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Conserved domains on  [gi|568933977|ref|XP_006503898|]
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transforming acidic coiled-coil-containing protein 3 isoform X7 [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 pfam05010
Transforming acidic coiled-coil-containing protein (TACC), C-terminal; This entry represents a ...
 362-558 1.74e-82

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: 256.14  E-value: 1.74e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568933977  362 YSQKDLDAVVNVMQQEN-------LELKSKYEDLNTKYLEMGKSVDEFEKIAYKSLEEAEKQRELKEIaedKIQKVLKER 434
Cdd:pfam05010   1 YSQKDMDAALEKARNEIeekeleiNELKAKYEELRRENLEMRKIVAEFEKTIAQMIEEKQKQKELEHA---EIQKVLEEK 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568933977  435 DQLNADLNSMEKSFSDLFKRFEKRKEVIEGYQKNEESLKKYVGECIVKIEKEGQRYQALKIHAEEKLRLANEEIAQVHSK 514
Cdd:pfam05010  78 DQALADLNSVEKSFSDLFKRYEKQKEVISGYKKNEESLKKCAQDYLARIKKEEQRYQALKAHAEEKLDQANEEIAQVRSK 157

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 568933977  515 AQAEVLALQASLRKAQMQNHSLEMTLEQKTKEIDELTRICDDLI 558
Cdd:pfam05010 158 AKAETAALQASLRKEQMKVQSLERQLEQKTKENEELTKICDELI 201
rne super family cl35953
ribonuclease E; Reviewed
 71-221 6.14e-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: 6.14e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568933977   71 VTPPIEPVLEPSHQGLEPVLESELVTPPVEPVLEPSHQE----------LEPVLESELVTPPIEPVLEPSHQGLEPVLDS 140
Cdd:PRK10811  847 VVRPQDVQVEEQREAEEVQVQPVVAEVPVAAAVEPVVSApvveavaevvEEPVVVAEPQPEEVVVVETTHPEVIAAPVTE 926

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568933977  141 E--LVTPPIEPVLEPSHQGLEPVLESELVTPPIEPVLEPSHqglEPVLDSELVTPPIEPVLEPSHQglePVLDSELVTPP 218
Cdd:PRK10811  927 QpqVITESDVAVAQEVAEHAEPVVEPQDETADIEEAAETAE---VVVAEPEVVAQPAAPVVAEVAA---EVETVTAVEPE 1000


                  ...
gi 568933977  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 ...
 362-558 1.74e-82

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: 256.14  E-value: 1.74e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568933977  362 YSQKDLDAVVNVMQQEN-------LELKSKYEDLNTKYLEMGKSVDEFEKIAYKSLEEAEKQRELKEIaedKIQKVLKER 434
Cdd:pfam05010   1 YSQKDMDAALEKARNEIeekeleiNELKAKYEELRRENLEMRKIVAEFEKTIAQMIEEKQKQKELEHA---EIQKVLEEK 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568933977  435 DQLNADLNSMEKSFSDLFKRFEKRKEVIEGYQKNEESLKKYVGECIVKIEKEGQRYQALKIHAEEKLRLANEEIAQVHSK 514
Cdd:pfam05010  78 DQALADLNSVEKSFSDLFKRYEKQKEVISGYKKNEESLKKCAQDYLARIKKEEQRYQALKAHAEEKLDQANEEIAQVRSK 157

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 568933977  515 AQAEVLALQASLRKAQMQNHSLEMTLEQKTKEIDELTRICDDLI 558
Cdd:pfam05010 158 AKAETAALQASLRKEQMKVQSLERQLEQKTKENEELTKICDELI 201
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 344-549 6.79e-07

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 51.75  E-value: 6.79e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568933977 344 VLEPRGLLPAEPIVDVLKYSQKDLDAVVNVMQQENLELKSKYEDLNTKYLEMGKSVDEFEKiaykSLEEAEKQRELKEIA 423
Cdd:COG3883    5 ALAAPTPAFADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQA----EIDKLQAEIAEAEAE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568933977 424 EDKIQKVLKER-----------DQLNADLNSmeKSFSDLFKRF-------EKRKEVIEGYQKNEESLKKYVGEcivkIEK 485
Cdd:COG3883   81 IEERREELGERaralyrsggsvSYLDVLLGS--ESFSDFLDRLsalskiaDADADLLEELKADKAELEAKKAE----LEA 154

