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Conserved domains on  [gi|13431935|sp|Q9JJ11|]
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RecName: Full=Transforming acidic coiled-coil-containing protein 3; AltName: Full=ARNT-interacting protein

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 ...
 429-625 6.82e-84

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: 261.53  E-value: 6.82e-84
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13431935   429 YSQKDLDAVVNVMQQEN-------LELKSKYEDLNTKYLEMGKSVDEFEKIAYKSLEEAEKQRELKEIaedKIQKVLKER 501
Cdd:pfam05010   1 YSQKDMDAALEKARNEIeekeleiNELKAKYEELRRENLEMRKIVAEFEKTIAQMIEEKQKQKELEHA---EIQKVLEEK 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13431935   502 DQLNADLNSMEKSFSDLFKRFEKRKEVIEGYQKNEESLKKYVGECIVKIEKEGQRYQALKIHAEEKLRLANEEIAQVHSK 581
Cdd:pfam05010  78 DQALADLNSVEKSFSDLFKRYEKQKEVISGYKKNEESLKKCAQDYLARIKKEEQRYQALKAHAEEKLDQANEEIAQVRSK 157

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 13431935   582 AQAEVLALQASLRKAQMQNHSLEMTLEQKTKEIDELTRICDDLI 625
Cdd:pfam05010 158 AKAETAALQASLRKEQMKVQSLERQLEQKTKENEELTKICDELI 201
rne super family cl35953
ribonuclease E; Reviewed
 144-294 6.80e-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: 6.80e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13431935   144 VTPPIEPVLEPSHQGLEPVLESELVTPPVEPVLEPSHQE----------LEPVLESELVTPPIEPVLEPSHQGLEPVLDS 213
Cdd:PRK10811  847 VVRPQDVQVEEQREAEEVQVQPVVAEVPVAAAVEPVVSApvveavaevvEEPVVVAEPQPEEVVVVETTHPEVIAAPVTE 926

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13431935   214 E--LVTPPIEPVLEPSHQGLEPVLESELVTPPIEPVLEPSHqglEPVLDSELVTPPIEPVLEPSHQglePVLDSELVTPP 291
Cdd:PRK10811  927 QpqVITESDVAVAQEVAEHAEPVVEPQDETADIEEAAETAE---VVVAEPEVVAQPAAPVVAEVAA---EVETVTAVEPE 1000


                  ...
gi 13431935   292 IEP 294
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 ...
 429-625 6.82e-84

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: 261.53  E-value: 6.82e-84
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13431935   429 YSQKDLDAVVNVMQQEN-------LELKSKYEDLNTKYLEMGKSVDEFEKIAYKSLEEAEKQRELKEIaedKIQKVLKER 501
Cdd:pfam05010   1 YSQKDMDAALEKARNEIeekeleiNELKAKYEELRRENLEMRKIVAEFEKTIAQMIEEKQKQKELEHA---EIQKVLEEK 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13431935   502 DQLNADLNSMEKSFSDLFKRFEKRKEVIEGYQKNEESLKKYVGECIVKIEKEGQRYQALKIHAEEKLRLANEEIAQVHSK 581
Cdd:pfam05010  78 DQALADLNSVEKSFSDLFKRYEKQKEVISGYKKNEESLKKCAQDYLARIKKEEQRYQALKAHAEEKLDQANEEIAQVRSK 157

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 13431935   582 AQAEVLALQASLRKAQMQNHSLEMTLEQKTKEIDELTRICDDLI 625
Cdd:pfam05010 158 AKAETAALQASLRKEQMKVQSLERQLEQKTKENEELTKICDELI 201
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 403-616 3.29e-07

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 52.91  E-value: 3.29e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13431935 403 VSAPTPVWSlEPRgLLPAEPIVDVLKYSQKDLDAVVNVMQQENLELKSKYEDLNTKYLEMGKSVDEFEK-IAYKSLEEAE 481
Cdd:COG3883   6 LAAPTPAFA-DPQ-IQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAeIAEAEAEIEE 83

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13431935 482 KQRELKEIAEDkIQKVLKERDQLNADLNSmeKSFSDLFKRF-------EKRKEVIEGYQKNEESLKKYVGEcivkIEKEG 554
Cdd:COG3883  84 RREELGERARA-LYRSGGSVSYLDVLLGS--ESFSDFLDRLsalskiaDADADLLEELKADKAELEAKKAE----LEAKL 156

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 13431935 555 QRYQALKIHAEEKLRLANEEIAQvhskAQAEVLALQASLRKAQMQNHSLEMTLEQKTKEIDE 616
Cdd:COG3883 157 AELEALKAELEAAKAELEAQQAE----QEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAA 214
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 427-619 3.06e-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: 47.37  E-value: 3.06e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13431935    427 LKYSQKDLDAVVNVMQQENLELKSKYEDLNTKYLEMG--KSVDEFEKI---------AYKSLEEAEKQREL-KEIAEDKI 494
Cdd:TIGR02169  756 VKSELKELEARIEELEEDLHKLEEALNDLEARLSHSRipEIQAELSKLeeevsrieaRLREIEQKLNRLTLeKEYLEKEI 835

