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Conserved domains on  [gi|7662234|ref|NP_055515|]
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rab11 family-interacting protein 3 isoform 1 [Homo sapiens]

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List of domain hits

Name Accession Description Interval E-value
RBD-FIP pfam09457
FIP domain; The FIP domain is the Rab11-binding domain (RBD) at the C-terminus of a family of ...
716-756 1.12e-11

FIP domain; The FIP domain is the Rab11-binding domain (RBD) at the C-terminus of a family of Rab11-interacting proteins (FIPs). The Rab proteins constitute the largest family of small GTPases (>60 members in mammals). Among them Rab11 is a well characterized regulator of endocytic and recycling pathways. Rab11 associates with a broad range of post-Golgi organelles, including recycling endosomes.


:

Pssm-ID: 255374  Cd Length: 48  Bit Score: 61.22  E-value: 1.12e-11
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 7662234    716 SRDELMEAIQKQEEINFR-------LQDYIDRIIVAIMETNPSILEVK 756
Cdd:pfam09457   1 SRDELIQELLKQEEENRRkdqhvreLEDYIDNLLVRIMEHTPSILEVP 48
EFh cd00051
EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal ...
206-264 5.34e-05

EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal modulators; most examples in this alignment model have 2 active canonical EF hands. Ca2+ binding induces a conformational change in the EF-hand motif, leading to the activation or inactivation of target proteins. EF-hands tend to occur in pairs or higher copy numbers.


:

Pssm-ID: 238008 [Multi-domain]  Cd Length: 63  Bit Score: 41.76  E-value: 5.34e-05
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 7662234  206 RLRAVFDALDGDGDGFVRIEDFIQFATVYGAEQVKDLTKYL----DPSGLGVISFEDFYQGIT 264
Cdd:cd00051   1 ELREAFRLFDKDGDGTISADELKAALKSLGEGLSEEEIDEMirevDKDGDGKIDFEEFLELMA 63
RILP-like super family cl18042
Rab interacting lysosomal protein-like 1 and 2 (Rilpl1 and Rilpl2); This domain is found in ...
493-592 4.33e-04

Rab interacting lysosomal protein-like 1 and 2 (Rilpl1 and Rilpl2); This domain is found in Rab interacting lysosomal protein-like 1 and 2, and appears to be conserved in Bilateria. The Rilp-like proteins regulate the concentration of ciliary membrane proteins in the primary cilium. Rilpl2 interacts with myosin-Va and has been linked to the regulation of cellular morphology in neurons; it forms a complex with Rac1 and activates Rac1-Pak signaling, dependent on myosin-Va.


The actual alignment was detected with superfamily member pfam09744:

Pssm-ID: 271823  Cd Length: 158  Bit Score: 40.16  E-value: 4.33e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7662234    493 ENLQLVHRANAlEEQLKEQELRACEMVLE-ETRRQKELLcKMEREKSIEIEN--------LQTRLQQLDEENSELRSCTP 563
Cdd:pfam09744  36 ENLDSLVSENQ-NLEVELLLLREDNEQLStQYEREKELR-KQAEEKLIELEDvlegekkeLQNKIEQLEENVRQLELKAK 113
                          90       100
                  ....*....|....*....|....*....
gi 7662234    564 CLKANIERLEEEKQKLLDEIESLTLRLSE 592
Cdd:pfam09744 114 NLADQISRLEERETELKKEYNALHERYTE 142
bZIP super family cl21462
Basic leucine zipper (bZIP) domain of bZIP transcription factors: a DNA-binding and ...
656-684 1.75e-03

Basic leucine zipper (bZIP) domain of bZIP transcription factors: a DNA-binding and dimerization domain; Basic leucine zipper (bZIP) factors comprise one of the most important classes of enhancer-type transcription factors. They act in networks of homo and heterodimers in the regulation of a diverse set of cellular processes including cell survival, learning and memory, lipid metabolism, and cancer progression, among others. They also play important roles in responses to stimuli or stress signals such as cytokines, genotoxic agents, or physiological stresses. The bZIP structural motif contains a basic region and a leucine zipper, composed of alpha helices with leucine residues 7 amino acids apart, which stabilize dimerization with a parallel leucine zipper domain. Dimerization of leucine zippers creates a pair of the adjacent basic regions that bind DNA and undergo conformational change. Dimerization occurs in a specific and predictable manner resulting in hundreds of dimers having unique effects on transcription.


The actual alignment was detected with superfamily member cd14707:

Pssm-ID: 276305  Cd Length: 55  Bit Score: 37.29  E-value: 1.75e-03
                        10        20        30
                ....*....|....*....|....*....|...
gi 7662234  656 SRAR----ESELEQEVRRLKQDNRNLKEQNEEL 684
Cdd:cd14707  16 SRARkqayTNELELEVAHLKEENARLKRQQEEL 48
HAUS-augmin3 super family cl22400
HAUS augmin-like complex subunit 3; This domain is subunit three of the augmin complex found ...
602-707 2.35e-03

HAUS augmin-like complex subunit 3; This domain is subunit three of the augmin complex found from Drosophila to humans. The HAUS-augmin complex is made up of eight subunits. The augmin complex interacts with gamma-TuRC, and attenuation of this interaction severely impairs spindle MT generation. Furthermore, we provide evidence that human augmin plays critical and non-redundant roles in the kinetochore-MT attachment and also central spindle formation during anaphase in human cells.The HAUS complex is required for mitotic spindle assembly and for maintenance of centrosome integrity.


The actual alignment was detected with superfamily member pfam14932:

Pssm-ID: 259069  Cd Length: 253  Bit Score: 39.27  E-value: 2.35e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7662234    602 DRLSHErhqFQRDKEATQELIEDLRKQLEHLQLLKLEAEQRRGRSSSMG-LQEYHSRARESELEQEVRRLKQDNRNLKEQ 680
Cdd:pfam14932  53 DTISAE---SSGLLDQTEEDIEALEDELEALAEAEELYIQLRNKLQQTDsLLSQELSELEGKLERAAAVLQAEEQLLLAM 129
                          90       100
                  ....*....|....*....|....*..
gi 7662234    681 NEELNGQIitLSIQGAKSLFSTAFSES 707
Cdd:pfam14932 130 LQKRNLEL--QELQGEVAKLSQELQHY 154
PspA COG1842
Phage shock protein A (IM30), suppresses sigma54-dependent transcription [Transcription / ...
459-674 3.68e-07

Phage shock protein A (IM30), suppresses sigma54-dependent transcription [Transcription / Signal transduction mechanisms]


:

Pssm-ID: 224755 [Multi-domain]  Cd Length: 225  Bit Score: 50.39  E-value: 3.68e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7662234  459 EEDIADKVVFLERRVLELEkdtaatgEQHSRLRQENLQLVHRANALEEQLKEQELRACEMvleETRRQKELLCKME---R 535
Cdd:COG1842  19 LDKAEDPEKMLEQAIRDME-------SELAKARQALAQAIARQKQLERKLEEAQARAEKL---EEKAELALQAGNEdlaR 88
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7662234  536 EKSIEIENLQTRLQQLDEENSELRSCTPCLKANIERLEEEKQKLLDEIESLTLRLSEE--QENKRRMGDRLSHER--HQF 611
Cdd:COG1842  89 EALEEKQSLEDLAKALEAELQQAEEQVEKLKKQLAALEQKIAELRAKKEALKARKAAAkaQEKVNRSLGGGSSSSamAAF 168
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 7662234  612 QR--DKEATQELIEDLRKQLEHLQLLKLEAEQRrgrsssmglQEYHSRARESELEQEVRRLKQDN 674
Cdd:COG1842 169 ERmeEKIEEREARAEAAAELAEGSGDDLDKEFA---------QAGAQSAVDSRLAALKARMKGPA 224
EF-hand_7 pfam13499
EF-hand domain pair;
212-263 5.51e-06

EF-hand domain pair;


:

Pssm-ID: 257819 [Multi-domain]  Cd Length: 60  Bit Score: 44.68  E-value: 5.51e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 7662234    212 DALDGDGDGFVRIEDFIQFATVYGA--------EQVKDLTKYLDPSGLGVISFEDFYQGI 263
Cdd:pfam13499   1 KLLDKDGDGYIDVEELRKLLKALGLkltdeeveELLEYDFNEFDKDGDGRISFEEFLEAY 60
 
Name Accession Description Interval E-value
RBD-FIP pfam09457
FIP domain; The FIP domain is the Rab11-binding domain (RBD) at the C-terminus of a family of ...
716-756 1.12e-11

FIP domain; The FIP domain is the Rab11-binding domain (RBD) at the C-terminus of a family of Rab11-interacting proteins (FIPs). The Rab proteins constitute the largest family of small GTPases (>60 members in mammals). Among them Rab11 is a well characterized regulator of endocytic and recycling pathways. Rab11 associates with a broad range of post-Golgi organelles, including recycling endosomes.


Pssm-ID: 255374  Cd Length: 48  Bit Score: 61.22  E-value: 1.12e-11
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 7662234    716 SRDELMEAIQKQEEINFR-------LQDYIDRIIVAIMETNPSILEVK 756
Cdd:pfam09457   1 SRDELIQELLKQEEENRRkdqhvreLEDYIDNLLVRIMEHTPSILEVP 48
EFh cd00051
EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal ...
206-264 5.34e-05

EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal modulators; most examples in this alignment model have 2 active canonical EF hands. Ca2+ binding induces a conformational change in the EF-hand motif, leading to the activation or inactivation of target proteins. EF-hands tend to occur in pairs or higher copy numbers.


Pssm-ID: 238008 [Multi-domain]  Cd Length: 63  Bit Score: 41.76  E-value: 5.34e-05
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 7662234  206 RLRAVFDALDGDGDGFVRIEDFIQFATVYGAEQVKDLTKYL----DPSGLGVISFEDFYQGIT 264
Cdd:cd00051   1 ELREAFRLFDKDGDGTISADELKAALKSLGEGLSEEEIDEMirevDKDGDGKIDFEEFLELMA 63
Jnk-SapK_ap_N pfam09744
JNK_SAPK-associated protein-1; This is the N-terminal 200 residues of a set of proteins ...
493-592 4.33e-04

JNK_SAPK-associated protein-1; This is the N-terminal 200 residues of a set of proteins conserved from yeasts to humans. Most of the proteins in this entry have an RhoGEF pfam00621 domain at their C-terminal end.


Pssm-ID: 255525  Cd Length: 158  Bit Score: 40.16  E-value: 4.33e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7662234    493 ENLQLVHRANAlEEQLKEQELRACEMVLE-ETRRQKELLcKMEREKSIEIEN--------LQTRLQQLDEENSELRSCTP 563
Cdd:pfam09744  36 ENLDSLVSENQ-NLEVELLLLREDNEQLStQYEREKELR-KQAEEKLIELEDvlegekkeLQNKIEQLEENVRQLELKAK 113
                          90       100
                  ....*....|....*....|....*....
gi 7662234    564 CLKANIERLEEEKQKLLDEIESLTLRLSE 592
Cdd:pfam09744 114 NLADQISRLEERETELKKEYNALHERYTE 142
bZIP_plant_BZIP46 cd14707
Basic leucine zipper (bZIP) domain of uncharaterized Plant BZIP transcription factors: a ...
656-684 1.75e-03

Basic leucine zipper (bZIP) domain of uncharaterized Plant BZIP transcription factors: a DNA-binding and dimerization domain; This subfamily is composed of uncharacterized plant bZIP transciption factors with similarity to Glycine max BZIP46, which may be a drought-responsive gene. Plant bZIPs are involved in developmental and physiological processes in response to stimuli/stresses such as light, hormones, and temperature changes. bZIP factors act in networks of homo and heterodimers in the regulation of a diverse set of cellular processes. The bZIP structural motif contains a basic region and a leucine zipper, composed of alpha helices with leucine residues 7 amino acids apart, which stabilize dimerization with a parallel leucine zipper domain. Dimerization of leucine zippers creates a pair of the adjacent basic regions that bind DNA and undergo conformational change. Dimerization occurs in a specific and predictable manner resulting in hundreds of dimers having unique effects on transcription.


Pssm-ID: 269855  Cd Length: 55  Bit Score: 37.29  E-value: 1.75e-03
                        10        20        30
                ....*....|....*....|....*....|...
gi 7662234  656 SRAR----ESELEQEVRRLKQDNRNLKEQNEEL 684
Cdd:cd14707  16 SRARkqayTNELELEVAHLKEENARLKRQQEEL 48
HAUS-augmin3 pfam14932
HAUS augmin-like complex subunit 3; This domain is subunit three of the augmin complex found ...
602-707 2.35e-03

HAUS augmin-like complex subunit 3; This domain is subunit three of the augmin complex found from Drosophila to humans. The HAUS-augmin complex is made up of eight subunits. The augmin complex interacts with gamma-TuRC, and attenuation of this interaction severely impairs spindle MT generation. Furthermore, we provide evidence that human augmin plays critical and non-redundant roles in the kinetochore-MT attachment and also central spindle formation during anaphase in human cells.The HAUS complex is required for mitotic spindle assembly and for maintenance of centrosome integrity.


