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Conserved domains on  [gi|157818155|ref|NP_001099699|]
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centrosomal protein CCDC61 [Rattus norvegicus]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
HD_CCDC61_N cd22284
N-terminal head domain found in coiled-coil domain-containing protein 61 and similar proteins; ...
 7-139 4.21e-74

N-terminal head domain found in coiled-coil domain-containing protein 61 and similar proteins; Coiled-coil domain-containing protein 61 (CCDC61), also known as variable flagellar number 3 (VFL3), is a centrosomal protein required for spindle assembly and precise chromosome alignments in mitosis. It is the human ortholog of proteins required for anchoring distinct sets of cytoskeletal fibers to centrioles in unicellular eukaryotes. CCDC61 monomers are comprised of an N-terminal globular head domain, a centrally located coiled-coil, and a C-terminal region. These monomers homodimerize through two homodimerization domains, the N-terminal globular head domains and long extended alpha-helical coiled-coil regions. These CCDC61 homodimers assembles into linear filaments. This model corresponds to the N-terminal head domain of CCDC61, which is structurally related to other XRCC4-superfamily members, XRCC4, XLF, SAS6, and PAXX.


:

Pssm-ID: 409001  Cd Length: 135  Bit Score: 230.57  E-value: 4.21e-74
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818155   7 LQVDYMFRGVEHAVRV-VVSGQVLELEVEDRMTADQWRGEFDANFIEDLTHKTGNFKQFSIFCNMLESALTQSSESVTLD 85
Cdd:cd22284    2 ISAELTFRGVEYLVTLkVDEGESLSVEVEDKDTGERWRGSFTASYIEELTRKTGNFKKFSVFVKMLKSALLKTSESVSLD 81

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 157818155  86 LLTYTDLESLRSRKLGGRPGPCPRSAQLNSKRYLILIYSVEFDRIHYPLPLPYQ 139
Cdd:cd22284   82 LLTYQDLEELRNRKSGGSSRNSASSSDLNNKRYLILTYTVEFDRVHYPLPLPYV 135
Smc super family cl34174
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 147-319 3.87e-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: 43.39  E-value: 3.87e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818155 147 LQGIIRSLKEELGHLrgmnggqdarETEIWHLREQVTRLASEKRELEAQLGRSREEALAGRAARQEAESLRGLVRGLELE 226
Cdd:COG1196  300 LEQDIARLEERRREL----------EERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLE 369

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818155 227 LRQERGLGGRAAGRRSQDCRRLAKELEEVKASERNLRARLKTLNCELAMYRRGRRTLPAGAREDRALSSRERSTSRGRTA 306
Cdd:COG1196  370 AEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAE 449

                        170
                 ....*....|...
gi 157818155 307 TRSSSRESNRGAR 319
Cdd:COG1196  450 EEAELEEEEEALL 462
 
Name Accession Description Interval E-value
HD_CCDC61_N cd22284
N-terminal head domain found in coiled-coil domain-containing protein 61 and similar proteins; ...
 7-139 4.21e-74

N-terminal head domain found in coiled-coil domain-containing protein 61 and similar proteins; Coiled-coil domain-containing protein 61 (CCDC61), also known as variable flagellar number 3 (VFL3), is a centrosomal protein required for spindle assembly and precise chromosome alignments in mitosis. It is the human ortholog of proteins required for anchoring distinct sets of cytoskeletal fibers to centrioles in unicellular eukaryotes. CCDC61 monomers are comprised of an N-terminal globular head domain, a centrally located coiled-coil, and a C-terminal region. These monomers homodimerize through two homodimerization domains, the N-terminal globular head domains and long extended alpha-helical coiled-coil regions. These CCDC61 homodimers assembles into linear filaments. This model corresponds to the N-terminal head domain of CCDC61, which is structurally related to other XRCC4-superfamily members, XRCC4, XLF, SAS6, and PAXX.