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13431935    495 QKVLKERDQLNADLNSMEKSFSDLFKRFEKRKEVIEGYQKNEESLKKYVGEcivkIEKEGQRyqalkihAEEKLRLANEE 574
Cdd:TIGR02169  836 QELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGD----LKKERDE-------LEAQLRELERK 904

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*
gi 13431935    575 IAQVhsKAQAEVLALQASLRKAQMQNhslemtLEQKTKEIDELTR 619
Cdd:TIGR02169  905 IEEL--EAQIEKKRKRLSELKAKLEA------LEEELSEIEDPKG 941
PTZ00121 PTZ00121
MAEBL; Provisional
 447-619 3.41e-05

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 47.44  E-value: 3.41e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13431935   447 ELKSKYEDLNtKYLEMGKSVDEFEKIA--YKSLEEAEKQRELKEIAEDKIQKVLKERDQLNADLNSMEKSFSD-LFKRFE 523
Cdd:PTZ00121 1402 EDKKKADELK-KAAAAKKKADEAKKKAeeKKKADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKADeAKKKAE 1480

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13431935   524 KRKEVIEGYQKNEESLKKyvGECIVKIEKEGQRYQALKiHAEEKLRLanEEIAQVHSKAQAEVLALQASLRKAQMQNHSL 603
Cdd:PTZ00121 1481 EAKKADEAKKKAEEAKKK--ADEAKKAAEAKKKADEAK-KAEEAKKA--DEAKKAEEAKKADEAKKAEEKKKADELKKAE 1555

                         170
                  ....*....|....*.
gi 13431935   604 EMTLEQKTKEIDELTR 619
Cdd:PTZ00121 1556 ELKKAEEKKKAEEAKK 1571
rne PRK10811
ribonuclease E; Reviewed
 144-294 6.80e-04

ribonuclease E; Reviewed


Pssm-ID: 236766 [Multi-domain]  Cd Length: 1068  Bit Score: 42.72  E-value: 6.80e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13431935   144 VTPPIEPVLEPSHQGLEPVLESELVTPPVEPVLEPSHQE----------LEPVLESELVTPPIEPVLEPSHQGLEPVLDS 213
Cdd:PRK10811  847 VVRPQDVQVEEQREAEEVQVQPVVAEVPVAAAVEPVVSApvveavaevvEEPVVVAEPQPEEVVVVETTHPEVIAAPVTE 926

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13431935   214 E--LVTPPIEPVLEPSHQGLEPVLESELVTPPIEPVLEPSHqglEPVLDSELVTPPIEPVLEPSHQglePVLDSELVTPP 291
Cdd:PRK10811  927 QpqVITESDVAVAQEVAEHAEPVVEPQDETADIEEAAETAE---VVVAEPEVVAQPAAPVVAEVAA---EVETVTAVEPE 1000


                  ...
gi 13431935   292 IEP 294
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 ...
 429-625 6.82e-84

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: 261.53  E-value: 6.82e-84
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13431935   429 YSQKDLDAVVNVMQQEN-------LELKSKYEDLNTKYLEMGKSVDEFEKIAYKSLEEAEKQRELKEIaedKIQKVLKER 501
Cdd:pfam05010   1 YSQKDMDAALEKARNEIeekeleiNELKAKYEELRRENLEMRKIVAEFEKTIAQMIEEKQKQKELEHA---EIQKVLEEK 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13431935   502 DQLNADLNSMEKSFSDLFKRFEKRKEVIEGYQKNEESLKKYVGECIVKIEKEGQRYQALKIHAEEKLRLANEEIAQVHSK 581
Cdd:pfam05010  78 DQALADLNSVEKSFSDLFKRYEKQKEVISGYKKNEESLKKCAQDYLARIKKEEQRYQALKAHAEEKLDQANEEIAQVRSK 157

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 13431935   582 AQAEVLALQASLRKAQMQNHSLEMTLEQKTKEIDELTRICDDLI 625
Cdd:pfam05010 158 AKAETAALQASLRKEQMKVQSLERQLEQKTKENEELTKICDELI 201
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 403-616 3.29e-07

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 52.91  E-value: 3.29e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13431935 403 VSAPTPVWSlEPRgLLPAEPIVDVLKYSQKDLDAVVNVMQQENLELKSKYEDLNTKYLEMGKSVDEFEK-IAYKSLEEAE 481
Cdd:COG3883   6 LAAPTPAFA-DPQ-IQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAeIAEAEAEIEE 83

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13431935 482 KQRELKEIAEDkIQKVLKERDQLNADLNSmeKSFSDLFKRF-------EKRKEVIEGYQKNEESLKKYVGEcivkIEKEG 554
Cdd:COG3883  84 RREELGERARA-LYRSGGSVSYLDVLLGS--ESFSDFLDRLsalskiaDADADLLEELKADKAELEAKKAE----LEAKL 156

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 13431935 555 QRYQALKIHAEEKLRLANEEIAQvhskAQAEVLALQASLRKAQMQNHSLEMTLEQKTKEIDE 616
Cdd:COG3883 157 AELEALKAELEAAKAELEAQQAE----QEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAA 214
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 426-619 2.13e-05