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568933977 486 EGQRYQALKIHAEEKLRLANEEIAQvhskAQAEVLALQASLRKAQMQNHSLEMTLEQKTKEIDE 549
Cdd:COG3883  155 KLAELEALKAELEAAKAELEAQQAE----QEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAA 214
PTZ00121 PTZ00121
MAEBL; Provisional
 380-552 4.18e-05

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 46.67  E-value: 4.18e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568933977  380 ELKSKYEDLNtKYLEMGKSVDEFEKIA--YKSLEEAEKQRELKEIAEDKIQKVLKERDQLNADLNSMEKSFSD-LFKRFE 456
Cdd:PTZ00121 1402 EDKKKADELK-KAAAAKKKADEAKKKAeeKKKADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKADeAKKKAE 1480

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568933977  457 KRKEVIEGYQKNEESLKKyvGECIVKIEKEGQRYQALKiHAEEKLRLanEEIAQVHSKAQAEVLALQASLRKAQMQNHSL 536
Cdd:PTZ00121 1481 EAKKADEAKKKAEEAKKK--ADEAKKAAEAKKKADEAK-KAEEAKKA--DEAKKAEEAKKADEAKKAEEKKKADELKKAE 1555

                         170
                  ....*....|....*.
gi 568933977  537 EMTLEQKTKEIDELTR 552
Cdd:PTZ00121 1556 ELKKAEEKKKAEEAKK 1571
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 360-552 9.54e-05

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: 45.44  E-value: 9.54e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568933977   360 LKYSQKDLDAVVNVMQQENLELKSKYEDLNTKYLEMG--KSVDEFEKI---------AYKSLEEAEKQREL-KEIAEDKI 427
Cdd:TIGR02169  756 VKSELKELEARIEELEEDLHKLEEALNDLEARLSHSRipEIQAELSKLeeevsrieaRLREIEQKLNRLTLeKEYLEKEI 835

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568933977   428 QKVLKERDQLNADLNSMEKSFSDLFKRFEKRKEVIEGYQKNEESLKKYVGEcivkIEKEGQRyqalkihAEEKLRLANEE 507
Cdd:TIGR02169  836 QELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGD----LKKERDE-------LEAQLRELERK 904

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*
gi 568933977   508 IAQVhsKAQAEVLALQASLRKAQMQNhslemtLEQKTKEIDELTR 552
Cdd:TIGR02169  905 IEEL--EAQIEKKRKRLSELKAKLEA------LEEELSEIEDPKG 941
rne PRK10811
ribonuclease E; Reviewed
 71-221 6.14e-04

ribonuclease E; Reviewed


Pssm-ID: 236766 [Multi-domain]  Cd Length: 1068  Bit Score: 42.72  E-value: 6.14e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568933977   71 VTPPIEPVLEPSHQGLEPVLESELVTPPVEPVLEPSHQE----------LEPVLESELVTPPIEPVLEPSHQGLEPVLDS 140
Cdd:PRK10811  847 VVRPQDVQVEEQREAEEVQVQPVVAEVPVAAAVEPVVSApvveavaevvEEPVVVAEPQPEEVVVVETTHPEVIAAPVTE 926

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568933977  141 E--LVTPPIEPVLEPSHQGLEPVLESELVTPPIEPVLEPSHqglEPVLDSELVTPPIEPVLEPSHQglePVLDSELVTPP 218
Cdd:PRK10811  927 QpqVITESDVAVAQEVAEHAEPVVEPQDETADIEEAAETAE---VVVAEPEVVAQPAAPVVAEVAA---EVETVTAVEPE 1000


                  ...
gi 568933977  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 ...
 362-558 1.74e-82

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: 256.14  E-value: 1.74e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568933977  362 YSQKDLDAVVNVMQQEN-------LELKSKYEDLNTKYLEMGKSVDEFEKIAYKSLEEAEKQRELKEIaedKIQKVLKER 434
Cdd:pfam05010   1 YSQKDMDAALEKARNEIeekeleiNELKAKYEELRRENLEMRKIVAEFEKTIAQMIEEKQKQKELEHA---EIQKVLEEK 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568933977  435 DQLNADLNSMEKSFSDLFKRFEKRKEVIEGYQKNEESLKKYVGECIVKIEKEGQRYQALKIHAEEKLRLANEEIAQVHSK 514
Cdd:pfam05010  78 DQALADLNSVEKSFSDLFKRYEKQKEVISGYKKNEESLKKCAQDYLARIKKEEQRYQALKAHAEEKLDQANEEIAQVRSK 157

