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Conserved domains on  [gi|530401193|ref|XP_005253890|]
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dynein regulatory complex protein 10 isoform X2 [Homo sapiens]

Protein Classification

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 ...
 393-422 1.46e-06

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: 44.46  E-value: 1.46e-06
                         10        20        30
                 ....*....|....*....|....*....|
gi 530401193 393 AEQEMVRMVRAATLIQALWKGYLVRSLLRS 422
Cdd:cd23767    1 EEEELQRMNRAATLIQALWRGYKVRKELKK 30
SMC_N super family cl47134
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...
 108-410 3.20e-03

RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.


The actual alignment was detected with superfamily member TIGR02169:

Pssm-ID: 481474 [Multi-domain]  Cd Length: 1164  Bit Score: 40.05  E-value: 3.20e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530401193   108 LKEKERQLQEQKEAEEEGWLRDRLLSIELQKSSLsplmQQIKDSTKNVLRLLLsnpQAARLLQMQTQGRSAEAQNfidsl 187
Cdd:TIGR02169  660 RAPRGGILFSRSEPAELQRLRERLEGLKRELSSL----QSELRRIENRLDELS---QELSDASRKIGEIEKEIEQ----- 727

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530401193   188 ielrgfLFEKLLTSPMEARDKAQFLQDISRQNSNNQQIIDTLEKELAERMKNRNAEVEKENfviqELKNHL-HQVLKFSE 266
Cdd:TIGR02169  728 ------LEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALN----DLEARLsHSRIPEIQ 797

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530401193   267 NSLVRTKQEAEKQQKAdFRASQARVAKIQQEILQLQSQFYNLVMENREAEQALRKKKYKVEtEIENWIQKYDTEMGEKQE 346
Cdd:TIGR02169  798 AELSKLEEEVSRIEAR-LREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIE-NLNGKKEELEEELEELEA 875

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 530401193   347 ELEDLDavhrEEKISLEELRRRHKvlvgefAQIREEREINSKKRMEAEQEMVRMVRAATLIQAL 410
Cdd:TIGR02169  876 ALRDLE----SRLGDLKKERDELE------AQLRELERKIEELEAQIEKKRKRLSELKAKLEAL 929
 
Name Accession Description Interval E-value
IQCD cd23767
IQ (isoleucine-glutamine) motif containing D (IQCD); IQCD, also called dynein regulatory ...
 393-422 1.46e-06

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: 44.46  E-value: 1.46e-06
                         10        20        30
                 ....*....|....*....|....*....|
gi 530401193 393 AEQEMVRMVRAATLIQALWKGYLVRSLLRS 422
Cdd:cd23767    1 EEEELQRMNRAATLIQALWRGYKVRKELKK 30
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 108-410 3.20e-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: 40.05  E-value: 3.20e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530401193   108 LKEKERQLQEQKEAEEEGWLRDRLLSIELQKSSLsplmQQIKDSTKNVLRLLLsnpQAARLLQMQTQGRSAEAQNfidsl 187
Cdd:TIGR02169  660 RAPRGGILFSRSEPAELQRLRERLEGLKRELSSL----QSELRRIENRLDELS---QELSDASRKIGEIEKEIEQ----- 727

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530401193   188 ielrgfLFEKLLTSPMEARDKAQFLQDISRQNSNNQQIIDTLEKELAERMKNRNAEVEKENfviqELKNHL-HQVLKFSE 266
Cdd:TIGR02169  728 ------LEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALN----DLEARLsHSRIPEIQ 797

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530401193   267 NSLVRTKQEAEKQQKAdFRASQARVAKIQQEILQLQSQFYNLVMENREAEQALRKKKYKVEtEIENWIQKYDTEMGEKQE 346
Cdd:TIGR02169  798 AELSKLEEEVSRIEAR-LREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIE-NLNGKKEELEEELEELEA 875