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 47.62  E-value: 2.13e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13431935 426 VLKY------SQKDLDAVvnvmqQENL--------ELKSKYEDLNT------KYLEMGKSVDEFEKIAY-KSLEEAEKQR 484
Cdd:COG1196 167 ISKYkerkeeAERKLEAT-----EENLerledilgELERQLEPLERqaekaeRYRELKEELKELEAELLlLKLRELEAEL 241

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13431935 485 ELkeiAEDKIQKVLKERDQLNADLNSMEKSFSDLFKRFEKRKEVIEGYQKNEESLKKYVGECIVKIEKEGQRYQALKiHA 564
Cdd:COG1196 242 EE---LEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELE-ER 317

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*
gi 13431935 565 EEKLRLANEEIAQVHSKAQAEVLALQASLRKAQMQNHSLEMTLEQKTKEIDELTR 619
Cdd:COG1196 318 LEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEA 372
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
453-631 2.31e-05

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 47.45  E-value: 2.31e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13431935 453 EDLNTKYLEMGKSVDEFEKIAYKSLEEAEKQRELKEIAEDKIQKVLKERDQLNADLNSMEKSFSDL---FKRFEKRKEVI 529
Cdd:COG4717  49 ERLEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELreeLEKLEKLLQLL 128

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13431935 530 EGYQKNEEsLKKYVGECIVKIEKEGQRYQALKiHAEEKLRLANEEIAQVHSKAQAEV----LALQASLRKAQMQNHSLEM 605
Cdd:COG4717 129 PLYQELEA-LEAELAELPERLEELEERLEELR-ELEEELEELEAELAELQEELEELLeqlsLATEEELQDLAEELEELQQ 206

                       170       180
                ....*....|....*....|....*.
gi 13431935 606 TLEQKTKEIDELTRICDDLISKMEKI 631
Cdd:COG4717 207 RLAELEEELEEAQEELEELEEELEQL 232
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 427-619 3.06e-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: 47.37  E-value: 3.06e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13431935    427 LKYSQKDLDAVVNVMQQENLELKSKYEDLNTKYLEMG--KSVDEFEKI---------AYKSLEEAEKQREL-KEIAEDKI 494
Cdd:TIGR02169  756 VKSELKELEARIEELEEDLHKLEEALNDLEARLSHSRipEIQAELSKLeeevsrieaRLREIEQKLNRLTLeKEYLEKEI 835

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13431935    495 QKVLKERDQLNADLNSMEKSFSDLFKRFEKRKEVIEGYQKNEESLKKYVGEcivkIEKEGQRyqalkihAEEKLRLANEE 574
Cdd:TIGR02169  836 QELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGD----LKKERDE-------LEAQLRELERK 904

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*
gi 13431935    575 IAQVhsKAQAEVLALQASLRKAQMQNhslemtLEQKTKEIDELTR 619
Cdd:TIGR02169  905 IEEL--EAQIEKKRKRLSELKAKLEA------LEEELSEIEDPKG 941
PTZ00121 PTZ00121
MAEBL; Provisional
 447-619 3.41e-05

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 47.44  E-value: 3.41e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13431935   447 ELKSKYEDLNtKYLEMGKSVDEFEKIA--YKSLEEAEKQRELKEIAEDKIQKVLKERDQLNADLNSMEKSFSD-LFKRFE 523
Cdd:PTZ00121 1402 EDKKKADELK-KAAAAKKKADEAKKKAeeKKKADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKADeAKKKAE 1480

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13431935   524 KRKEVIEGYQKNEESLKKyvGECIVKIEKEGQRYQALKiHAEEKLRLanEEIAQVHSKAQAEVLALQASLRKAQMQNHSL 603
Cdd:PTZ00121 1481 EAKKADEAKKKAEEAKKK--ADEAKKAAEAKKKADEAK-KAEEAKKA--DEAKKAEEAKKADEAKKAEEKKKADELKKAE 1555

                         170
                  ....*....|....*.
gi 13431935   604 EMTLEQKTKEIDELTR 619
Cdd:PTZ00121 1556 ELKKAEEKKKAEEAKK 1571
PTZ00121 PTZ00121
MAEBL; Provisional
 447-630 3.50e-05

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 47.06  E-value: 3.50e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13431935   447 ELKSKYEDLNTKYLEMGKSVDEFEKIAYKSLEEAEKQRELKEIAEDKiqkvlKERDQLNADlnSMEKSFSDLFKRFEKRK 526
Cdd:PTZ00121 1319 EAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEK-----AEAAEKKKE--EAKKKADAAKKKAEEKK 1391

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13431935   527 EVIEGYQKNEESLKKyvGECIVKIEKEGQRYQALKIHAEEKlRLANEEIAQVHSKAQAEVLALQA-SLRKAQ-MQNHSLE 604
Cdd:PTZ00121 1392 KADEAKKKAEEDKKK--ADELKKAAAAKKKADEAKKKAEEK-KKADEAKKKAEEAKKADEAKKKAeEAKKAEeAKKKAEE 1468

