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Conserved domains on  [gi|1720412945|ref|XP_030110212|]
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transforming acidic coiled-coil-containing protein 3 isoform X9 [Mus musculus]

Protein Classification

transforming acidic coiled-coil-containing protein( domain architecture ID 12059788)

transforming acidic coiled-coil (TACC)-containing protein similar to human TACC1 that is involved in transcription regulation induced by nuclear receptors, including in T3 thyroid hormone and all-trans retinoic acid pathways

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
TACC_C super family cl25596
Transforming acidic coiled-coil-containing protein (TACC), C-terminal; This entry represents a ...
355-494 4.10e-50

Transforming acidic coiled-coil-containing protein (TACC), C-terminal; This entry represents a C-terminal domain found in the the proteins TACC 1, 2 and 3 (TACC1-3). TACC1 is found concentrated in the centrosomes of eukaryotes which may play a conserved role in organizing centrosomal microtubules. The human TACC proteins have been linked to cancer and TACC2 has been identified as a possible tumour suppressor (AZU-1). TACC 3 from Xenopus laevis, also known as maskin, associates XMAP215 and promotes efficient microtubule elongation during mitosis. Maskin is also found to bind CPEB and elF-4E. Interestingly, the functional homolog (Alp7) in Schizosaccharomyces pombe (not included in this entry) has been shown to be required for organization of bipolar spindles.


The actual alignment was detected with superfamily member pfam05010:

Pssm-ID: 461517 [Multi-domain]  Cd Length: 201  Bit Score: 170.24  E-value: 4.10e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412945 355 YSQKDLDAVVNVMQQEN-------LELKSKYEDLNTKYLEMGKSVDEFEKIAYKSLEEAEKQRELKEIaedKIQKVLKER 427
Cdd:pfam05010   1 YSQKDMDAALEKARNEIeekeleiNELKAKYEELRRENLEMRKIVAEFEKTIAQMIEEKQKQKELEHA---EIQKVLEEK 77
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1720412945 428 DQLNADLNSMEKSFSDLFKRFEKRKEVIEGYQKNEESLKKYVGECIVKIEKEGQRYQALKIHAEEKL 494
Cdd:pfam05010  78 DQALADLNSVEKSFSDLFKRYEKQKEVISGYKKNEESLKKCAQDYLARIKKEEQRYQALKAHAEEKL 144
rne super family cl35953
ribonuclease E; Reviewed
71-221 5.93e-04

ribonuclease E; Reviewed


The actual alignment was detected with superfamily member PRK10811:

Pssm-ID: 236766 [Multi-domain]  Cd Length: 1068  Bit Score: 42.72  E-value: 5.93e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412945   71 VTPPIEPVLEPSHQGLEPVLESELVTPPVEPVLEPSHQE----------LEPVLESELVTPPIEPVLEPSHQGLEPVLDS 140
Cdd:PRK10811   847 VVRPQDVQVEEQREAEEVQVQPVVAEVPVAAAVEPVVSApvveavaevvEEPVVVAEPQPEEVVVVETTHPEVIAAPVTE 926
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412945  141 E--LVTPPIEPVLEPSHQGLEPVLESELVTPPIEPVLEPSHqglEPVLDSELVTPPIEPVLEPSHQglePVLDSELVTPP 218
Cdd:PRK10811   927 QpqVITESDVAVAQEVAEHAEPVVEPQDETADIEEAAETAE---VVVAEPEVVAQPAAPVVAEVAA---EVETVTAVEPE 1000

                   ...
gi 1720412945  219 IEP 221
Cdd:PRK10811  1001 VAP 1003
 
Name Accession Description Interval E-value
TACC_C pfam05010
Transforming acidic coiled-coil-containing protein (TACC), C-terminal; This entry represents a ...
355-494 4.10e-50

Transforming acidic coiled-coil-containing protein (TACC), C-terminal; This entry represents a C-terminal domain found in the the proteins TACC 1, 2 and 3 (TACC1-3). TACC1 is found concentrated in the centrosomes of eukaryotes which may play a conserved role in organizing centrosomal microtubules. The human TACC proteins have been linked to cancer and TACC2 has been identified as a possible tumour suppressor (AZU-1). TACC 3 from Xenopus laevis, also known as maskin, associates XMAP215 and promotes efficient microtubule elongation during mitosis. Maskin is also found to bind CPEB and elF-4E. Interestingly, the functional homolog (Alp7) in Schizosaccharomyces pombe (not included in this entry) has been shown to be required for organization of bipolar spindles.