Pssm-ID: 409001  Cd Length: 135  Bit Score: 230.57  E-value: 4.21e-74
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818155   7 LQVDYMFRGVEHAVRV-VVSGQVLELEVEDRMTADQWRGEFDANFIEDLTHKTGNFKQFSIFCNMLESALTQSSESVTLD 85
Cdd:cd22284    2 ISAELTFRGVEYLVTLkVDEGESLSVEVEDKDTGERWRGSFTASYIEELTRKTGNFKKFSVFVKMLKSALLKTSESVSLD 81

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 157818155  86 LLTYTDLESLRSRKLGGRPGPCPRSAQLNSKRYLILIYSVEFDRIHYPLPLPYQ 139
Cdd:cd22284   82 LLTYQDLEELRNRKSGGSSRNSASSSDLNNKRYLILTYTVEFDRVHYPLPLPYV 135
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 147-319 3.87e-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: 3.87e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818155 147 LQGIIRSLKEELGHLrgmnggqdarETEIWHLREQVTRLASEKRELEAQLGRSREEALAGRAARQEAESLRGLVRGLELE 226
Cdd:COG1196  300 LEQDIARLEERRREL----------EERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLE 369

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818155 227 LRQERGLGGRAAGRRSQDCRRLAKELEEVKASERNLRARLKTLNCELAMYRRGRRTLPAGAREDRALSSRERSTSRGRTA 306
Cdd:COG1196  370 AEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAE 449

                        170
                 ....*....|...
gi 157818155 307 TRSSSRESNRGAR 319
Cdd:COG1196  450 EEAELEEEEEALL 462
PspA_IM30 pfam04012
PspA/IM30 family; This family includes PspA a protein that suppresses sigma54-dependent ...
 143-268 7.42e-04

PspA/IM30 family; This family includes PspA a protein that suppresses sigma54-dependent transcription. The PspA protein, a negative regulator of the Escherichia coli phage shock psp operon, is produced when virulence factors are exported through secretins in many Gram-negative pathogenic bacteria and its homolog in plants, VIPP1, plays a critical role in thylakoid biogenesis, essential for photosynthesis. Activation of transcription by the enhancer-dependent bacterial sigma(54) containing RNA polymerase occurs through ATP hydrolysis-driven protein conformational changes enabled by activator proteins that belong to the large AAA(+) mechanochemical protein family. It has been shown that PspA directly and specifically acts upon and binds to the AAA(+) domain of the PspF transcription activator.


Pssm-ID: 461130 [Multi-domain]  Cd Length: 215  Bit Score: 41.20  E-value: 7.42e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818155  143 DP-VVLQGIIRSLKEELGHLRGMNGGQDARETEIWHLREQVTRLAsEKRELEAQLGRSR-EEALAgRAARQEAESLRGLV 220
Cdd:pfam04012  22 DPeKMLEQAIRDMQSELVKARQALAQTIARQKQLERRLEQQTEQA-KKLEEKAQAALTKgNEELA-REALAEKKSLEKQA 99

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 157818155  221 RGLELELRQERGLggrAAGRRSQdCRRLAKELEEVKASERNLRARLKT 268
Cdd:pfam04012 100 EALETQLAQQRSA---VEQLRKQ-LAALETKIQQLKAKKNLLKARLKA 143
 
Name Accession Description Interval E-value
HD_CCDC61_N cd22284
N-terminal head domain found in coiled-coil domain-containing protein 61 and similar proteins; ...
 7-139 4.21e-74

N-terminal head domain found in coiled-coil domain-containing protein 61 and similar proteins; Coiled-coil domain-containing protein 61 (CCDC61), also known as variable flagellar number 3 (VFL3), is a centrosomal protein required for spindle assembly and precise chromosome alignments in mitosis. It is the human ortholog of proteins required for anchoring distinct sets of cytoskeletal fibers to centrioles in unicellular eukaryotes. CCDC61 monomers are comprised of an N-terminal globular head domain, a centrally located coiled-coil, and a C-terminal region. These monomers homodimerize through two homodimerization domains, the N-terminal globular head domains and long extended alpha-helical coiled-coil regions. These CCDC61 homodimers assembles into linear filaments. This model corresponds to the N-terminal head domain of CCDC61, which is structurally related to other XRCC4-superfamily members, XRCC4, XLF, SAS6, and PAXX.