                         170       180
                  ....*....|....*....|....*.
gi 13431935   605 MTLEQKTKEIDELTRICDDLISKMEK 630
Cdd:PTZ00121 1469 AKKADEAKKKAEEAKKADEAKKKAEE 1494
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 430-610 5.11e-05

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: 46.59  E-value: 5.11e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13431935    430 SQKDLDA-VVNVMQQENLELKSKYEDLNtkylemgKSVDEFEKIAYKSLEEAEKQRELKEIAEDKIQKVLKERDQLNADL 508
Cdd:TIGR02168  330 SKLDELAeELAELEEKLEELKEELESLE-------AELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEI 402

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13431935    509 NSMEKSFSDLFKRFEKRKEVIEGYQKN-EESLKKYVGECIVKIEKEGQRYQALKIHAEEKLRLANEEIAQvhskAQAEVL 587
Cdd:TIGR02168  403 ERLEARLERLEDRRERLQQEIEELLKKlEEAELKELQAELEELEEELEELQEELERLEEALEELREELEE----AEQALD 478

                          170       180
                   ....*....|....*....|...
gi 13431935    588 ALQASLRKAQMQNHSLEMTLEQK 610
Cdd:TIGR02168  479 AAERELAQLQARLDSLERLQENL 501
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 433-617 6.72e-05

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: 46.20  E-value: 6.72e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13431935    433 DLDAVVNVMQQENLELKSKYEDLNTKYLEMGKSVDEFEKIAYKSLEEAEKQRELKEIAED-------KIQKVLKERDQLN 505
Cdd:TIGR02168  751 QLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAeltllneEAANLRERLESLE 830

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13431935    506 ADLNSMEKSFSDLFKRFEKRKEVIEGYQKNEESLkkyvGECIVKIEKEGQRYQALKIHAEEKLRLANEEIAQVHSKAQA- 584
Cdd:TIGR02168  831 RRIAATERRLEDLEEQIEELSEDIESLAAEIEEL----EELIEELESELEALLNERASLEEALALLRSELEELSEELREl 906

                          170       180       190
                   ....*....|....*....|....*....|....*
gi 13431935    585 --EVLALQASLRKAQMQNHSLEMTLEQKTKEIDEL 617
Cdd:TIGR02168  907 esKRSELRRELEELREKLAQLELRLEGLEVRIDNL 941
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 442-619 1.30e-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: 44.75  E-value: 1.30e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13431935 442 QQENLELKSKYEDLNTKYLEMGKSVDEFEKIAYKSLEEAEKQRELKEIAEDKIQKVLKERDQLNADLNSMEKSFSDLFKR 521
Cdd:COG4942  19 ADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAE 98

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13431935 522 FEKRKEVIEG-----YQKNEESLKKYV--GECIVKIEKEGQRYQALKIHAE---EKLRLANEEIAQVHSKAQAEVLALQA 591
Cdd:COG4942  99 LEAQKEELAEllralYRLGRQPPLALLlsPEDFLDAVRRLQYLKYLAPARReqaEELRADLAELAALRAELEAERAELEA 178

                       170       180
                ....*....|....*....|....*...
gi 13431935 592 SLRKAQMQNHSLEMTLEQKTKEIDELTR 619
Cdd:COG4942 179 LLAELEEERAALEALKAERQKLLARLEK 206
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
447-597 2.43e-04

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 44.28  E-value: 2.43e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13431935  447 ELKSKYEDLN------TKYLEMGKSVDEFEKIAYKSLEEAEKQRELKEiaedKIQKVLKERDQLNADLNSMEKSFSDLFK 520
Cdd:PRK03918 277 ELEEKVKELKelkekaEEYIKLSEFYEEYLDELREIEKRLSRLEEEIN----GIEERIKELEEKEERLEELKKKLKELEK 352

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13431935  521 RFEKRKEVIEGYQK------NEESLKKYV-GECIVKIEKEGQRYQALKIHAEEKLRLANEEIAQVHSKAQAEVLALQAsL 593
Cdd:PRK03918 353 RLEELEERHELYEEakakkeELERLKKRLtGLTPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEE-L 431


                 ....
gi 13431935  594 RKAQ 597
Cdd:PRK03918 432 KKAK 435
HEC1 COG5185
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ...
 442-629 2.78e-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: 43.79  E-value: 2.78e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13431935 442 QQENLELKSKYEDLNTKYLEMGKSVDEFEKIAYKSL-EEAEKQRELKEIAEDKIQKVLKERDQL--NADLNSMEKSFSDL 518
Cdd:COG5185 235 LKGFQDPESELEDLAQTSDKLEKLVEQNTDLRLEKLgENAESSKRLNENANNLIKQFENTKEKIaeYTKSIDIKKATESL 314

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13431935 519 ---FKRFEKRKEVIEGYQKNEESLKKYVGECIVKIEKEGQRYQALK-----IHAEEKLRLANEEI----AQVHSKAQAEV 586
Cdd:COG5185 315 eeqLAAAEAEQELEESKRETETGIQNLTAEIEQGQESLTENLEAIKeeienIVGEVELSKSSEELdsfkDTIESTKESLD 394