Pssm-ID: 461517 [Multi-domain]  Cd Length: 201  Bit Score: 170.24  E-value: 4.10e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412945 355 YSQKDLDAVVNVMQQEN-------LELKSKYEDLNTKYLEMGKSVDEFEKIAYKSLEEAEKQRELKEIaedKIQKVLKER 427
Cdd:pfam05010   1 YSQKDMDAALEKARNEIeekeleiNELKAKYEELRRENLEMRKIVAEFEKTIAQMIEEKQKQKELEHA---EIQKVLEEK 77
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1720412945 428 DQLNADLNSMEKSFSDLFKRFEKRKEVIEGYQKNEESLKKYVGECIVKIEKEGQRYQALKIHAEEKL 494
Cdd:pfam05010  78 DQALADLNSVEKSFSDLFKRYEKQKEVISGYKKNEESLKKCAQDYLARIKKEEQRYQALKAHAEEKL 144
rne PRK10811
ribonuclease E; Reviewed
71-221 5.93e-04

ribonuclease E; Reviewed


Pssm-ID: 236766 [Multi-domain]  Cd Length: 1068  Bit Score: 42.72  E-value: 5.93e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412945   71 VTPPIEPVLEPSHQGLEPVLESELVTPPVEPVLEPSHQE----------LEPVLESELVTPPIEPVLEPSHQGLEPVLDS 140
Cdd:PRK10811   847 VVRPQDVQVEEQREAEEVQVQPVVAEVPVAAAVEPVVSApvveavaevvEEPVVVAEPQPEEVVVVETTHPEVIAAPVTE 926
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412945  141 E--LVTPPIEPVLEPSHQGLEPVLESELVTPPIEPVLEPSHqglEPVLDSELVTPPIEPVLEPSHQglePVLDSELVTPP 218
Cdd:PRK10811   927 QpqVITESDVAVAQEVAEHAEPVVEPQDETADIEEAAETAE---VVVAEPEVVAQPAAPVVAEVAA---EVETVTAVEPE 1000

                   ...
gi 1720412945  219 IEP 221
Cdd:PRK10811  1001 VAP 1003
PTZ00121 PTZ00121
MAEBL; Provisional
373-493 9.08e-04

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 42.05  E-value: 9.08e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412945  373 ELKSKYEDLNTKYLEMGKSVDEFEKIAYKSLEEAEKQRELKEIAEDKiqkvlKERDQLNADlnSMEKSFSDLFKRFEKRK 452
Cdd:PTZ00121  1319 EAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEK-----AEAAEKKKE--EAKKKADAAKKKAEEKK 1391
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|.
gi 1720412945  453 EVIEGYQKNEESLKKyvGECIVKIEKEGQRYQALKIHAEEK 493
Cdd:PTZ00121  1392 KADEAKKKAEEDKKK--ADELKKAAAAKKKADEAKKKAEEK 1430
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
353-493 2.76e-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: 2.76e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412945  353 LKYSQKDLDAVVNVMQQENLELKSKYEDLNTKYLEMG--KSVDEFEKI---------AYKSLEEAEKQREL-KEIAEDKI 420
Cdd:TIGR02169  756 VKSELKELEARIEELEEDLHKLEEALNDLEARLSHSRipEIQAELSKLeeevsrieaRLREIEQKLNRLTLeKEYLEKEI 835
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412945  421 QKVLKERDQLNADLNSMEKSFSDLFKRFEKRKEVIEGYQKNEESL-------KKYVGECIVKIEKEGQRYQALKIHAEEK 493
Cdd:TIGR02169  836 QELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLesrlgdlKKERDELEAQLRELERKIEELEAQIEKK 915
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
337-494 4.27e-03

Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 39.43  E-value: 4.27e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412945 337 VLEPRGLLPAEPIVDVLKYSQKDLDAVVNVMQQENLELKSKYEDLNTKYLEMGKSVDEFEkiayKSLEEAEKQRELKEIA 416
Cdd:COG3883     5 ALAAPTPAFADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQ----AEIDKLQAEIAEAEAE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412945 417 EDKIQKVLKER-----------DQLNADLNSmeKSFSDLFKRF-------EKRKEVIEGYQKNEESL---KKYVGECIVK 475
Cdd:COG3883    81 IEERREELGERaralyrsggsvSYLDVLLGS--ESFSDFLDRLsalskiaDADADLLEELKADKAELeakKAELEAKLAE 158
                         170
                  ....*....|....*....
gi 1720412945 476 IEKEGQRYQALKIHAEEKL 494
Cdd:COG3883   159 LEALKAELEAAKAELEAQQ 177
 
Name Accession Description Interval E-value
TACC_C pfam05010
Transforming acidic coiled-coil-containing protein (TACC), C-terminal; This entry represents a ...
355-494 4.10e-50

Transforming acidic coiled-coil-containing protein (TACC), C-terminal; This entry represents a C-terminal domain found in the the proteins TACC 1, 2 and 3 (TACC1-3). TACC1 is found concentrated in the centrosomes of eukaryotes which may play a conserved role in organizing centrosomal microtubules. The human TACC proteins have been linked to cancer and TACC2 has been identified as a possible tumour suppressor (AZU-1). TACC 3 from Xenopus laevis, also known as maskin, associates XMAP215 and promotes efficient microtubule elongation during mitosis. Maskin is also found to bind CPEB and elF-4E. Interestingly, the functional homolog (Alp7) in Schizosaccharomyces pombe (not included in this entry) has been shown to be required for organization of bipolar spindles.