Pssm-ID: 259069  Cd Length: 253  Bit Score: 39.27  E-value: 2.35e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7662234    602 DRLSHErhqFQRDKEATQELIEDLRKQLEHLQLLKLEAEQRRGRSSSMG-LQEYHSRARESELEQEVRRLKQDNRNLKEQ 680
Cdd:pfam14932  53 DTISAE---SSGLLDQTEEDIEALEDELEALAEAEELYIQLRNKLQQTDsLLSQELSELEGKLERAAAVLQAEEQLLLAM 129
                          90       100
                  ....*....|....*....|....*..
gi 7662234    681 NEELNGQIitLSIQGAKSLFSTAFSES 707
Cdd:pfam14932 130 LQKRNLEL--QELQGEVAKLSQELQHY 154
GimC COG1382
Prefoldin, chaperonin cofactor [Posttranslational modification, protein turnover, chaperones]
540-677 2.91e-03

Prefoldin, chaperonin cofactor [Posttranslational modification, protein turnover, chaperones]


Pssm-ID: 224300  Cd Length: 119  Bit Score: 36.90  E-value: 2.91e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7662234  540 EIENLQTRLQQLDEENSELRSctpcLKANIERLEEEKQKLLDEIEsltlRLSEEQENKRRMGDRLsherhqFQRDKEatq 619
Cdd:COG1382   7 EVQAQLAQLQQLQQQLQKVIL----QKQQLEAQLKEIEKALEELE----KLDEDAPVYKKVGNLL------VKVSKE--- 69
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 7662234  620 ELIEDLRKQLEHLQlLKLEAEQRrgrsssmglQEYHSRARESELEQEVRRLKQDNRNL 677
Cdd:COG1382  70 EAVDELEERKETLE-LRIKTLEK---------QEEKLQERLEELQSEIQKALGDAANG 117
conserved_hypothetical_protein TIGR02473
flagellar export protein FliJ; Members of this family are the FliJ protein found, in nearly ...
517-643 5.60e-03

flagellar export protein FliJ; Members of this family are the FliJ protein found, in nearly every case, in the midst of other flagellar biosynthesis genes in bacgterial genomes. Typically the fliJ gene is found adjacent to the gene for the flagellum-specific ATPase FliI. Sequence scoring in the gray zone between trusted and noise cutoffs include both probable FliJ proteins and components of bacterial type III secretion systems.


Pssm-ID: 131526  Cd Length: 141  Bit Score: 36.52  E-value: 5.60e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7662234    517 EMVLEETRRQKELLcKMEREKSI-EIENLQTRLQQLDEE--------NSELRSCTPCLK-----ANIERLEEEKQKLLDE 582
Cdd:TIGR02473   5 QKLLDLREKEEEQA-KLELAKAQaEFERLETQLQQLIKYreeyeqqaLEKVGAGTSALElsnyqRFIRQLDQRIQQQQQE 83
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 7662234    583 IEsltlRLSEEQENKRrmgDRLSHERhqfqRDKEATQELIEdlrKQLEHLQLLKLEAEQRR 643
Cdd:TIGR02473  84 LA----LLQQEVEAKR---ERLLEAR----RELKALEKLKE---KKQKEYRAEEAKREQKE 130
RhoGEF cd00160
Guanine nucleotide exchange factor for Rho/Rac/Cdc42-like GTPases; Also called Dbl-homologous ...
568-654 6.20e-03

Guanine nucleotide exchange factor for Rho/Rac/Cdc42-like GTPases; Also called Dbl-homologous (DH) domain. It appears that PH domains invariably occur C-terminal to RhoGEF/DH domains.


Pssm-ID: 238091  Cd Length: 181  Bit Score: 37.28  E-value: 6.20e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7662234  568 NIERLEEEKQKLLDEIESltlRLSEEQENKRRMGDRLSHERHQFQ------RDKEATQELIEDLRKQLEHLQLLKLEAEQ 641
Cdd:cd00160  48 NIEEIYEFHRIFLKSLEE---RVEEWDKSGPRIGDVFLKLAPFFKiyseycSNHPDALELLKKLKKFNKFFQEFLEKAES 124
                        90
                ....*....|...
gi 7662234  642 RRGRsssMGLQEY 654
Cdd:cd00160 125 ECGR---LKLESL 134
EF-hand_6 pfam13405
EF-hand domain;
206-235 7.46e-03

EF-hand domain;


Pssm-ID: 257730  Cd Length: 30  Bit Score: 35.26  E-value: 7.46e-03
                          10        20        30
                  ....*....|....*....|....*....|
gi 7662234    206 RLRAVFDALDGDGDGFVRIEDFIQFATVYG 235
Cdd:pfam13405   1 ELREAFKLFDKDGDGYISLEELKKALRSLG 30
PspA COG1842
Phage shock protein A (IM30), suppresses sigma54-dependent transcription [Transcription / ...
459-674 3.68e-07

Phage shock protein A (IM30), suppresses sigma54-dependent transcription [Transcription / Signal transduction mechanisms]


Pssm-ID: 224755 [Multi-domain]  Cd Length: 225  Bit Score: 50.39  E-value: 3.68e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7662234  459 EEDIADKVVFLERRVLELEkdtaatgEQHSRLRQENLQLVHRANALEEQLKEQELRACEMvleETRRQKELLCKME---R 535
Cdd:COG1842  19 LDKAEDPEKMLEQAIRDME-------SELAKARQALAQAIARQKQLERKLEEAQARAEKL---EEKAELALQAGNEdlaR 88
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7662234  536 EKSIEIENLQTRLQQLDEENSELRSCTPCLKANIERLEEEKQKLLDEIESLTLRLSEE--QENKRRMGDRLSHER--HQF 611
Cdd:COG1842  89 EALEEKQSLEDLAKALEAELQQAEEQVEKLKKQLAALEQKIAELRAKKEALKARKAAAkaQEKVNRSLGGGSSSSamAAF 168
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 7662234  612 QR--DKEATQELIEDLRKQLEHLQLLKLEAEQRrgrsssmglQEYHSRARESELEQEVRRLKQDN 674
Cdd:COG1842 169 ERmeEKIEEREARAEAAAELAEGSGDDLDKEFA---------QAGAQSAVDSRLAALKARMKGPA 224
EF-hand_7 pfam13499
EF-hand domain pair;
212-263 5.51e-06

EF-hand domain pair;


Pssm-ID: 257819 [Multi-domain]  Cd Length: 60  Bit Score: 44.68  E-value: 5.51e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 7662234    212 DALDGDGDGFVRIEDFIQFATVYGA--------EQVKDLTKYLDPSGLGVISFEDFYQGI 263
Cdd:pfam13499   1 KLLDKDGDGYIDVEELRKLLKALGLkltdeeveELLEYDFNEFDKDGDGRISFEEFLEAY 60
Chromosome_partition_protein_Smc TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
470-742 2.99e-15

