEALAELEEEEEEEEEALEE 446

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2024358976 319 YTKEKAELSLLMEKHAVLLQEYSQIEEERRINEEKKKQALEELAVLTLAATRIQAFWRGYL 379
Cdd:COG1196   447 AAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFL 507
IQCD cd23767
IQ (isoleucine-glutamine) motif containing D (IQCD); IQCD, also called dynein regulatory ...
 357-381 2.78e-04

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: 37.91  E-value: 2.78e-04
                          10        20
                  ....*....|....*....|....*
gi 2024358976 357 ALEELAVLTLAATRIQAFWRGYLIR 381
Cdd:cd23767     1 EEEELQRMNRAATLIQALWRGYKVR 25
CCDC22 pfam05667
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 ...
 239-364 1.67e-03

Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 (CCDC22) is involved in regulation of NF-kappa-B signalling; the function may involve association with COMMD8 and a CUL1-dependent E3 ubiquitin ligase complex. It is part of the OMMD/CCDC22/CCDC93 (CCC) complex, which interacts with the multisubunit WASH complex required for endosomal deposition of F-actin and cargo trafficking in conjunction with the retromer. This entry also includes CCDC22 homologs from animals and plants.


Pssm-ID: 461708 [Multi-domain]  Cd Length: 600  Bit Score: 40.40  E-value: 1.67e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024358976 239 EGEKQQKEELRASQARCARLQQNIQQLEAQFNKLVLEHRASELALRKRK---CRLETEILNWIQAYD------TDMAEKQ 309
Cdd:pfam05667 328 ELQQQREEELEELQEQLEDLESSIQELEKEIKKLESSIKQVEEELEELKeqnEELEKQYKVKKKTLDllpdaeENIAKLQ 407

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2024358976 310 AEFEEVhaayTKEKAELSLLMEKHAV-LLQEYSQIEEERRINEEKKKQALEELAVL 364
Cdd:pfam05667 408 ALVDAS----AQRLVELAGQWEKHRVpLIEEYRALKEAKSNKEDESQRKLEEIKEL 459
IQ smart00015
Calmodulin-binding motif; Short calmodulin-binding motif containing conserved Ile and Gln ...
 364-384 5.40e-03

Calmodulin-binding motif; Short calmodulin-binding motif containing conserved Ile and Gln residues.


Pssm-ID: 197470 [Multi-domain]  Cd Length: 23  Bit Score: 34.22  E-value: 5.40e-03
                           10        20
                   ....*....|....*....|.
gi 2024358976  364 LTLAATRIQAFWRGYLIRSTF 384
Cdd:smart00015   2 LTRAAIIIQAAWRGYLARKRY 22
 
Name Accession Description Interval E-value
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 159-379 1.77e-04

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 43.77  E-value: 1.77e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024358976 159 LERLLTSPTKEEETVQLMEDISLRINKNTETITALQAELAAAIRAQDEEIQNKDNMIKDLKNSMEILDEccKDNILQVKW 238
Cdd:COG1196   290 EYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEA--ELAEAEEAL 367

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024358976 239 EGEKQQKEELRASQARCARLQQNIQQLEAQFNKLVLEHRASELALRKRKCRLETEILNwIQAYDTDMAEKQAEFEEVHAA 318
Cdd:COG1196   368 LEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEE-LEEALAELEEEEEEEEEALEE 446

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2024358976 319 YTKEKAELSLLMEKHAVLLQEYSQIEEERRINEEKKKQALEELAVLTLAATRIQAFWRGYL 379
Cdd:COG1196   447 AAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFL 507
IQCD cd23767
IQ (isoleucine-glutamine) motif containing D (IQCD); IQCD, also called dynein regulatory ...
 357-381 2.78e-04

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: 37.91  E-value: 2.78e-04
                          10        20
                  ....*....|....*....|....*
gi 2024358976 357 ALEELAVLTLAATRIQAFWRGYLIR 381
Cdd:cd23767     1 EEEELQRMNRAATLIQALWRGYKVR 25
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
154-361 1.44e-03