Pssm-ID: 461517 [Multi-domain]  Cd Length: 201  Bit Score: 170.24  E-value: 4.10e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412945 355 YSQKDLDAVVNVMQQEN-------LELKSKYEDLNTKYLEMGKSVDEFEKIAYKSLEEAEKQRELKEIaedKIQKVLKER 427
Cdd:pfam05010   1 YSQKDMDAALEKARNEIeekeleiNELKAKYEELRRENLEMRKIVAEFEKTIAQMIEEKQKQKELEHA---EIQKVLEEK 77
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1720412945 428 DQLNADLNSMEKSFSDLFKRFEKRKEVIEGYQKNEESLKKYVGECIVKIEKEGQRYQALKIHAEEKL 494
Cdd:pfam05010  78 DQALADLNSVEKSFSDLFKRYEKQKEVISGYKKNEESLKKCAQDYLARIKKEEQRYQALKAHAEEKL 144
rne PRK10811
ribonuclease E; Reviewed
71-221 5.93e-04

ribonuclease E; Reviewed


Pssm-ID: 236766 [Multi-domain]  Cd Length: 1068  Bit Score: 42.72  E-value: 5.93e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412945   71 VTPPIEPVLEPSHQGLEPVLESELVTPPVEPVLEPSHQE----------LEPVLESELVTPPIEPVLEPSHQGLEPVLDS 140
Cdd:PRK10811   847 VVRPQDVQVEEQREAEEVQVQPVVAEVPVAAAVEPVVSApvveavaevvEEPVVVAEPQPEEVVVVETTHPEVIAAPVTE 926
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412945  141 E--LVTPPIEPVLEPSHQGLEPVLESELVTPPIEPVLEPSHqglEPVLDSELVTPPIEPVLEPSHQglePVLDSELVTPP 218
Cdd:PRK10811   927 QpqVITESDVAVAQEVAEHAEPVVEPQDETADIEEAAETAE---VVVAEPEVVAQPAAPVVAEVAA---EVETVTAVEPE 1000

                   ...
gi 1720412945  219 IEP 221
Cdd:PRK10811  1001 VAP 1003
PTZ00121 PTZ00121
MAEBL; Provisional
373-493 9.08e-04

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 42.05  E-value: 9.08e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412945  373 ELKSKYEDLNTKYLEMGKSVDEFEKIAYKSLEEAEKQRELKEIAEDKiqkvlKERDQLNADlnSMEKSFSDLFKRFEKRK 452
Cdd:PTZ00121  1319 EAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEK-----AEAAEKKKE--EAKKKADAAKKKAEEKK 1391
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|.
gi 1720412945  453 EVIEGYQKNEESLKKyvGECIVKIEKEGQRYQALKIHAEEK 493
Cdd:PTZ00121  1392 KADEAKKKAEEDKKK--ADELKKAAAAKKKADEAKKKAEEK 1430
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
353-493 2.76e-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: 2.76e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412945  353 LKYSQKDLDAVVNVMQQENLELKSKYEDLNTKYLEMG--KSVDEFEKI---------AYKSLEEAEKQREL-KEIAEDKI 420
Cdd:TIGR02169  756 VKSELKELEARIEELEEDLHKLEEALNDLEARLSHSRipEIQAELSKLeeevsrieaRLREIEQKLNRLTLeKEYLEKEI 835
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412945  421 QKVLKERDQLNADLNSMEKSFSDLFKRFEKRKEVIEGYQKNEESL-------KKYVGECIVKIEKEGQRYQALKIHAEEK 493
Cdd:TIGR02169  836 QELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLesrlgdlKKERDELEAQLRELERKIEELEAQIEKK 915
rne PRK10811
ribonuclease E; Reviewed
26-203 2.85e-03