Pssm-ID: 409001  Cd Length: 135  Bit Score: 230.57  E-value: 4.21e-74
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818155   7 LQVDYMFRGVEHAVRV-VVSGQVLELEVEDRMTADQWRGEFDANFIEDLTHKTGNFKQFSIFCNMLESALTQSSESVTLD 85
Cdd:cd22284    2 ISAELTFRGVEYLVTLkVDEGESLSVEVEDKDTGERWRGSFTASYIEELTRKTGNFKKFSVFVKMLKSALLKTSESVSLD 81

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 157818155  86 LLTYTDLESLRSRKLGGRPGPCPRSAQLNSKRYLILIYSVEFDRIHYPLPLPYQ 139
Cdd:cd22284   82 LLTYQDLEELRNRKSGGSSRNSASSSDLNNKRYLILTYTVEFDRVHYPLPLPYV 135
HD_XRCC4-like_N cd22210
N-terminal head domain found in the XRCC4 superfamily of proteins; The XRCC4 superfamily ...
 15-138 3.54e-15

N-terminal head domain found in the XRCC4 superfamily of proteins; The XRCC4 superfamily includes five families: XRCC4, XLF, PAXX, SAS6 and CCDC61. XRCC4 (X-ray repair cross-complementing protein 4), XLF (XRCC4-like factor) and PAXX (paralog of XRCC4 and XLF) play crucial roles in the non-homologous end-joining (NHEJ) DNA repair pathway. SAS6 (spindle assembly abnormal protein 6) and CCDC61 (coiled-coil domain-containing protein 61) have a centrosomal/centriolar function. Members of this superfamily have an N-terminal globular head domain, a centrally located coiled-coil, and a C-terminal low-complexity region. They form homodimers through two homodimerization domains: an N-terminal globular head domain and a parallel coiled-coil domain. In addition, some members such as XRCC4 and XLF form symmetric heterodimers that interact through their globular head domains at the opposite end of the homodimer interface, and may form XLF-XRCC4 filaments. This model corresponds to the N-terminal head domain of XRCC4 superfamily proteins.


Pssm-ID: 408999  Cd Length: 115  Bit Score: 71.80  E-value: 3.54e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818155  15 GVEHAVRV---VVSGQVLELEVEDrmTADQWRGEFDANFIEDLTHKTGNFKQFSIFCNMLESALTQS---SESVTLDLLT 88
Cdd:cd22210   11 LEELTFKVeteVANERGLRLHVSD--DAFLWTGEVSESDISQLKNDQGILVDFASFPGKLRSALEKCilaSDRFTFVLTI 88

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 157818155  89 YTDleslrsrklggrpgpcprsaqlnsKRYLILIYSVEFDRIHYPLPLPY 138
Cdd:cd22210   89 RGD------------------------EAYLKLVEILDEQLPHITFALRK 114
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 147-319 3.87e-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: 3.87e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818155 147 LQGIIRSLKEELGHLrgmnggqdarETEIWHLREQVTRLASEKRELEAQLGRSREEALAGRAARQEAESLRGLVRGLELE 226
Cdd:COG1196  300 LEQDIARLEERRREL----------EERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLE 369

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818155 227 LRQERGLGGRAAGRRSQDCRRLAKELEEVKASERNLRARLKTLNCELAMYRRGRRTLPAGAREDRALSSRERSTSRGRTA 306
Cdd:COG1196  370 AEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAE 449

                        170
                 ....*....|...
gi 157818155 307 TRSSSRESNRGAR 319
Cdd:COG1196  450 EEAELEEEEEALL 462
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
151-308 4.67e-04