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 530401193   347 ELEDLDavhrEEKISLEELRRRHKvlvgefAQIREEREINSKKRMEAEQEMVRMVRAATLIQAL 410
Cdd:TIGR02169  876 ALRDLE----SRLGDLKKERDELE------AQLRELERKIEELEAQIEKKRKRLSELKAKLEAL 929
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 212-410 5.17e-03

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 39.53  E-value: 5.17e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530401193 212 LQDISRQNSNNQQIIDTLEKELAERMK---NRNAEVEKENFVIQELKNHLHQVLKfSENSLVRTKQEAEKQ---QKADFR 285
Cdd:COG1196  234 LRELEAELEELEAELEELEAELEELEAelaELEAELEELRLELEELELELEEAQA-EEYELLAELARLEQDiarLEERRR 312

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530401193 286 ASQARVAKIQQEILQLQSQFYNLVMENREAEQALRKKKYKVETEIENWIQKYDTEMGEKQEELEDLDAVHREEKISLEEL 365
Cdd:COG1196  313 ELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEAL 392

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 530401193 366 RRRHKVLVG-EFAQIREEREINSKKRMEAEQEMVRMVRAATLIQAL 410
Cdd:COG1196  393 RAAAELAAQlEELEEAEEALLERLERLEEELEELEEALAELEEEEE 438
 
Name Accession Description Interval E-value
IQCD cd23767
IQ (isoleucine-glutamine) motif containing D (IQCD); IQCD, also called dynein regulatory ...
 393-422 1.46e-06

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: 44.46  E-value: 1.46e-06
                         10        20        30
                 ....*....|....*....|....*....|
gi 530401193 393 AEQEMVRMVRAATLIQALWKGYLVRSLLRS 422
Cdd:cd23767    1 EEEELQRMNRAATLIQALWRGYKVRKELKK 30
IQCG-IQCD cd21098
IQ (isoleucine-glutamine) motif containing G and D (IQCG and IQCD); IQCG and IQCD belong to ...
 394-418 4.08e-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: 40.43  E-value: 4.08e-05
                         10        20
                 ....*....|....*....|....*
gi 530401193 394 EQEMVRMVRAATLIQALWKGYLVRS 418
Cdd:cd21098    1 QSEDERELWAATKIQALWRGYMVRR 25
Adgb_C_mid-like cd22307
C-terminal middle region of Androglobins (Adgbs) and related proteins; including permuted ...
 375-422 1.19e-04

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: 44.08  E-value: 1.19e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
gi 530401193 375 EFAQIREEREINSKKRMEAEQEMVRMVRAATLIQALWKGYLVRSLLRS 422
Cdd:cd22307  121 SPSSSLREIVEPDECDCRTREPTIEEHEAATKIQAFFRGTLVRKLLKA 168
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 108-410 3.20e-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: 40.05  E-value: 3.20e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530401193   108 LKEKERQLQEQKEAEEEGWLRDRLLSIELQKSSLsplmQQIKDSTKNVLRLLLsnpQAARLLQMQTQGRSAEAQNfidsl 187
Cdd:TIGR02169  660 RAPRGGILFSRSEPAELQRLRERLEGLKRELSSL----QSELRRIENRLDELS---QELSDASRKIGEIEKEIEQ----- 727

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530401193   188 ielrgfLFEKLLTSPMEARDKAQFLQDISRQNSNNQQIIDTLEKELAERMKNRNAEVEKENfviqELKNHL-HQVLKFSE 266
Cdd:TIGR02169  728 ------LEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALN----DLEARLsHSRIPEIQ 797

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530401193   267 NSLVRTKQEAEKQQKAdFRASQARVAKIQQEILQLQSQFYNLVMENREAEQALRKKKYKVEtEIENWIQKYDTEMGEKQE 346
Cdd:TIGR02169  798 AELSKLEEEVSRIEAR-LREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIE-NLNGKKEELEEELEELEA 875