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: 78.56  E-value: 2.99e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7662234     470 ERRVLELEKDTAATGEQHSRLRQENLQLVHRANALEEQL---------KEQELRACEMVLEETRRQKELLCKMEREKSIE 540
Cdd:TIGR02168  676 RREIEELEEKIEELEEKIAELEKALAELRKELEELEEELeqlrkeleeLSRQISALRKDLARLEAEVEQLEERIAQLSKE 755
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7662234     541 IENLQTRLQQLDEENSELRSCTPCLKANIERLEEEKQKLLDEIESLTLRLSEEQENKRRMGDR---LSHERHQFQRDKEA 617
Cdd:TIGR02168  756 LTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEaanLRERLESLERRIAA 835
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7662234     618 TQELIEDLRKQLEHL--QLLKLEAEQRRGRSS--------------SMGLQEYHSRARE--SELEQEVRRLKQDNRNLKE 679
Cdd:TIGR02168  836 TERRLEDLEEQIEELseDIESLAAEIEELEELieeleseleallneRASLEEALALLRSelEELSEELRELESKRSELRR 915
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 7662234     680 QNEELNGQI--ITLSIQGAKSLFstafsESLAAEISSVSRDELMEAIQKQEEINFRLQDYIDRII 742
Cdd:TIGR02168  916 ELEELREKLaqLELRLEGLEVRI-----DNLQERLSEEYSLTLEEAEALENKIEDDEEEARRRLK 975
PRK03918 PRK03918
chromosome segregation protein; Provisional
459-697 4.69e-11

chromosome segregation protein; Provisional


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 65.09  E-value: 4.69e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7662234   459 EEDIADKVVFLERRVLELEKdtaaTGEQHSRLRQENLQLVHRANALEEQLKEQELRacemvLEETRRQKELLCKMEREkS 538
Cdd:PRK03918 216 LPELREELEKLEKEVKELEE----LKEEIEELEKELESLEGSKRKLEEKIRELEER-----IEELKKEIEELEEKVKE-L 285
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7662234   539 IEIENLQTRLQQLDEENSELRSCTPCLKANIERLEEEK---QKLLDEIESLTLRLSEEQENKRRMGDRLS--HERHQFQR 613
Cdd:PRK03918 286 KELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEIngiEERIKELEEKEERLEELKKKLKELEKRLEelEERHELYE 365
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7662234   614 DKEATQELIEDLRKQLEHLQLLKLEAEQrrgrsssmglqEYHSRAREsELEQEVRRLKQDNRNLKEQNEELNGQIITLsi 693
Cdd:PRK03918 366 EAKAKKEELERLKKRLTGLTPEKLEKEL-----------EELEKAKE-EIEEEISKITARIGELKKEIKELKKAIEEL-- 431

                 ....
gi 7662234   694 QGAK 697
Cdd:PRK03918 432 KKAK 435
SCP-1 pfam05483
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ...
453-747 6.99e-10

Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.


Pssm-ID: 114219 [Multi-domain]  Cd Length: 787  Bit Score: 61.28  E-value: 6.99e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7662234    453 ELMEGPEEDIADKVVFLERRV--LELEKDTAATGEQH---------SRLRQE---NLQLVHRANALEEQLKEQELRACEM 518
Cdd:pfam05483 432 EELKGKEQELIFLLQAREKEIhdLEIQLTAIKTSEEHylkevedlkTELEKEklkNIELTAHCDKLLLENKELTQEASDM 511
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7662234    519 VLEETRRQKELL-CKMEREKSI-EIENLQTRLQQLDEEnselrsctpclkanIERLEEEKQKLLDEIESltlRLSEEQEN 596
Cdd:pfam05483 512 TLELKKHQEDIInCKKQEERMLkQIENLEEKEMNLRDE--------------LESVREEFIQKGDEVKC---KLDKSEEN 574
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7662234    597 KRRMGDRLSHERHQFQRDKEATQEL---IEDLRKQLEHLQlLKLEAEQRRGRSSSMGLQEYHSRARESELEQEvrrlkqd 673
Cdd:pfam05483 575 ARSIEYEVLKKEKQMKILENKCNNLkkqIENKNKNIEELH-QENKALKKKGSAENKQLNAYEIKVNKLELELA------- 646
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 7662234    674 nrNLKEQNEElngqiITLSIQgaKSLFSTAFSESLAAEISSVSRDELMEAIQKQEEINFRLQDYIDRiIVAIME 747
Cdd:pfam05483 647 --SAKQKFEE-----IIDNYQ--KEIEDKKISEEKLLEEVEKAKAIADEAVKLQKEIDKRCQHKIAE-MVALME 710
PTZ00121 PTZ00121
MAEBL; Provisional
453-754 9.50e-07

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 51.30  E-value: 9.50e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7662234    453 ELMEGPEEDIADKVvfleRRVLELEKDTAATGEQHSRLRQENLQLVHRANALEEQLKEQELRACEMVLEETRRQKELLCK 532
Cdd:PTZ00121 1538 EAKKAEEKKKADEL----KKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAK 1613
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7662234    533 MEREKSIEIENLQtrlqqldeENSELRSCTPCLKanieRLEEEKQKLLDEIESltlrlsEEQENKRRMGDRLSHERHQFQ 612
Cdd:PTZ00121 1614 KAEEAKIKAEELK--------KAEEEKKKVEQLK----KKEAEEKKKAEELKK------AEEENKIKAAEEAKKAEEDKK 1675
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7662234    613 RDKEATQELiEDLRKQLEhlQLLKLEAEQRRGRSSSMGLQEYHSRARESELEQEVRRLKQDNRNLKEQNEELNGQIITLS 692
Cdd:PTZ00121 1676 KAEEAKKAE-EDEKKAAE--ALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKD 1752
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 7662234    693 IQGAKSLFSTAFSESLAAEISSVSRDELMEAIQKQEEINFRLQdyIDRIIVAIMETNPSILE 754
Cdd:PTZ00121 1753 EEEKKKIAHLKKEEEKKAEEIRKEKEAVIEEELDEEDEKRRME--VDKKIKDIFDNFANIIE 1812
Spc7 smart00787
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ...
493-636 4.89e-06

Spc7 kinetochore protein; This domain is found in cell division proteins which are required for kinetochore-spindle association.