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 42.98  E-value: 4.67e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818155  151 IRSLKEELGHLRGMNGGQDA--RETEIWHLREQVTRLASEKRELEAQLgrsreealagRAARQEAESLRGLVRGLElelR 228
Cdd:COG4913   264 YAAARERLAELEYLRAALRLwfAQRRLELLEAELEELRAELARLEAEL----------ERLEARLDALREELDELE---A 330

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818155  229 QERGLGGRAAGRRSQDCRRLAKELEEVKASERNLRARLKTLNCEL--------AMYRRGRRTLPAGAREDRALSSRERST 300
Cdd:COG4913   331 QIRGNGGDRLEQLEREIERLERELEERERRRARLEALLAALGLPLpasaeefaALRAEAAALLEALEEELEALEEALAEA 410


                  ....*...
gi 157818155  301 SRGRTATR 308
Cdd:COG4913   411 EAALRDLR 418
PspA_IM30 pfam04012
PspA/IM30 family; This family includes PspA a protein that suppresses sigma54-dependent ...
 143-268 7.42e-04

PspA/IM30 family; This family includes PspA a protein that suppresses sigma54-dependent transcription. The PspA protein, a negative regulator of the Escherichia coli phage shock psp operon, is produced when virulence factors are exported through secretins in many Gram-negative pathogenic bacteria and its homolog in plants, VIPP1, plays a critical role in thylakoid biogenesis, essential for photosynthesis. Activation of transcription by the enhancer-dependent bacterial sigma(54) containing RNA polymerase occurs through ATP hydrolysis-driven protein conformational changes enabled by activator proteins that belong to the large AAA(+) mechanochemical protein family. It has been shown that PspA directly and specifically acts upon and binds to the AAA(+) domain of the PspF transcription activator.


Pssm-ID: 461130 [Multi-domain]  Cd Length: 215  Bit Score: 41.20  E-value: 7.42e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818155  143 DP-VVLQGIIRSLKEELGHLRGMNGGQDARETEIWHLREQVTRLAsEKRELEAQLGRSR-EEALAgRAARQEAESLRGLV 220
Cdd:pfam04012  22 DPeKMLEQAIRDMQSELVKARQALAQTIARQKQLERRLEQQTEQA-KKLEEKAQAALTKgNEELA-REALAEKKSLEKQA 99

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 157818155  221 RGLELELRQERGLggrAAGRRSQdCRRLAKELEEVKASERNLRARLKT 268
Cdd:pfam04012 100 EALETQLAQQRSA---VEQLRKQ-LAALETKIQQLKAKKNLLKARLKA 143
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
168-320 9.05e-04

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 42.21  E-value: 9.05e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818155  168 QDARETEIWHLREQVTRLASEKRELEAQLGRSREEALAGRAARQEA-----ESLRGLVRGLELELRqerglggraagRRS 242
Cdd:COG4913   290 LELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIRGNggdrlEQLEREIERLERELE-----------ERE 358

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 157818155  243 QDCRRLAKELEEVKASERNLRARLKTLNCELAMYRRGRRTLPAGAREDRALSSRERSTSRGRTATRSSSRESNRGARS 320
Cdd:COG4913   359 RRRARLEALLAALGLPLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERRKS 436
COG5283 COG5283
Phage-related tail protein [Mobilome: prophages, transposons];
179-270 5.00e-03

Phage-related tail protein [Mobilome: prophages, transposons];


Pssm-ID: 444094 [Multi-domain]  Cd Length: 747  Bit Score: 39.45  E-value: 5.00e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157818155 179 REQVTRLASEKRELEAQLGR-SREEALAGRAARQEAESLRGLVRGLElELRQERGLGGRAAGRRSQDCRRLAKELEEVKA 257
Cdd:COG5283   20 KQRVAALAQALKALEAPTRAlARALERAKQAAARLQTKYNKLRQSLQ-RLRQALDQAGIDTRQLSAAQRRLRSSLEQTNR 98

                         90
                 ....*....|...
gi 157818155 258 SERNLRARLKTLN 270
Cdd:COG5283   99 QLERQQQRLARLG 111
 
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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