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 568933977  515 AQAEVLALQASLRKAQMQNHSLEMTLEQKTKEIDELTRICDDLI 558
Cdd:pfam05010 158 AKAETAALQASLRKEQMKVQSLERQLEQKTKENEELTKICDELI 201
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 344-549 6.79e-07

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 51.75  E-value: 6.79e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568933977 344 VLEPRGLLPAEPIVDVLKYSQKDLDAVVNVMQQENLELKSKYEDLNTKYLEMGKSVDEFEKiaykSLEEAEKQRELKEIA 423
Cdd:COG3883    5 ALAAPTPAFADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQA----EIDKLQAEIAEAEAE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568933977 424 EDKIQKVLKER-----------DQLNADLNSmeKSFSDLFKRF-------EKRKEVIEGYQKNEESLKKYVGEcivkIEK 485
Cdd:COG3883   81 IEERREELGERaralyrsggsvSYLDVLLGS--ESFSDFLDRLsalskiaDADADLLEELKADKAELEAKKAE----LEA 154

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568933977 486 EGQRYQALKIHAEEKLRLANEEIAQvhskAQAEVLALQASLRKAQMQNHSLEMTLEQKTKEIDE 549
Cdd:COG3883  155 KLAELEALKAELEAAKAELEAQQAE----QEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAA 214
PTZ00121 PTZ00121
MAEBL; Provisional
 380-552 4.18e-05

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 46.67  E-value: 4.18e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568933977  380 ELKSKYEDLNtKYLEMGKSVDEFEKIA--YKSLEEAEKQRELKEIAEDKIQKVLKERDQLNADLNSMEKSFSD-LFKRFE 456
Cdd:PTZ00121 1402 EDKKKADELK-KAAAAKKKADEAKKKAeeKKKADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKADeAKKKAE 1480

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568933977  457 KRKEVIEGYQKNEESLKKyvGECIVKIEKEGQRYQALKiHAEEKLRLanEEIAQVHSKAQAEVLALQASLRKAQMQNHSL 536
Cdd:PTZ00121 1481 EAKKADEAKKKAEEAKKK--ADEAKKAAEAKKKADEAK-KAEEAKKA--DEAKKAEEAKKADEAKKAEEKKKADELKKAE 1555

                         170
                  ....*....|....*.
gi 568933977  537 EMTLEQKTKEIDELTR 552
Cdd:PTZ00121 1556 ELKKAEEKKKAEEAKK 1571
PTZ00121 PTZ00121
MAEBL; Provisional
 380-563 4.67e-05

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 46.67  E-value: 4.67e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568933977  380 ELKSKYEDLNTKYLEMGKSVDEFEKIAYKSLEEAEKQRELKEIAEDKiqkvlKERDQLNADlnSMEKSFSDLFKRFEKRK 459
Cdd:PTZ00121 1319 EAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEK-----AEAAEKKKE--EAKKKADAAKKKAEEKK 1391

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568933977  460 EVIEGYQKNEESLKKyvGECIVKIEKEGQRYQALKIHAEEKlRLANEEIAQVHSKAQAEVLALQA-SLRKAQ-MQNHSLE 537
Cdd:PTZ00121 1392 KADEAKKKAEEDKKK--ADELKKAAAAKKKADEAKKKAEEK-KKADEAKKKAEEAKKADEAKKKAeEAKKAEeAKKKAEE 1468

                         170       180
                  ....*....|....*....|....*.
gi 568933977  538 MTLEQKTKEIDELTRICDDLISKMEK 563
Cdd:PTZ00121 1469 AKKADEAKKKAEEAKKADEAKKKAEE 1494
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 359-552 5.75e-05

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 46.08  E-value: 5.75e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568933977 359 VLKY------SQKDLDAVvnvmqQENL--------ELKSKYEDLNT------KYLEMGKSVDEFEKIAY-KSLEEAEKQR 417
Cdd:COG1196  167 ISKYkerkeeAERKLEAT-----EENLerledilgELERQLEPLERqaekaeRYRELKEELKELEAELLlLKLRELEAEL 241

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568933977 418 ELkeiAEDKIQKVLKERDQLNADLNSMEKSFSDLFKRFEKRKEVIEGYQKNEESLKKYVGECIVKIEKEGQRYQALKiHA 497
Cdd:COG1196  242 EE---LEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELE-ER 317

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 568933977 498 EEKLRLANEEIAQVHSKAQAEVLALQASLRKAQMQNHSLEMTLEQKTKEIDELTR 552
Cdd:COG1196  318 LEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEA 372
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
386-564 6.25e-05