Pssm-ID: 197874 [Multi-domain]  Cd Length: 312  Bit Score: 47.70  E-value: 4.89e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7662234     493 ENLQLVHRANAL----EEQLKE--QELRACEMVLEETRRQ-KELLCKMEREKSIEIENLQTRLQQLDEENSELRSctpcl 565
Cdd:smart00787 151 ENLEGLKEDYKLlmkeLELLNSikPKLRDRKDALEEELRQlKQLEDELEDCDPTELDRAKEKLKKLLQEIMIKVK----- 225
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 7662234     566 kaNIERLEEEKQKLLDEIESLTLRLSEEQenkrrmgDRLSHERHQFQRDKEATQELIEDLRKQLEHLQLLK 636
Cdd:smart00787 226 --KLEELEEELQELESKIEDLTNKKSELN-------TEIAEAEKKLEQCRGFTFKEIEKLKEQLKLLQSLT 287
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
3-223 6.62e-06

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 48.06  E-value: 6.62e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7662234     3 SAPPASPPGSEPPGPDPEPGGPDGPGAAQLAPGPAELRLGAPVGGPDPQSPGLDEPAPGAAADGGARWSAGPAPGLEGGP 82
Cdd:PRK07764 591 APGAAGGEGPPAPASSGPPEEAARPAAPAAPAAPAAPAPAGAAAAPAEASAAPAPGVAAPEHHPKHVAVPDASDGGDGWP 670
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7662234    83 RDPGPSAPPPRSGPRGQLASPDAPGPGPRSEAPLPeldplfSWTEEPEecgPASCPESAPfRLQGSSSSHRARGEVDVFS 162
Cdd:PRK07764 671 AKAGGAAPAAPPPAPAPAAPAAPAGAAPAQPAPAP------AATPPAG---QADDPAAQP-PQAAQGASAPSPAADDPVP 740
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 7662234   163 PFPAPTAGELALEQGPGSPPQPSDLSQTHPLPSEPVGSQEDGPRLRAvfDALDGDGDGFVR 223
Cdd:PRK07764 741 LPPEPDDPPDPAGAPAQPPPPPAPAPAAAPAAAPPPSPPSEEEEMAE--DDAPSMDDEDRR 799
PHA02682 PHA02682
ORF080 virion core protein; Provisional
82-243 9.84e-05

ORF080 virion core protein; Provisional


Pssm-ID: 177464 [Multi-domain]  Cd Length: 280  Bit Score: 43.70  E-value: 9.84e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7662234    82 PRDPGPSAPPPRsgPRGQLASPDAPGPGPRSEAPLPELDPLFSWTEEPeecgPASCPESAPFRLQGSSSSHRARGEVDVF 161
Cdd:PHA02682  81 PLAPSPACAAPA--PACPACAPAAPAPAVTCPAPAPACPPATAPTCPP----PAVCPAPARPAPACPPSTRQCPPAPPLP 154
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7662234   162 SPFPAPTAGELALEQGPGSPPQPSDLSQThpLPSEPVGSQEDGPRLRAvfDALDGDGDGfvriEDFIQFATVYGAEQVKD 241
Cdd:PHA02682 155 TPKPAPAAKPIFLHNQLPPPDYPAASCPT--IETAPAASPVLEPRIPD--KIIDADNDD----KDLIKKELADIADSVRD 226

                 ..
gi 7662234   242 LT 243
Cdd:PHA02682 227 LN 228
FRQ1 COG5126
Ca2+-binding protein (EF-Hand superfamily) [Signal transduction mechanisms / Cytoskeleton / ...
206-263 7.26e-04

Ca2+-binding protein (EF-Hand superfamily) [Signal transduction mechanisms / Cytoskeleton / Cell division and chromosome partitioning / General function prediction only]


Pssm-ID: 227455 [Multi-domain]  Cd Length: 160  Bit Score: 39.60  E-value: 7.26e-04
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 7662234  206 RLRAVFDALDGDGDGFVRIEDFIQFATVYG----AEQVKDLTKYLDPSGLGVISFEDFYQGI 263
Cdd:COG5126  93 ELREAFKLFDKDHDGYISIGELRRVLKSLGerlsDEEVEKLLKEYDEDGDGEIDYEEFKKLI 154
PLN02939 PLN02939
transferase, transferring glycosyl groups
489-699 9.07e-04

transferase, transferring glycosyl groups


Pssm-ID: 215507 [Multi-domain]  Cd Length: 977  Bit Score: 41.43  E-value: 9.07e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7662234   489 RLRQENLQLVHRANAL--EEQLKEQELRACEMVLEETRRQKELLCKMEREKSIEIENLQTRLQQLDEENSELRSCTPCLK 566
Cdd:PLN02939 146 LLNQARLQALEDLEKIltEKEALQGKINILEMRLSETDARIKLAAQEKIHVEILEEQLEKLRNELLIRGATEGLCVHSLS 225
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7662234   567 ANIERLEEEKQKLLDEIESLTLRLSEEQENKRRMGdRLSHERHQFQ---RDKEAT----QE--------LIEDLRKQLEH 631
Cdd:PLN02939 226 KELDVLKEENMLLKDDIQFLKAELIEVAETEERVF-KLEKERSLLDaslRELESKfivaQEdvsklsplQYDCWWEKVEN 304
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 7662234   632 LQLLkLEAEQRRGRSSSMGLQEYHsraresELEQEVRRLKQdnrNLKEQN-EELNGQIITLSIQGAKSL 699
Cdd:PLN02939 305 LQDL-LDRATNQVEKAALVLDQNQ------DLRDKVDKLEA---SLKEANvSKFSSYKVELLQQKLKLL 363
Pro-rich pfam15240
Proline-rich; This family includes several eukaryotic proline-rich proteins.
34-186 4.92e-03

Proline-rich; This family includes several eukaryotic proline-rich proteins.


Pssm-ID: 259374 [Multi-domain]  Cd Length: 170  Bit Score: 37.24  E-value: 4.92e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7662234     34 PGPAELRLGAPVGGPDPQSPGLDEpapgaaadggarwsagPAPGLEGGPRDPGPSAPPPRSGPRGQlasPDAPGPGPRSE 113
Cdd:pfam15240  40 QQGGNQSQGPPQGGFQSQPPAGDE----------------DVNRPEGPPPQGGPQQRPPQGGNQQQ---PPPPQGGQRPP 100
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 7662234    114 APLPELDPLFSWTEEPEECGPASCPESAPF-RLQGSSSSHRARGEvdvfspfPAPTAGElalEQGPGSPPQPSD 186
Cdd:pfam15240 101 GPGKPQGPPPQGGNQQQGPPPPGKPQGPPPqGGPGPPQPGNQQGP-------PPPPPGN---PQGPPRPPQPGN 164
 
Name Accession Description Interval E-value
RBD-FIP pfam09457
FIP domain; The FIP domain is the Rab11-binding domain (RBD) at the C-terminus of a family of ...
716-756 1.12e-11

FIP domain; The FIP domain is the Rab11-binding domain (RBD) at the C-terminus of a family of Rab11-interacting proteins (FIPs). The Rab proteins constitute the largest family of small GTPases (>60 members in mammals). Among them Rab11 is a well characterized regulator of endocytic and recycling pathways. Rab11 associates with a broad range of post-Golgi organelles, including recycling endosomes.