                       170       180       190       200
                ....*....|....*....|....*....|....*....|...
gi 13431935 587 LALQASLRKAQMQNHSLEMTLEQKTKEIDELTRICDDLISKME 629
Cdd:COG5185 395 EIPQNQRGYAQEILATLEDTLKAADRQIEELQRQIEQATSSNE 437
PTZ00121 PTZ00121
MAEBL; Provisional
 447-630 3.16e-04

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 43.98  E-value: 3.16e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13431935   447 ELKSKYEDLntKYLEMGKSVDEFEKIAykslEEAEKQRELKEIAE------DKIQKVLKERDQLNADLNSMEKSFSDLFK 520
Cdd:PTZ00121 1287 EEKKKADEA--KKAEEKKKADEAKKKA----EEAKKADEAKKKAEeakkkaDAAKKKAEEAKKAAEAAKAEAEAAADEAE 1360

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13431935   521 RFEKRKEVIEgyQKNEESLKKyvGECIVKIEKEGQRYQALKIHAEEKLRLANEEIAQVHSKAQAEVLALQA-SLRKA-QM 598
Cdd:PTZ00121 1361 AAEEKAEAAE--KKKEEAKKK--ADAAKKKAEEKKKADEAKKKAEEDKKKADELKKAAAAKKKADEAKKKAeEKKKAdEA 1436

                         170       180       190
                  ....*....|....*....|....*....|..
gi 13431935   599 QNHSLEMTLEQKTKEIDELTRICDDLISKMEK 630
Cdd:PTZ00121 1437 KKKAEEAKKADEAKKKAEEAKKAEEAKKKAEE 1468
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 466-617 3.39e-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: 43.90  E-value: 3.39e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13431935    466 VDEFEKIAYKSLEEAEKQRELKEIAEDKIQKVLKERDQLNADLNSMEKsfsdlFKRFEKRKEVIEGY------QKNEESL 539
Cdd:TIGR02169  165 VAEFDRKKEKALEELEEVEENIERLDLIIDEKRQQLERLRREREKAER-----YQALLKEKREYEGYellkekEALERQK 239

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13431935    540 KKYVGEcIVKIEKEGQ----RYQALKIHAEEKLRLANEEIAQVHSKAQAEVLALQASLRKAQMQNHSLEMTLEQKTKEID 615
Cdd:TIGR02169  240 EAIERQ-LASLEEELEklteEISELEKRLEEIEQLLEELNKKIKDLGEEEQLRVKEKIGELEAEIASLERSIAEKERELE 318


                   ..
gi 13431935    616 EL 617
Cdd:TIGR02169  319 DA 320
rne PRK10811
ribonuclease E; Reviewed
 144-294 6.80e-04

ribonuclease E; Reviewed


Pssm-ID: 236766 [Multi-domain]  Cd Length: 1068  Bit Score: 42.72  E-value: 6.80e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13431935   144 VTPPIEPVLEPSHQGLEPVLESELVTPPVEPVLEPSHQE----------LEPVLESELVTPPIEPVLEPSHQGLEPVLDS 213
Cdd:PRK10811  847 VVRPQDVQVEEQREAEEVQVQPVVAEVPVAAAVEPVVSApvveavaevvEEPVVVAEPQPEEVVVVETTHPEVIAAPVTE 926

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13431935   214 E--LVTPPIEPVLEPSHQGLEPVLESELVTPPIEPVLEPSHqglEPVLDSELVTPPIEPVLEPSHQglePVLDSELVTPP 291
Cdd:PRK10811  927 QpqVITESDVAVAQEVAEHAEPVVEPQDETADIEEAAETAE---VVVAEPEVVAQPAAPVVAEVAA---EVETVTAVEPE 1000


                  ...
gi 13431935   292 IEP 294
Cdd:PRK10811 1001 VAP 1003
235kDa-fam TIGR01612
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ...
 423-624 9.20e-04

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: 42.73  E-value: 9.20e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13431935    423 IVDVLKYSQKDLDAVVNVMQQENLEL---KSKYEDLNTKYLEMGKSVDEFEKIAYKSLEEAEKQRELKEIAEDKIQKVLK 499
Cdd:TIGR01612  756 ILEDFKNKEKELSNKINDYAKEKDELnkyKSKISEIKNHYNDQINIDNIKDEDAKQNYDKSKEYIKTISIKEDEIFKIIN 835

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13431935    500 ERDQLNAD------------------LNSMEKSFSDLFKRF--EKRKEVIEGYQKNEESLKKYVGECIVKIEKEGQRYQA 559
Cdd:TIGR01612  836 EMKFMKDDflnkvdkfinfennckekIDSEHEQFAELTNKIkaEISDDKLNDYEKKFNDSKSLINEINKSIEEEYQNINT 915

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 13431935    560 LKiHAEEKLRL---ANEEIAQVHSKAQAEVLALQASLRKAQMQNhSLEMTLEQK-----TKEIDELTRICDDL 624
Cdd:TIGR01612  916 LK-KVDEYIKIcenTKESIEKFHNKQNILKEILNKNIDTIKESN-LIEKSYKDKfdntlIDKINELDKAFKDA 986
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 476-631 9.21e-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: 42.35  E-value: 9.21e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13431935    476 SLEEAEKQRelkEIAEDKIQKVLKERDQLNADLNSMEKSFSDLFKRFEKRKEVIEGYQKNEESLKKYVGECIVKIEKEGQ 555
Cdd:TIGR02168  692 KIAELEKAL---AELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEE 768