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 530401193   347 ELEDLDavhrEEKISLEELRRRHKvlvgefAQIREEREINSKKRMEAEQEMVRMVRAATLIQAL 410
Cdd:TIGR02169  876 ALRDLE----SRLGDLKKERDELE------AQLRELERKIEELEAQIEKKRKRLSELKAKLEAL 929
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 207-397 4.60e-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: 39.65  E-value: 4.60e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530401193   207 DKAQFLQDISRQNSNNQQIIDTLE-KELAERMKNRNAEVEKENFVIQELKNHLHQV-LKFSE-NSLVRTKQEAEKQQKAD 283
Cdd:TIGR02168  210 EKAERYKELKAELRELELALLVLRlEELREELEELQEELKEAEEELEELTAELQELeEKLEElRLEVSELEEEIEELQKE 289

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530401193   284 FRASQARVAKIQQEILQLQSQFYNLVMENREAEQALRKKKYKVE------TEIENWIQKYDTEMGEKQEELEDLDAVHRE 357
Cdd:TIGR02168  290 LYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDelaeelAELEEKLEELKEELESLEAELEELEAELEE 369

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|
gi 530401193   358 EKISLEELRRRHKVLVGEFAQIREEREINSKKRMEAEQEM 397
Cdd:TIGR02168  370 LESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARL 409
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 212-410 5.17e-03

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 39.53  E-value: 5.17e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530401193 212 LQDISRQNSNNQQIIDTLEKELAERMK---NRNAEVEKENFVIQELKNHLHQVLKfSENSLVRTKQEAEKQ---QKADFR 285
Cdd:COG1196  234 LRELEAELEELEAELEELEAELEELEAelaELEAELEELRLELEELELELEEAQA-EEYELLAELARLEQDiarLEERRR 312

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530401193 286 ASQARVAKIQQEILQLQSQFYNLVMENREAEQALRKKKYKVETEIENWIQKYDTEMGEKQEELEDLDAVHREEKISLEEL 365
Cdd:COG1196  313 ELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEAL 392

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 530401193 366 RRRHKVLVG-EFAQIREEREINSKKRMEAEQEMVRMVRAATLIQAL 410
Cdd:COG1196  393 RAAAELAAQlEELEEAEEALLERLERLEEELEELEEALAELEEEEE 438
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 204-404 7.57e-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: 7.57e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530401193   204 EARDKAQFLQDISRQNSNNQQIIDTLEKElAERMKNRNAEVEKENFVIQELKNHLHQVLKFSENSLVRTKQEAEKQQkAD 283
Cdd:TIGR02168  713 ELEQLRKELEELSRQISALRKDLARLEAE-VEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELE-AQ 790

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530401193   284 FRASQARVAKIQQEILQLQSQFYNL---VMENREAEQALRKKKYKVETEIENWIQKYDT---EMGEKQEELEDLDAVHRE 357
Cdd:TIGR02168  791 IEQLKEELKALREALDELRAELTLLneeAANLRERLESLERRIAATERRLEDLEEQIEElseDIESLAAEIEELEELIEE 870

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*..
gi 530401193   358 EKISLEELRRRHKVLVGEFAQIREEREINSKKRMEAEQEMVRMVRAA 404
Cdd:TIGR02168  871 LESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRREL 917
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 271-412 8.73e-03

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 38.76  E-value: 8.73e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530401193 271 RTKQEAEKQQKADFRASQARVAKIQQEILQLQSQFYNLVMENREAEQALRKKKYKVEtEIENWIQKYDTEMGEKQEELED 350
Cdd:COG1196  242 EELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELA-RLEQDIARLEERRRELEERLEE 320

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 530401193 351 LDAVHREEKISLEELRRRHKVLVGEFAQIREEREINSKKRMEAEQEMVRMVRAATLIQALWK 412
Cdd:COG1196  321 LEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELE 382
 
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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