Pssm-ID: 255374  Cd Length: 48  Bit Score: 61.22  E-value: 1.12e-11
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 7662234    716 SRDELMEAIQKQEEINFR-------LQDYIDRIIVAIMETNPSILEVK 756
Cdd:pfam09457   1 SRDELIQELLKQEEENRRkdqhvreLEDYIDNLLVRIMEHTPSILEVP 48
EFh cd00051
EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal ...
206-264 5.34e-05

EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal modulators; most examples in this alignment model have 2 active canonical EF hands. Ca2+ binding induces a conformational change in the EF-hand motif, leading to the activation or inactivation of target proteins. EF-hands tend to occur in pairs or higher copy numbers.


Pssm-ID: 238008 [Multi-domain]  Cd Length: 63  Bit Score: 41.76  E-value: 5.34e-05
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 7662234  206 RLRAVFDALDGDGDGFVRIEDFIQFATVYGAEQVKDLTKYL----DPSGLGVISFEDFYQGIT 264
Cdd:cd00051   1 ELREAFRLFDKDGDGTISADELKAALKSLGEGLSEEEIDEMirevDKDGDGKIDFEEFLELMA 63
Jnk-SapK_ap_N pfam09744
JNK_SAPK-associated protein-1; This is the N-terminal 200 residues of a set of proteins ...
493-592 4.33e-04

JNK_SAPK-associated protein-1; This is the N-terminal 200 residues of a set of proteins conserved from yeasts to humans. Most of the proteins in this entry have an RhoGEF pfam00621 domain at their C-terminal end.


Pssm-ID: 255525  Cd Length: 158  Bit Score: 40.16  E-value: 4.33e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7662234    493 ENLQLVHRANAlEEQLKEQELRACEMVLE-ETRRQKELLcKMEREKSIEIEN--------LQTRLQQLDEENSELRSCTP 563
Cdd:pfam09744  36 ENLDSLVSENQ-NLEVELLLLREDNEQLStQYEREKELR-KQAEEKLIELEDvlegekkeLQNKIEQLEENVRQLELKAK 113
                          90       100
                  ....*....|....*....|....*....
gi 7662234    564 CLKANIERLEEEKQKLLDEIESLTLRLSE 592
Cdd:pfam09744 114 NLADQISRLEERETELKKEYNALHERYTE 142
BCAS2 pfam05700
Breast carcinoma amplified sequence 2 (BCAS2); This family consists of several eukaryotic ...
479-583 6.31e-04

Breast carcinoma amplified sequence 2 (BCAS2); This family consists of several eukaryotic sequences of unknown function. The mammalian members of this family are annotated as breast carcinoma amplified sequence 2 (BCAS2) proteins. BCAS2 is a putative spliceosome associated protein.


Pssm-ID: 253334  Cd Length: 221  Bit Score: 40.52  E-value: 6.31e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7662234    479 DTAATGEQHSRLRQENLQLV--HRANA-------LEEQLK--EQELRACEMVLEETRRQKellcKMEREKS-IEIENLQT 546
Cdd:pfam05700 107 NNARAQLEHQLIRIINLELLskYGKNAwlvyneqLEALLKrlEKELAELKEEIEEVNRQR----KYSQEEAgEKLRSLEQ 182
                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 7662234    547 RLQQLDEENSELRSCTPCLKANIERLEEEKQKLLDEI 583
Cdd:pfam05700 183 RWVDLVSKNLEIEVACAELEQEIEQLKRKKAELKWKE 219
HALZ pfam02183
Homeobox associated leucine zipper;
550-593 9.27e-04

Homeobox associated leucine zipper;


Pssm-ID: 202143  Cd Length: 45  Bit Score: 37.87  E-value: 9.27e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 7662234    550 QLDEENSELRSCTPCLKANIERLEEEKQKLLDEIESLTLRLSEE 593
Cdd:pfam02183   2 QLERDYEVLKRCYDALKAENDSLQKENEKLRAEVLSLKEKLQEK 45
bZIP_plant_BZIP46 cd14707
Basic leucine zipper (bZIP) domain of uncharaterized Plant BZIP transcription factors: a ...
656-684 1.75e-03

Basic leucine zipper (bZIP) domain of uncharaterized Plant BZIP transcription factors: a DNA-binding and dimerization domain; This subfamily is composed of uncharacterized plant bZIP transciption factors with similarity to Glycine max BZIP46, which may be a drought-responsive gene. Plant bZIPs are involved in developmental and physiological processes in response to stimuli/stresses such as light, hormones, and temperature changes. bZIP factors act in networks of homo and heterodimers in the regulation of a diverse set of cellular processes. The bZIP structural motif contains a basic region and a leucine zipper, composed of alpha helices with leucine residues 7 amino acids apart, which stabilize dimerization with a parallel leucine zipper domain. Dimerization of leucine zippers creates a pair of the adjacent basic regions that bind DNA and undergo conformational change. Dimerization occurs in a specific and predictable manner resulting in hundreds of dimers having unique effects on transcription.


Pssm-ID: 269855  Cd Length: 55  Bit Score: 37.29  E-value: 1.75e-03
                        10        20        30
                ....*....|....*....|....*....|...
gi 7662234  656 SRAR----ESELEQEVRRLKQDNRNLKEQNEEL 684
Cdd:cd14707  16 SRARkqayTNELELEVAHLKEENARLKRQQEEL 48
CDC37_N pfam03234
Cdc37 N terminal kinase binding; Cdc37 is a molecular chaperone required for the activity of ...
491-600 1.75e-03

Cdc37 N terminal kinase binding; Cdc37 is a molecular chaperone required for the activity of numerous eukaryotic protein kinases. This domain corresponds to the N terminal domain which binds predominantly to protein kinases and is found N terminal to the Hsp (Heat shocked protein) 90-binding domain pfam08565. Expression of a construct consisting of only the N-terminal domain of Saccharomyces pombe Cdc37 results in cellular viability. This indicates that interactions with the cochaperone Hsp90 may not be essential for Cdc37 function.


Pssm-ID: 251818  Cd Length: 172  Bit Score: 38.62  E-value: 1.75e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7662234    491 RQENLQLVHRANALEEQLKEQELRACEMVLEETRRQKELLCKMEREKSIEIENLQTRLQQLDEENSELRSctpclKANIE 570
Cdd:pfam03234  55 RIMNDRLLERVDKLLSELKEESLDSSQAVMKSLNENFTDKENVEPEQPTYNEMVEDLFDQVKDEVDEKNG-----AALIE 129
                          90       100       110
                  ....*....|....*....|....*....|
gi 7662234    571 RLEEEKQKLLDEIESLTLRLSEEQENKRRM 600
Cdd:pfam03234 130 ELQKHRDKLKKEQKELLKKLDELEKEEKKK 159
HAUS-augmin3 pfam14932
HAUS augmin-like complex subunit 3; This domain is subunit three of the augmin complex found ...
602-707 2.35e-03

HAUS augmin-like complex subunit 3; This domain is subunit three of the augmin complex found from Drosophila to humans. The HAUS-augmin complex is made up of eight subunits. The augmin complex interacts with gamma-TuRC, and attenuation of this interaction severely impairs spindle MT generation. Furthermore, we provide evidence that human augmin plays critical and non-redundant roles in the kinetochore-MT attachment and also central spindle formation during anaphase in human cells.The HAUS complex is required for mitotic spindle assembly and for maintenance of centrosome integrity.