ribonuclease E; Reviewed


Pssm-ID: 236766 [Multi-domain]  Cd Length: 1068  Bit Score: 40.41  E-value: 2.85e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412945   26 PLAPVDDAPVVQmaaeilraegELQEGILTSSSLSASTSLLDSELVTPPIEPVLEPSHQGLEPVLESELVTPPVEPVlEP 105
Cdd:PRK10811   846 PVVRPQDVQVEE----------QREAEEVQVQPVVAEVPVAAAVEPVVSAPVVEAVAEVVEEPVVVAEPQPEEVVVV-ET 914
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412945  106 SHQEL--EPVLES-ELVTPPIEPVLEPSHQGLEPVLDSELVTPPIEPVLEPSHqglEPVLESELVTPPIEPVLEPSHQGL 182
Cdd:PRK10811   915 THPEViaAPVTEQpQVITESDVAVAQEVAEHAEPVVEPQDETADIEEAAETAE---VVVAEPEVVAQPAAPVVAEVAAEV 991
                          170       180
                   ....*....|....*....|....
gi 1720412945  183 --EPVLDSELVTPPI-EPVLEPSH 203
Cdd:PRK10811   992 etVTAVEPEVAPAQVpEATVEHNH 1015
PTZ00121 PTZ00121
MAEBL; Provisional
373-493 4.12e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 40.12  E-value: 4.12e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412945  373 ELKSKYEDLNtKYLEMGKSVDEFEKIA--YKSLEEAEKQRELKEIAEDKIQKVLKERDQLNADLNSMEKSFSD-LFKRFE 449
Cdd:PTZ00121  1402 EDKKKADELK-KAAAAKKKADEAKKKAeeKKKADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKADeAKKKAE 1480
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....
gi 1720412945  450 KRKEVIEGYQKNEESLKKyvGECIVKIEKEGQRYQALKiHAEEK 493
Cdd:PTZ00121  1481 EAKKADEAKKKAEEAKKK--ADEAKKAAEAKKKADEAK-KAEEA 1521
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
337-494 4.27e-03

Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 39.43  E-value: 4.27e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412945 337 VLEPRGLLPAEPIVDVLKYSQKDLDAVVNVMQQENLELKSKYEDLNTKYLEMGKSVDEFEkiayKSLEEAEKQRELKEIA 416
Cdd:COG3883     5 ALAAPTPAFADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQ----AEIDKLQAEIAEAEAE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412945 417 EDKIQKVLKER-----------DQLNADLNSmeKSFSDLFKRF-------EKRKEVIEGYQKNEESL---KKYVGECIVK 475
Cdd:COG3883    81 IEERREELGERaralyrsggsvSYLDVLLGS--ESFSDFLDRLsalskiaDADADLLEELKADKAELeakKAELEAKLAE 158
                         170
                  ....*....|....*....
gi 1720412945 476 IEKEGQRYQALKIHAEEKL 494
Cdd:COG3883   159 LEALKAELEAAKAELEAQQ 177
PRK01156 PRK01156
chromosome segregation protein; Provisional
351-471 6.20e-03

chromosome segregation protein; Provisional


Pssm-ID: 100796 [Multi-domain]  Cd Length: 895  Bit Score: 39.11  E-value: 6.20e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412945 351 DVLKYSQKDLDAVVNVMQQENLELKSKYEDLNtkylEMGKSVDEFEKIayKSLEEAEKQRelkeiAEDKIQKVLKERDQL 430
Cdd:PRK01156  169 DKLKDVIDMLRAEISNIDYLEEKLKSSNLELE----NIKKQIADDEKS--HSITLKEIER-----LSIEYNNAMDDYNNL 237
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1720412945 431 NADLNSMeKSFSDLFKRFEKRKEVIEGYQKNEESLKKYVGE 471
Cdd:PRK01156  238 KSALNEL-SSLEDMKNRYESEIKTAESDLSMELEKNNYYKE 277
PTZ00121 PTZ00121
MAEBL; Provisional
373-497 6.26e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 39.35  E-value: 6.26e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412945  373 ELKSKYEDLNTKYLEMGKSVDEF----EKIAYKSLEEAEKQRELKEIAEDKIQKVLKERDQLNADLNSME--KSFSDLFK 446
Cdd:PTZ00121  1630 EEKKKVEQLKKKEAEEKKKAEELkkaeEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEeaKKAEELKK 1709
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1720412945  447 RFEKRKEVIEGYQKNEESLKKYVGECIVKIEKEGQRYQALKIHAEEKLRLQ 497
Cdd:PTZ00121  1710 KEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEEKKKIA 1760
PRK12704 PRK12704
phosphodiesterase; Provisional
390-497 9.02e-03

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 38.61  E-value: 9.02e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412945 390 KSVDEFEKIAYKSLEEAEKqrELKEIAEDKI----QKVLKERDQLNADLNSMEKSFSDLFKR--------------FEKR 451
Cdd:PRK12704   31 AKIKEAEEEAKRILEEAKK--EAEAIKKEALleakEEIHKLRNEFEKELRERRNELQKLEKRllqkeenldrklelLEKR 108
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1720412945 452 KEVIEGYQKNEESLKKYVGECIVKIEkegqryqalKIHAEEKLRLQ 497
Cdd:PRK12704  109 EEELEKKEKELEQKQQELEKKEEELE---------ELIEEQLQELE 145
 
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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