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 45.91  E-value: 6.25e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568933977 386 EDLNTKYLEMGKSVDEFEKIAYKSLEEAEKQRELKEIAEDKIQKVLKERDQLNADLNSMEKSFSDL---FKRFEKRKEVI 462
Cdd:COG4717   49 ERLEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELreeLEKLEKLLQLL 128

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568933977 463 EGYQKNEEsLKKYVGECIVKIEKEGQRYQALKiHAEEKLRLANEEIAQVHSKAQAEV----LALQASLRKAQMQNHSLEM 538
Cdd:COG4717  129 PLYQELEA-LEAELAELPERLEELEERLEELR-ELEEELEELEAELAELQEELEELLeqlsLATEEELQDLAEELEELQQ 206

                        170       180
                 ....*....|....*....|....*.
gi 568933977 539 TLEQKTKEIDELTRICDDLISKMEKI 564
Cdd:COG4717  207 RLAELEEELEEAQEELEELEEELEQL 232
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 360-552 9.54e-05

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: 45.44  E-value: 9.54e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568933977   360 LKYSQKDLDAVVNVMQQENLELKSKYEDLNTKYLEMG--KSVDEFEKI---------AYKSLEEAEKQREL-KEIAEDKI 427
Cdd:TIGR02169  756 VKSELKELEARIEELEEDLHKLEEALNDLEARLSHSRipEIQAELSKLeeevsrieaRLREIEQKLNRLTLeKEYLEKEI 835

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568933977   428 QKVLKERDQLNADLNSMEKSFSDLFKRFEKRKEVIEGYQKNEESLKKYVGEcivkIEKEGQRyqalkihAEEKLRLANEE 507
Cdd:TIGR02169  836 QELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGD----LKKERDE-------LEAQLRELERK 904

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*
gi 568933977   508 IAQVhsKAQAEVLALQASLRKAQMQNhslemtLEQKTKEIDELTR 552
Cdd:TIGR02169  905 IEEL--EAQIEKKRKRLSELKAKLEA------LEEELSEIEDPKG 941
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 363-543 1.04e-04

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: 45.43  E-value: 1.04e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568933977   363 SQKDLDA-VVNVMQQENLELKSKYEDLNtkylemgKSVDEFEKIAYKSLEEAEKQRELKEIAEDKIQKVLKERDQLNADL 441
Cdd:TIGR02168  330 SKLDELAeELAELEEKLEELKEELESLE-------AELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEI 402

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568933977   442 NSMEKSFSDLFKRFEKRKEVIEGYQKN-EESLKKYVGECIVKIEKEGQRYQALKIHAEEKLRLANEEIAQvhskAQAEVL 520
Cdd:TIGR02168  403 ERLEARLERLEDRRERLQQEIEELLKKlEEAELKELQAELEELEEELEELQEELERLEEALEELREELEE----AEQALD 478

                          170       180
                   ....*....|....*....|...
gi 568933977   521 ALQASLRKAQMQNHSLEMTLEQK 543
Cdd:TIGR02168  479 AAERELAQLQARLDSLERLQENL 501
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 366-550 1.20e-04

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: 45.05  E-value: 1.20e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568933977   366 DLDAVVNVMQQENLELKSKYEDLNTKYLEMGKSVDEFEKIAYKSLEEAEKQRELKEIAED-------KIQKVLKERDQLN 438
Cdd:TIGR02168  751 QLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAeltllneEAANLRERLESLE 830

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568933977   439 ADLNSMEKSFSDLFKRFEKRKEVIEGYQKNEESLkkyvGECIVKIEKEGQRYQALKIHAEEKLRLANEEIAQVHSKAQA- 517
Cdd:TIGR02168  831 RRIAATERRLEDLEEQIEELSEDIESLAAEIEEL----EELIEELESELEALLNERASLEEALALLRSELEELSEELREl 906

                          170       180       190
                   ....*....|....*....|....*....|....*
gi 568933977   518 --EVLALQASLRKAQMQNHSLEMTLEQKTKEIDEL 550
Cdd:TIGR02168  907 esKRSELRRELEELREKLAQLELRLEGLEVRIDNL 941
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 375-552 1.71e-04

Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 43.98  E-value: 1.71e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568933977 375 QQENLELKSKYEDLNTKYLEMGKSVDEFEKIAYKSLEEAEKQRELKEIAEDKIQKVLKERDQLNADLNSMEKSFSDLFKR 454
Cdd:COG4942   19 ADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAE 98