Pssm-ID: 259069  Cd Length: 253  Bit Score: 39.27  E-value: 2.35e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7662234    602 DRLSHErhqFQRDKEATQELIEDLRKQLEHLQLLKLEAEQRRGRSSSMG-LQEYHSRARESELEQEVRRLKQDNRNLKEQ 680
Cdd:pfam14932  53 DTISAE---SSGLLDQTEEDIEALEDELEALAEAEELYIQLRNKLQQTDsLLSQELSELEGKLERAAAVLQAEEQLLLAM 129
                          90       100
                  ....*....|....*....|....*..
gi 7662234    681 NEELNGQIitLSIQGAKSLFSTAFSES 707
Cdd:pfam14932 130 LQKRNLEL--QELQGEVAKLSQELQHY 154
GimC COG1382
Prefoldin, chaperonin cofactor [Posttranslational modification, protein turnover, chaperones]
540-677 2.91e-03

Prefoldin, chaperonin cofactor [Posttranslational modification, protein turnover, chaperones]


Pssm-ID: 224300  Cd Length: 119  Bit Score: 36.90  E-value: 2.91e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7662234  540 EIENLQTRLQQLDEENSELRSctpcLKANIERLEEEKQKLLDEIEsltlRLSEEQENKRRMGDRLsherhqFQRDKEatq 619
Cdd:COG1382   7 EVQAQLAQLQQLQQQLQKVIL----QKQQLEAQLKEIEKALEELE----KLDEDAPVYKKVGNLL------VKVSKE--- 69
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 7662234  620 ELIEDLRKQLEHLQlLKLEAEQRrgrsssmglQEYHSRARESELEQEVRRLKQDNRNL 677
Cdd:COG1382  70 EAVDELEERKETLE-LRIKTLEK---------QEEKLQERLEELQSEIQKALGDAANG 117
AAA_23 pfam13476
AAA domain;
504-630 3.28e-03

AAA domain;


Pssm-ID: 257800  Cd Length: 203  Bit Score: 38.29  E-value: 3.28e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7662234    504 LEEQLKEQELRACEMVLEETRRQKELLCKMEREKsIEIENLQTRLQQLDEENSELRSCTPCLKANIERLEEEKQKLLDEI 583
Cdd:pfam13476  80 FENNKGRLKLRLIEESRKLTKKKGKKVKKSILEI-VEIDELEEFIDELLKSDKEILPLLLYLGQEREEKKFKRKEKKERL 158
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 7662234    584 ESLTLRLSEEQENKRRMGDRLshERHQFQRDKEATQELIEDLRKQLE 630
Cdd:pfam13476 159 EELEKELEELEDEKDLLEKLL--EEKEKKKELEELKEELEELLEELE 203
bZIP cd14686
Basic leucine zipper (bZIP) domain of bZIP transcription factors: a DNA-binding and ...
657-688 3.83e-03

Basic leucine zipper (bZIP) domain of bZIP transcription factors: a DNA-binding and dimerization domain; Basic leucine zipper (bZIP) factors comprise one of the most important classes of enhancer-type transcription factors. They act in networks of homo and heterodimers in the regulation of a diverse set of cellular processes including cell survival, learning and memory, lipid metabolism, and cancer progression, among others. They also play important roles in responses to stimuli or stress signals such as cytokines, genotoxic agents, or physiological stresses. The bZIP structural motif contains a basic region and a leucine zipper, composed of alpha helices with leucine residues 7 amino acids apart, which stabilize dimerization with a parallel leucine zipper domain. Dimerization of leucine zippers creates a pair of the adjacent basic regions that bind DNA and undergo conformational change. Dimerization occurs in a specific and predictable manner resulting in hundreds of dimers having unique effects on transcription.


Pssm-ID: 269834  Cd Length: 52  Bit Score: 36.37  E-value: 3.83e-03
                        10        20        30
                ....*....|....*....|....*....|..
gi 7662234  657 RARESELEQEVRRLKQDNRNLKEQNEELNGQI 688
Cdd:cd14686  20 KERIEELEEEVEELEEENEELKAELEELRAEV 51
Tropomyosin_1 pfam12718
Tropomyosin like; This family is a set of eukaryotic tropomyosins. Within the yeast Tmp1 and ...
490-596 3.89e-03

Tropomyosin like; This family is a set of eukaryotic tropomyosins. Within the yeast Tmp1 and Tmp2, biochemical and sequence analyses indicate that Tpm2p spans four actin monomers along a filament, whereas Tpmlp spans five. Despite its shorter length, Tpm2p can compete with Tpm1p for binding to F-actin. Over-expression of Tpm2p in vivo alters the axial budding of haploids to a bipolar pattern, and this can be partially suppressed by co-over-expression of Tpm1p. This suggests distinct functions for the two tropomyosins, and indicates that the ratio between them is important for correct morphogenesis. The family also contains higher eukaryote Tmp3 members.


Pssm-ID: 257245  Cd Length: 143  Bit Score: 37.19  E-value: 3.89e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7662234    490 LRQENLQLVHRANALEEQLKEqelracemvLEETRRQKELlckmereksiEIENLQTRLQQLDEENSELRSCTPCLKAni 569
Cdd:pfam12718   5 LKLEAENAQERAEELEEKLKE---------LEQENLEKEQ----------EIKSLQKKNQQLEEEVEKLEEQLKEAKE-- 63
                          90       100       110
                  ....*....|....*....|....*....|
gi 7662234    570 erLEEEKQKLLDEIESLTLR---LSEEQEN 596
Cdd:pfam12718  64 --KLEESEKLATNAEALTRRiqlLEEELEE 91
Sec2p pfam06428
GDP/GTP exchange factor Sec2p; In Saccharomyces cerevisiae, Sec2p is a GDP/GTP exchange factor ...
570-648 4.02e-03

GDP/GTP exchange factor Sec2p; In Saccharomyces cerevisiae, Sec2p is a GDP/GTP exchange factor for Sec4p, which is required for vesicular transport at the post-Golgi stage of yeast secretion.