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13431935    556 RY---QALKIHAEEKLRLANEEIAQV----------HSKAQAEVLALQASLRKAQMQNHSLEMTLEQKTKEIDELTRICD 622
Cdd:TIGR02168  769 RLeeaEEELAEAEAEIEELEAQIEQLkeelkalreaLDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIE 848


                   ....*....
gi 13431935    623 DLISKMEKI 631
Cdd:TIGR02168  849 ELSEDIESL 857
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 443-631 1.54e-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: 41.97  E-value: 1.54e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13431935    443 QENLElksKYEDLNTkylEMGKSVDEFEKIAYKSLEEAEKQRELKEI------------------AEDKIQKVLKERDQL 504
Cdd:TIGR02168  185 RENLD---RLEDILN---ELERQLKSLERQAEKAERYKELKAELRELelallvlrleelreeleeLQEELKEAEEELEEL 258

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13431935    505 NADLNSMEKSFSDLFKRFEKRKEVIEGYQKNEESLKkyvgECIVKIEKEGQRYQALKIHAEEKLRLANEEIAQVHSK--- 581
Cdd:TIGR02168  259 TAELQELEEKLEELRLEVSELEEEIEELQKELYALA----NEISRLEQQKQILRERLANLERQLEELEAQLEELESKlde 334

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 13431935    582 --------------AQAEVLALQASLRKAQMQNHSLEMTLEQKTKEIDELTRICDDLISKMEKI 631
Cdd:TIGR02168  335 laeelaeleekleeLKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASL 398
PRK01156 PRK01156
chromosome segregation protein; Provisional
 425-624 1.73e-03

chromosome segregation protein; Provisional


Pssm-ID: 100796 [Multi-domain]  Cd Length: 895  Bit Score: 41.43  E-value: 1.73e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13431935  425 DVLKYSQKDLDAVVNVMQQENLELKSKYEDLNtkylEMGKSVDEFEKIayKSLEEAEKQRelkeiAEDKIQKVLKERDQL 504
Cdd:PRK01156 169 DKLKDVIDMLRAEISNIDYLEEKLKSSNLELE----NIKKQIADDEKS--HSITLKEIER-----LSIEYNNAMDDYNNL 237

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13431935  505 NADLNSMeKSFSDLFKRFEKRKEVIEG-----------YQKNEESLKKYVGECIVKIEKEGQRYQALKIHAEEKlrlane 573
Cdd:PRK01156 238 KSALNEL-SSLEDMKNRYESEIKTAESdlsmeleknnyYKELEERHMKIINDPVYKNRNYINDYFKYKNDIENK------ 310

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 13431935  574 eiAQVHSKAQAEVLALQASLRKAQMQnHSLEMTLEQKTKEIDELTRICDDL 624
Cdd:PRK01156 311 --KQILSNIDAEINKYHAIIKKLSVL-QKDYNDYIKKKSRYDDLNNQILEL 358
PTZ00121 PTZ00121
MAEBL; Provisional
 447-631 1.73e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 41.67  E-value: 1.73e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13431935   447 ELKSKYEDLNTKYLEMGKSVDEF----EKIAYKSLEEAEKQRELKEIAEDKIQKVLKERDQLNADLNSME--KSFSDLFK 520
Cdd:PTZ00121 1630 EEKKKVEQLKKKEAEEKKKAEELkkaeEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEeaKKAEELKK 1709

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13431935   521 RFEKRKEVIEGYQKNEESLKKYVGECIVKIEKEGQRYQALKIHAEEKLRLAneeiaqvHSKAQAEVLALQASLRKAQMQN 600
Cdd:PTZ00121 1710 KEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEEKKKIA-------HLKKEEEKKAEEIRKEKEAVIE 1782

                         170       180       190
                  ....*....|....*....|....*....|.
gi 13431935   601 HSLEMTLEQKTKEIDELTRicdDLISKMEKI 631
Cdd:PTZ00121 1783 EELDEEDEKRRMEVDKKIK---DIFDNFANI 1810
DUF4407 pfam14362
Domain of unknown function (DUF4407); This family of proteins is found in bacteria. Proteins ...
 403-594 1.89e-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: 1.89e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13431935   403 VSAPTPVWSLEPRGLLP-------AEPIVdvLKYSQKDLDAVVNVMQQEnlelkskyedlntkylemgksvdefekiayk 475
Cdd:pfam14362  72 VSGRRELALALPRLLLAvligvviSEPLE--LKIFEKEIDRELLEIQQE------------------------------- 118

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13431935   476 slEEAEKQRELKEIAEDKIQKVLKERDQLNADLNSMEKSFSDLFKrfEKRKEvIEGYQKNEESLKKYVGECIVK---IEK 552
Cdd:pfam14362 119 --EADAAKAQLAAAYRARLAELEAQIAALDAEIDAAEARLDALQA--EARCE-LDGTPGTGTGVPGDGPVAKTKqaqLDA 193

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 13431935   553 EGQRYQALKIHAEEKLRLANEEIAQVHSKAQAEVLALQASLR 594
Cdd:pfam14362 194 AQAELAALQAQNDARLAALRAELARLTAERAAARARSQAAID 235
EzrA pfam06160
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ...
 442-630 2.68e-03

Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like cell-division protein FtsZ polymerizes into a ring structure that establishes the location of the nascent division site. EzrA modulates the frequency and position of FtsZ ring formation. The structure contains 5 spectrin like alpha helical repeats.