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568933977 455 FEKRKEVIEG-----YQKNEESLKKYV--GECIVKIEKEGQRYQALKIHAE---EKLRLANEEIAQVHSKAQAEVLALQA 524
Cdd:COG4942   99 LEAQKEELAEllralYRLGRQPPLALLlsPEDFLDAVRRLQYLKYLAPARReqaEELRADLAELAALRAELEAERAELEA 178

                        170       180
                 ....*....|....*....|....*...
gi 568933977 525 SLRKAQMQNHSLEMTLEQKTKEIDELTR 552
Cdd:COG4942  179 LLAELEEERAALEALKAERQKLLARLEK 206
PTZ00121 PTZ00121
MAEBL; Provisional
 380-563 4.32e-04

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 43.59  E-value: 4.32e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568933977  380 ELKSKYEDLntKYLEMGKSVDEFEKIAykslEEAEKQRELKEIAE------DKIQKVLKERDQLNADLNSMEKSFSDLFK 453
Cdd:PTZ00121 1287 EEKKKADEA--KKAEEKKKADEAKKKA----EEAKKADEAKKKAEeakkkaDAAKKKAEEAKKAAEAAKAEAEAAADEAE 1360

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568933977  454 RFEKRKEVIEgyQKNEESLKKyvGECIVKIEKEGQRYQALKIHAEEKLRLANEEIAQVHSKAQAEVLALQA-SLRKA-QM 531
Cdd:PTZ00121 1361 AAEEKAEAAE--KKKEEAKKK--ADAAKKKAEEKKKADEAKKKAEEDKKKADELKKAAAAKKKADEAKKKAeEKKKAdEA 1436

                         170       180       190
                  ....*....|....*....|....*....|..
gi 568933977  532 QNHSLEMTLEQKTKEIDELTRICDDLISKMEK 563
Cdd:PTZ00121 1437 KKKAEEAKKADEAKKKAEEAKKAEEAKKKAEE 1468
rne PRK10811
ribonuclease E; Reviewed
 71-221 6.14e-04

ribonuclease E; Reviewed


Pssm-ID: 236766 [Multi-domain]  Cd Length: 1068  Bit Score: 42.72  E-value: 6.14e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568933977   71 VTPPIEPVLEPSHQGLEPVLESELVTPPVEPVLEPSHQE----------LEPVLESELVTPPIEPVLEPSHQGLEPVLDS 140
Cdd:PRK10811  847 VVRPQDVQVEEQREAEEVQVQPVVAEVPVAAAVEPVVSApvveavaevvEEPVVVAEPQPEEVVVVETTHPEVIAAPVTE 926

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568933977  141 E--LVTPPIEPVLEPSHQGLEPVLESELVTPPIEPVLEPSHqglEPVLDSELVTPPIEPVLEPSHQglePVLDSELVTPP 218
Cdd:PRK10811  927 QpqVITESDVAVAQEVAEHAEPVVEPQDETADIEEAAETAE---VVVAEPEVVAQPAAPVVAEVAA---EVETVTAVEPE 1000


                  ...
gi 568933977  219 IEP 221
Cdd:PRK10811 1001 VAP 1003
HEC1 COG5185
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ...
 375-562 6.66e-04

Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 444066 [Multi-domain]  Cd Length: 594  Bit Score: 42.64  E-value: 6.66e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568933977 375 QQENLELKSKYEDLNTKYLEMGKSVDEFEKIAYKSL-EEAEKQRELKEIAEDKIQKVLKERDQL--NADLNSMEKSFSDL 451
Cdd:COG5185  235 LKGFQDPESELEDLAQTSDKLEKLVEQNTDLRLEKLgENAESSKRLNENANNLIKQFENTKEKIaeYTKSIDIKKATESL 314

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568933977 452 ---FKRFEKRKEVIEGYQKNEESLKKYVGECIVKIEKEGQRYQALK-----IHAEEKLRLANEEI----AQVHSKAQAEV 519
Cdd:COG5185  315 eeqLAAAEAEQELEESKRETETGIQNLTAEIEQGQESLTENLEAIKeeienIVGEVELSKSSEELdsfkDTIESTKESLD 394

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 568933977 520 LALQASLRKAQMQNHSLEMTLEQKTKEIDELTRICDDLISKME 562
Cdd:COG5185  395 EIPQNQRGYAQEILATLEDTLKAADRQIEELQRQIEQATSSNE 437
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 399-550 7.36e-04