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 41.05  E-value: 1.44e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024358976  154 FRNFMLERlltSPTKE--EETVQLMEDISlRINKNTETITAlQAELAAAIRAQDEEIQnkdnmikDLKNSMEILDECckD 231
Cdd:COG4913    213 VREYMLEE---PDTFEaaDALVEHFDDLE-RAHEALEDARE-QIELLEPIRELAERYA-------AARERLAELEYL--R 278

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024358976  232 NILQVkWEGEKQQ---KEELRASQARCARLQQNIQQLEAQFNKLVLEHRASELALR----KRKCRLETEILNWIQAYDtD 304
Cdd:COG4913    279 AALRL-WFAQRRLellEAELEELRAELARLEAELERLEARLDALREELDELEAQIRgnggDRLEQLEREIERLERELE-E 356

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2024358976  305 MAEKQAEFEE----VHAAYTKEKAELSLLMEKHAVLLQEYSQIEEERRINEEKKKQALEEL 361
Cdd:COG4913    357 RERRRARLEAllaaLGLPLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDL 417
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 177-373 1.52e-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: 1.52e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024358976 177 EDISLRINKNTETITALQAELAAAIRAQDEEIQNKDNMIKDLKNSMEILDEcckdnilqvkwegekqQKEELRASQARCA 256
Cdd:COG1196   270 EELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEE----------------LEEELAELEEELE 333

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024358976 257 RLQQNIQQLEAQFNKLVLEHRASELALRKRKCRLETEILNWIQAYDTDMAEKQAEFEEVHAAYTKEKAELSLLmEKHAVL 336
Cdd:COG1196   334 ELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELE-EAEEAL 412

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 2024358976 337 LQEYSQIEEERRINEEKKKQALEELAVLTLAATRIQA 373
Cdd:COG1196   413 LERLERLEEELEELEEALAELEEEEEEEEEALEEAAE 449
CCDC22 pfam05667
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 ...
 239-364 1.67e-03

Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 (CCDC22) is involved in regulation of NF-kappa-B signalling; the function may involve association with COMMD8 and a CUL1-dependent E3 ubiquitin ligase complex. It is part of the OMMD/CCDC22/CCDC93 (CCC) complex, which interacts with the multisubunit WASH complex required for endosomal deposition of F-actin and cargo trafficking in conjunction with the retromer. This entry also includes CCDC22 homologs from animals and plants.


Pssm-ID: 461708 [Multi-domain]  Cd Length: 600  Bit Score: 40.40  E-value: 1.67e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024358976 239 EGEKQQKEELRASQARCARLQQNIQQLEAQFNKLVLEHRASELALRKRK---CRLETEILNWIQAYD------TDMAEKQ 309
Cdd:pfam05667 328 ELQQQREEELEELQEQLEDLESSIQELEKEIKKLESSIKQVEEELEELKeqnEELEKQYKVKKKTLDllpdaeENIAKLQ 407

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2024358976 310 AEFEEVhaayTKEKAELSLLMEKHAV-LLQEYSQIEEERRINEEKKKQALEELAVL 364
Cdd:pfam05667 408 ALVDAS----AQRLVELAGQWEKHRVpLIEEYRALKEAKSNKEDESQRKLEEIKEL 459
IQ smart00015
Calmodulin-binding motif; Short calmodulin-binding motif containing conserved Ile and Gln ...
 364-384 5.40e-03

Calmodulin-binding motif; Short calmodulin-binding motif containing conserved Ile and Gln residues.


Pssm-ID: 197470 [Multi-domain]  Cd Length: 23  Bit Score: 34.22  E-value: 5.40e-03
                           10        20
                   ....*....|....*....|.
gi 2024358976  364 LTLAATRIQAFWRGYLIRSTF 384
Cdd:smart00015   2 LTRAAIIIQAAWRGYLARKRY 22
 
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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