Pssm-ID: 428797 [Multi-domain]  Cd Length: 542  Bit Score: 40.61  E-value: 2.68e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13431935   442 QQENLELKSKYEDLNTKYLE----MGKSVDEFEKIayksLEEAEKQR----ELKE----IAEDKIQKVLKER-DQLNADL 508
Cdd:pfam06160 120 REEVEELKDKYRELRKTLLAnrfsYGPAIDELEKQ----LAEIEEEFsqfeELTEsgdyLEAREVLEKLEEEtDALEELM 195

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13431935   509 NSMEKSFSDLFKRFEKR-KEVIEGYQKNEEslKKY------VGECIVKIEKEGQRYQA----LKI-HAEEKLRLANEEIA 576
Cdd:pfam06160 196 EDIPPLYEELKTELPDQlEELKEGYREMEE--EGYalehlnVDKEIQQLEEQLEENLAllenLELdEAEEALEEIEERID 273

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13431935   577 QVHSKAQAEVLA----------LQASLRKAQMQNHSL--EMTLEQKT---------------KEIDELTRICDDLISKME 629
Cdd:pfam06160 274 QLYDLLEKEVDAkkyveknlpeIEDYLEHAEEQNKELkeELERVQQSytlnenelervrgleKQLEELEKRYDEIVERLE 353


                  .
gi 13431935   630 K 630
Cdd:pfam06160 354 E 354
PRK12704 PRK12704
phosphodiesterase; Provisional
 464-577 2.91e-03

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 40.53  E-value: 2.91e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13431935  464 KSVDEFEKIAYKSLEEAEKqrELKEIAEDKI----QKVLKERDQLNADLNSMEKSFSDLFKR--------------FEKR 525
Cdd:PRK12704  31 AKIKEAEEEAKRILEEAKK--EAEAIKKEALleakEEIHKLRNEFEKELRERRNELQKLEKRllqkeenldrklelLEKR 108

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 13431935  526 KEVIEGYQKNEESLKKYVGECIVKIEkegqryqalKIHAEEKLRLanEEIAQ 577
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 ...
 431-631 3.41e-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: 40.39  E-value: 3.41e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13431935   431 QKDLDAVVNVMQQENLELKSKYEDLNTKYLEMGKSVDEFEK------IAYKSL---------EEAEKQRELKEIAEDKIQ 495
Cdd:TIGR04523 428 IERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETqlkvlsRSINKIkqnleqkqkELKSKEKELKKLNEEKKE 507

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13431935   496 -----KVLKER--------DQLNADLNSMEKSFSDLFKRFEKRKEViegyqKNEESLKKYVGECIVKIEKegqryqaLKi 562
Cdd:TIGR04523 508 leekvKDLTKKisslkekiEKLESEKKEKESKISDLEDELNKDDFE-----LKKENLEKEIDEKNKEIEE-------LK- 574

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 13431935   563 HAEEKLRLANEEIAQVHSKAQAEVLALQASLRKAQMQNHSLEMTLEQKTKEIDELTRICDDLISKMEKI 631
Cdd:TIGR04523 575 QTQKSLKKKQEEKQELIDQKEKEKKDLIKEIEEKEKKISSLEKELEKAKKENEKLSSIIKNIKSKKNKL 643
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
447-631 3.47e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 40.43  E-value: 3.47e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13431935  447 ELKSKYEDLNtKYLEMGKSVDEFEKIAYKSLEeaEKQRELKEIaEDKIQKVLKERDQLNADLnsmeksfsdlfKRFEKRK 526
Cdd:PRK03918 173 EIKRRIERLE-KFIKRTENIEELIKEKEKELE--EVLREINEI-SSELPELREELEKLEKEV-----------KELEELK 237

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13431935  527 EVIEGYQKNEESLKKYVGECIVKIEKEGQRYQALKIHAEEkLRLANEEIAQVHSKAQaEVLALQASLRKAQMQNHSLEMT 606
Cdd:PRK03918 238 EEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEE-LEEKVKELKELKEKAE-EYIKLSEFYEEYLDELREIEKR 315