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: 42.75  E-value: 7.36e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568933977   399 VDEFEKIAYKSLEEAEKQRELKEIAEDKIQKVLKERDQLNADLNSMEKsFSDLFKRFEKRK--EVIEGYQKNEESLKKYV 476
Cdd:TIGR02169  165 VAEFDRKKEKALEELEEVEENIERLDLIIDEKRQQLERLRREREKAER-YQALLKEKREYEgyELLKEKEALERQKEAIE 243

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568933977   477 GEcIVKIEKEGQ----RYQALKIHAEEKLRLANEEIAQVHSKAQAEVLALQASLRKAQMQNHSLEMTLEQKTKEIDEL 550
Cdd:TIGR02169  244 RQ-LASLEEELEklteEISELEKRLEEIEQLLEELNKKIKDLGEEEQLRVKEKIGELEAEIASLERSIAEKERELEDA 320
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
380-530 1.01e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 41.97  E-value: 1.01e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568933977 380 ELKSKYEDLN------TKYLEMGKSVDEFEKIAYKSLEEAEKQRELKEiaedKIQKVLKERDQLNADLNSMEKSFSDLFK 453
Cdd:PRK03918 277 ELEEKVKELKelkekaEEYIKLSEFYEEYLDELREIEKRLSRLEEEIN----GIEERIKELEEKEERLEELKKKLKELEK 352

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568933977 454 RFEKRKEVIEGYQK------NEESLKKYV-GECIVKIEKEGQRYQALKIHAEEKLRLANEEIAQVHSKAQAEVLALQAsL 526
Cdd:PRK03918 353 RLEELEERHELYEEakakkeELERLKKRLtGLTPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEE-L 431


                 ....
gi 568933977 527 RKAQ 530
Cdd:PRK03918 432 KKAK 435
235kDa-fam TIGR01612
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ...
 356-557 1.05e-03

reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in plasmodium species alternately annotated as reticulocyte binding protein, 235-kDa family protein and rhoptry protein. Rhoptry protein is localized on the cell surface and is extremely large (although apparently lacking in repeat structure) and is important for the process of invasion of the RBCs by the parasite. These proteins are found in P. falciparum, P. vivax and P. yoelii.


Pssm-ID: 130673 [Multi-domain]  Cd Length: 2757  Bit Score: 42.35  E-value: 1.05e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568933977   356 IVDVLKYSQKDLDAVVNVMQQENLEL---KSKYEDLNTKYLEMGKSVDEFEKIAYKSLEEAEKQRELKEIAEDKIQKVLK 432
Cdd:TIGR01612  756 ILEDFKNKEKELSNKINDYAKEKDELnkyKSKISEIKNHYNDQINIDNIKDEDAKQNYDKSKEYIKTISIKEDEIFKIIN 835

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568933977   433 ERDQLNAD------------------LNSMEKSFSDLFKRF--EKRKEVIEGYQKNEESLKKYVGECIVKIEKEGQRYQA 492
Cdd:TIGR01612  836 EMKFMKDDflnkvdkfinfennckekIDSEHEQFAELTNKIkaEISDDKLNDYEKKFNDSKSLINEINKSIEEEYQNINT 915

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568933977   493 LKiHAEEKLRL---ANEEIAQVHSKAQAEVLALQASLRKAQMQNhSLEMTLEQK-----TKEIDELTRICDDL 557
Cdd:TIGR01612  916 LK-KVDEYIKIcenTKESIEKFHNKQNILKEILNKNIDTIKESN-LIEKSYKDKfdntlIDKINELDKAFKDA 986
DUF4407 pfam14362
Domain of unknown function (DUF4407); This family of proteins is found in bacteria. Proteins ...
 349-527 1.73e-03

Domain of unknown function (DUF4407); This family of proteins is found in bacteria. Proteins in this family are typically between 366 and 597 amino acids in length. There is a single completely conserved residue R that may be functionally important.


Pssm-ID: 464151 [Multi-domain]  Cd Length: 295  Bit Score: 40.70  E-value: 1.73e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568933977  349 GLLPAEPIVdvLKYSQKDLDAVVNVMQQEnlelkskyedlntkylemgksvdefekiaykslEEAEKQRELKEIAEDKIQ 428
Cdd:pfam14362  92 GVVISEPLE--LKIFEKEIDRELLEIQQE---------------------------------EADAAKAQLAAAYRARLA 136

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568933977  429 KVLKERDQLNADLNSMEKSFSDLFKrfEKRKEvIEGYQKNEESLKKYVGECIVK---IEKEGQRYQALKIHAEEKLRLAN 505
Cdd:pfam14362 137 ELEAQIAALDAEIDAAEARLDALQA--EARCE-LDGTPGTGTGVPGDGPVAKTKqaqLDAAQAELAALQAQNDARLAALR 213

                         170       180
                  ....*....|....*....|..
gi 568933977  506 EEIAQVHSKAQAEVLALQASLR 527
Cdd:pfam14362 214 AELARLTAERAAARARSQAAID 235
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 409-564 1.79e-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: 41.20  E-value: 1.79e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568933977   409 SLEEAEKQRelkEIAEDKIQKVLKERDQLNADLNSMEKSFSDLFKRFEKRKEVIEGYQKNEESLKKYVGECIVKIEKEGQ 488
Cdd:TIGR02168  692 KIAELEKAL---AELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEE 768

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568933977   489 RY---QALKIHAEEKLRLANEEIAQV----------HSKAQAEVLALQASLRKAQMQNHSLEMTLEQKTKEIDELTRICD 555
Cdd:TIGR02168  769 RLeeaEEELAEAEAEIEELEAQIEQLkeelkalreaLDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIE 848


                   ....*....
gi 568933977   556 DLISKMEKI 564
Cdd:TIGR02168  849 ELSEDIESL 857
PTZ00121 PTZ00121
MAEBL; Provisional
 380-564 1.92e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 41.28  E-value: 1.92e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568933977  380 ELKSKYEDLNTKYLEMGKSVDEF----EKIAYKSLEEAEKQRELKEIAEDKIQKVLKERDQLNADLNSME--KSFSDLFK 453
Cdd:PTZ00121 1630 EEKKKVEQLKKKEAEEKKKAEELkkaeEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEeaKKAEELKK 1709

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568933977  454 RFEKRKEVIEGYQKNEESLKKYVGECIVKIEKEGQRYQALKIHAEEKLRLAneeiaqvHSKAQAEVLALQASLRKAQMQN 533
Cdd:PTZ00121 1710 KEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEEKKKIA-------HLKKEEEKKAEEIRKEKEAVIE 1782

                         170       180       190
                  ....*....|....*....|....*....|.
gi 568933977  534 HSLEMTLEQKTKEIDELTRicdDLISKMEKI 564
Cdd:PTZ00121 1783 EELDEEDEKRRMEVDKKIK---DIFDNFANI 1810
rne PRK10811
ribonuclease E; Reviewed
 26-203 3.14e-03

ribonuclease E; Reviewed


Pssm-ID: 236766 [Multi-domain]  Cd Length: 1068  Bit Score: 40.41  E-value: 3.14e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568933977   26 PLAPVDDAPVV-QMAAEILRAEGELQEgiltssslSASTSLLDSELVTPPIEPVLEPSHqglEPVLESELVTPPVEPVlE 104
Cdd:PRK10811  846 PVVRPQDVQVEeQREAEEVQVQPVVAE--------VPVAAAVEPVVSAPVVEAVAEVVE---EPVVVAEPQPEEVVVV-E 913

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568933977  105 PSHQEL--EPVLES-ELVTPPIEPVLEPSHQGLEPVLDSELVTPPIEPVLEPSHqglEPVLESELVTPPIEPVLEPSHQG 181
Cdd:PRK10811  914 TTHPEViaAPVTEQpQVITESDVAVAQEVAEHAEPVVEPQDETADIEEAAETAE---VVVAEPEVVAQPAAPVVAEVAAE 990

                         170       180
                  ....*....|....*....|....*
gi 568933977  182 L--EPVLDSELVTPPI-EPVLEPSH 203
Cdd:PRK10811  991 VetVTAVEPEVAPAQVpEATVEHNH 1015
PRK01156 PRK01156
chromosome segregation protein; Provisional
 358-557 3.18e-03

chromosome segregation protein; Provisional


Pssm-ID: 100796 [Multi-domain]  Cd Length: 895  Bit Score: 40.66  E-value: 3.18e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568933977 358 DVLKYSQKDLDAVVNVMQQENLELKSKYEDLNtkylEMGKSVDEFEKIayKSLEEAEKQRelkeiAEDKIQKVLKERDQL 437
Cdd:PRK01156 169 DKLKDVIDMLRAEISNIDYLEEKLKSSNLELE----NIKKQIADDEKS--HSITLKEIER-----LSIEYNNAMDDYNNL 237