                        170       180
                 ....*....|....*....|....*
gi 13431935  607 LEQKTKEIDELTRICDDLISKMEKI 631
Cdd:PRK03918 316 LSRLEEEINGIEERIKELEEKEERL 340
rne PRK10811
ribonuclease E; Reviewed
 99-276 3.50e-03

ribonuclease E; Reviewed


Pssm-ID: 236766 [Multi-domain]  Cd Length: 1068  Bit Score: 40.41  E-value: 3.50e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13431935    99 PLAPVDDAPVV-QMAAEILRAEGELQEgiltssslSASTSLLDSELVTPPIEPVLEPSHqglEPVLESELVTPPVEPVlE 177
Cdd:PRK10811  846 PVVRPQDVQVEeQREAEEVQVQPVVAE--------VPVAAAVEPVVSAPVVEAVAEVVE---EPVVVAEPQPEEVVVV-E 913

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13431935   178 PSHQEL--EPVLES-ELVTPPIEPVLEPSHQGLEPVLDSELVTPPIEPVLEPSHqglEPVLESELVTPPIEPVLEPSHQG 254
Cdd:PRK10811  914 TTHPEViaAPVTEQpQVITESDVAVAQEVAEHAEPVVEPQDETADIEEAAETAE---VVVAEPEVVAQPAAPVVAEVAAE 990

                         170       180
                  ....*....|....*....|....*
gi 13431935   255 L--EPVLDSELVTPPI-EPVLEPSH 276
Cdd:PRK10811  991 VetVTAVEPEVAPAQVpEATVEHNH 1015
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
447-631 4.72e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 40.05  E-value: 4.72e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13431935  447 ELKSKYEDLNTKYLEmgKSVDEFEKIAYKSLEEAEKQRELKEIAEdKIQKVLKERDQLNADLNSMEKSFSDLFKR----- 521
Cdd:PRK03918 507 ELEEKLKKYNLEELE--KKAEEYEKLKEKLIKLKGEIKSLKKELE-KLEELKKKLAELEKKLDELEEELAELLKEleelg 583

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13431935  522 FEKRKEVIEGYQKNEESLKKYVGecIVKIEKEGQRYQALKIHAEEKLRLANEEIAQVHSKAQAEVLALQASLRKAQMQNH 601
Cdd:PRK03918 584 FESVEELEERLKELEPFYNEYLE--LKDAEKELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELEKKYSEEEY 661

                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 13431935  602 --------SLEMTLEQKTKEIDELTRICDDLISKMEKI 631
Cdd:PRK03918 662 eelreeylELSRELAGLRAELEELEKRREEIKKTLEKL 699
PRK12704 PRK12704
phosphodiesterase; Provisional
 523-631 5.40e-03

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 39.76  E-value: 5.40e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13431935  523 EKRKEVIEGYQKNEESLKKyvgECIVKIEKEgqrYQALKIHAEEKLRLANEEIAQVHSKAQAEVLAL---QASLRKAQMQ 599
Cdd:PRK12704  38 EEAKRILEEAKKEAEAIKK---EALLEAKEE---IHKLRNEFEKELRERRNELQKLEKRLLQKEENLdrkLELLEKREEE 111

                         90       100       110
                 ....*....|....*....|....*....|..
gi 13431935  600 NHSLEMTLEQKTKEIDELTRICDDLISKMEKI 631
Cdd:PRK12704 112 LEKKEKELEQKQQELEKKEEELEELIEEQLQE 143
HlpA COG2825
Periplasmic chaperone for outer membrane proteins, Skp family [Cell wall/membrane/envelope ...
 471-586 6.11e-03

Periplasmic chaperone for outer membrane proteins, Skp family [Cell wall/membrane/envelope biogenesis, Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 442073 [Multi-domain]  Cd Length: 171  Bit Score: 37.89  E-value: 6.11e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13431935 471 KIAYKSLEEAEKQRELKEIAEDKIQKvlkERDQLNADLNSMEKSFSDLFKRFEKRKEVIegyqkNEESLKKYVGEcIVKI 550
Cdd:COG2825  25 KIGVVDVQRILQESPEGKAAQKKLEK---EFKKRQAELQKLEKELQALQEKLQKEAATL-----SEEERQKKERE-LQKK 95

                        90       100       110
                ....*....|....*....|....*....|....*..
gi 13431935 551 EKEGQRYQALkihAEEKLRLA-NEEIAQVHSKAQAEV 586
Cdd:COG2825  96 QQELQRKQQE---AQQDLQKRqQELLQPILEKIQKAI 129
tolA PRK09510
cell envelope integrity inner membrane protein TolA; Provisional
 475-596 8.62e-03

cell envelope integrity inner membrane protein TolA; Provisional


Pssm-ID: 236545 [Multi-domain]  Cd Length: 387  Bit Score: 39.02  E-value: 8.62e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13431935  475 KSLEEAEKQRELKE--IAEDKIQKVLKERDQLNADLNSMEKSFSDLFKRFEKRKEVIEGYQKNEESLKKYVGECIVKIEK 552
Cdd:PRK09510  72 KSAKRAEEQRKKKEqqQAEELQQKQAAEQERLKQLEKERLAAQEQKKQAEEAAKQAALKQKQAEEAAAKAAAAAKAKAEA 151

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 13431935  553 EGQRYQALKIHAEEKLRLANEEIAQVHSKAQAEVLALQASLRKA 596
Cdd:PRK09510 152 EAKRAAAAAKKAAAEAKKKAEAEAAKKAAAEAKKKAEAEAAAKA 195
 
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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