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568933977 438 NADLNSMeKSFSDLFKRFEKRKEVIEG-----------YQKNEESLKKYVGECIVKIEKEGQRYQALKIHAEEKlrlane 506
Cdd:PRK01156 238 KSALNEL-SSLEDMKNRYESEIKTAESdlsmeleknnyYKELEERHMKIINDPVYKNRNYINDYFKYKNDIENK------ 310

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 568933977 507 eiAQVHSKAQAEVLALQASLRKAQMQnHSLEMTLEQKTKEIDELTRICDDL 557
Cdd:PRK01156 311 --KQILSNIDAEINKYHAIIKKLSVL-QKDYNDYIKKKSRYDDLNNQILEL 358
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 376-564 3.23e-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: 40.43  E-value: 3.23e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568933977   376 QENLElksKYEDLNTkylEMGKSVDEFEKIAYKSLEEAEKQRELKEI------------------AEDKIQKVLKERDQL 437
Cdd:TIGR02168  185 RENLD---RLEDILN---ELERQLKSLERQAEKAERYKELKAELRELelallvlrleelreeleeLQEELKEAEEELEEL 258

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568933977   438 NADLNSMEKSFSDLFKRFEKRKEVIEGYQKNEESLKKYVGECIVKI----------EKEGQRYQALKIHAEEKLRLANEE 507
Cdd:TIGR02168  259 TAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKqilrerlanlERQLEELEAQLEELESKLDELAEE 338

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 568933977   508 IAQVHSK---AQAEVLALQASLRKAQMQNHSLEMTLEQKTKEIDELTRICDDLISKMEKI 564
Cdd:TIGR02168  339 LAELEEKleeLKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASL 398
PRK12704 PRK12704
phosphodiesterase; Provisional
 397-510 5.74e-03

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 39.38  E-value: 5.74e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568933977 397 KSVDEFEKIAYKSLEEAEKqrELKEIAEDKI----QKVLKERDQLNADLNSMEKSFSDLFKR--------------FEKR 458
Cdd:PRK12704  31 AKIKEAEEEAKRILEEAKK--EAEAIKKEALleakEEIHKLRNEFEKELRERRNELQKLEKRllqkeenldrklelLEKR 108

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 568933977 459 KEVIEGYQKNEESLKKYVGECIVKIEkegqryqalKIHAEEKLRLanEEIAQ 510
Cdd:PRK12704 109 EEELEKKEKELEQKQQELEKKEEELE---------ELIEEQLQEL--ERISG 149
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 364-564 7.95e-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: 39.23  E-value: 7.95e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568933977  364 QKDLDAVVNVMQQENLELKSKYEDLNTKYLEMGKSVDEFEK------IAYKS----LEEAEKQRELKEIAEDKIQKVLKE 433
Cdd:TIGR04523 428 IERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETqlkvlsRSINKikqnLEQKQKELKSKEKELKKLNEEKKE 507

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568933977  434 RDQLNADLNSMEKSFSDLFKRFEKRKEVIEG--YQKNEESLKKYVGECIVKIEKEGQRYQ----ALKiHAEEKLRLANEE 507
Cdd:TIGR04523 508 LEEKVKDLTKKISSLKEKIEKLESEKKEKESkiSDLEDELNKDDFELKKENLEKEIDEKNkeieELK-QTQKSLKKKQEE 586

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 568933977  508 IAQVHSKAQAEVLALQASLRKAQMQNHSLEMTLEQKTKEIDELTRICDDLISKMEKI 564
Cdd:TIGR04523 587 KQELIDQKEKEKKDLIKEIEEKEKKISSLEKELEKAKKENEKLSSIIKNIKSKKNKL 643
PRK12704 PRK12704
phosphodiesterase; Provisional
 456-564 8.24e-03

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 38.99  E-value: 8.24e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568933977 456 EKRKEVIEGYQKNEESLKKyvgECIVKIEKEgqrYQALKIHAEEKLRLANEEIAQVHSKAQAEVLAL---QASLRKAQMQ 532
Cdd:PRK12704  38 EEAKRILEEAKKEAEAIKK---EALLEAKEE---IHKLRNEFEKELRERRNELQKLEKRLLQKEENLdrkLELLEKREEE 111

                         90       100       110
                 ....*....|....*....|....*....|..
gi 568933977 533 NHSLEMTLEQKTKEIDELTRICDDLISKMEKI 564
Cdd:PRK12704 112 LEKKEKELEQKQQELEKKEEELEELIEEQLQE 143
 
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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