Pssm-ID: 253724  Cd Length: 101  Bit Score: 36.21  E-value: 4.02e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7662234    570 ERLEEEKQKLLDEIESLTLRLSEEQENkrrMGDRLSHERHQFQRDKEATQE-------LIEDLRKQLEHLQ--LLKLEAE 640
Cdd:pfam06428  11 LRAEKERTKLEQEVEDLTASLFDEANK---MVANARREREAVEIKNEKLEEqlkeketLLDSLQAQLKELKqvLIGLENE 87

                  ....*...
gi 7662234    641 QRRGRSSS 648
Cdd:pfam06428  88 QNPSKTKS 95
conserved_hypothetical_protein TIGR02473
flagellar export protein FliJ; Members of this family are the FliJ protein found, in nearly ...
517-643 5.60e-03

flagellar export protein FliJ; Members of this family are the FliJ protein found, in nearly every case, in the midst of other flagellar biosynthesis genes in bacgterial genomes. Typically the fliJ gene is found adjacent to the gene for the flagellum-specific ATPase FliI. Sequence scoring in the gray zone between trusted and noise cutoffs include both probable FliJ proteins and components of bacterial type III secretion systems.


Pssm-ID: 131526  Cd Length: 141  Bit Score: 36.52  E-value: 5.60e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7662234    517 EMVLEETRRQKELLcKMEREKSI-EIENLQTRLQQLDEE--------NSELRSCTPCLK-----ANIERLEEEKQKLLDE 582
Cdd:TIGR02473   5 QKLLDLREKEEEQA-KLELAKAQaEFERLETQLQQLIKYreeyeqqaLEKVGAGTSALElsnyqRFIRQLDQRIQQQQQE 83
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 7662234    583 IEsltlRLSEEQENKRrmgDRLSHERhqfqRDKEATQELIEdlrKQLEHLQLLKLEAEQRR 643
Cdd:TIGR02473  84 LA----LLQQEVEAKR---ERLLEAR----RELKALEKLKE---KKQKEYRAEEAKREQKE 130
BCAS2 pfam05700
Breast carcinoma amplified sequence 2 (BCAS2); This family consists of several eukaryotic ...
518-687 5.91e-03

Breast carcinoma amplified sequence 2 (BCAS2); This family consists of several eukaryotic sequences of unknown function. The mammalian members of this family are annotated as breast carcinoma amplified sequence 2 (BCAS2) proteins. BCAS2 is a putative spliceosome associated protein.


Pssm-ID: 253334  Cd Length: 221  Bit Score: 37.83  E-value: 5.91e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7662234    518 MVLEETRRQKELLckmereksieieNLQTRLQQLDEENSELRScTPCLKANIERleEEKQKLLDEIESLTLRLSEEQENK 597
Cdd:pfam05700  31 LVEEEMKRYRPTK------------NYLEHLPSLQGPDYSLFE-TPLLRNEFER--VQAGQPMKGLDMSRYELPEPPAGK 95
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7662234    598 RRmgdrlsherhqfqrDKEATQELIEDLRKQLEHLQ--LLKLEAEQRRGRSSSmglqeyhsRARESELEQEVRRLKQDNR 675
Cdd:pfam05700  96 AN--------------DDKAWKAALNNARAQLEHQLirIINLELLSKYGKNAW--------LVYNEQLEALLKRLEKELA 153
                         170
                  ....*....|..
gi 7662234    676 NLKEQNEELNGQ 687
Cdd:pfam05700 154 ELKEEIEEVNRQ 165
RhoGEF cd00160
Guanine nucleotide exchange factor for Rho/Rac/Cdc42-like GTPases; Also called Dbl-homologous ...
568-654 6.20e-03

Guanine nucleotide exchange factor for Rho/Rac/Cdc42-like GTPases; Also called Dbl-homologous (DH) domain. It appears that PH domains invariably occur C-terminal to RhoGEF/DH domains.


Pssm-ID: 238091  Cd Length: 181  Bit Score: 37.28  E-value: 6.20e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7662234  568 NIERLEEEKQKLLDEIESltlRLSEEQENKRRMGDRLSHERHQFQ------RDKEATQELIEDLRKQLEHLQLLKLEAEQ 641
Cdd:cd00160  48 NIEEIYEFHRIFLKSLEE---RVEEWDKSGPRIGDVFLKLAPFFKiyseycSNHPDALELLKKLKKFNKFFQEFLEKAES 124
                        90
                ....*....|...
gi 7662234  642 RRGRsssMGLQEY 654
Cdd:cd00160 125 ECGR---LKLESL 134
TBPIP pfam07106
Tat binding protein 1(TBP-1)-interacting protein (TBPIP); This family consists of several ...
520-633 6.22e-03

Tat binding protein 1(TBP-1)-interacting protein (TBPIP); This family consists of several eukaryotic TBP-1 interacting protein (TBPIP) sequences. TBP-1 has been demonstrated to interact with the human immunodeficiency virus type 1 (HIV-1) viral protein Tat, then modulate the essential replication process of HIV. In addition, TBP-1 has been shown to be a component of the 26S proteasome, a basic multiprotein complex that degrades ubiquitinated proteins in an ATP-dependent fashion. Human TBPIP interacts with human TBP-1 then modulates the inhibitory action of human TBP-1 on HIV-Tat-mediated transactivation.


Pssm-ID: 148614  Cd Length: 169  Bit Score: 36.90  E-value: 6.22e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7662234    520 LEETRRQKELLCKMEREKSIEIENLQ-------TRLQQLDEENSELRSCTPCLKANIERLEEEKQKLLDEIESLTLR--L 590
Cdd:pfam07106  39 LDELVDEGKIICKEYGKQKIYLCNQDqfelpsdEELNKLDMEIEELREEVQLLKQDCSTLEIELKSLTSDLTTEELQeeI 118
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 7662234    591 SEEQENKRRMGDRLsherHQFQRD-KEATQELIEDLRKQLEHLQ 633
Cdd:pfam07106 119 QELKKEVREIEEKL----ESLEEGwKPVTPEEMEKVKKEYKDLH 158
EF-hand_6 pfam13405
EF-hand domain;
206-235 7.46e-03

EF-hand domain;


Pssm-ID: 257730  Cd Length: 30  Bit Score: 35.26  E-value: 7.46e-03
                          10        20        30
                  ....*....|....*....|....*....|
gi 7662234    206 RLRAVFDALDGDGDGFVRIEDFIQFATVYG 235
Cdd:pfam13405   1 ELREAFKLFDKDGDGYISLEELKKALRSLG 30
PspA COG1842
Phage shock protein A (IM30), suppresses sigma54-dependent transcription [Transcription / ...
459-674 3.68e-07

Phage shock protein A (IM30), suppresses sigma54-dependent transcription [Transcription / Signal transduction mechanisms]


Pssm-ID: 224755 [Multi-domain]  Cd Length: 225  Bit Score: 50.39  E-value: 3.68e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7662234  459 EEDIADKVVFLERRVLELEkdtaatgEQHSRLRQENLQLVHRANALEEQLKEQELRACEMvleETRRQKELLCKME---R 535
Cdd:COG1842  19 LDKAEDPEKMLEQAIRDME-------SELAKARQALAQAIARQKQLERKLEEAQARAEKL---EEKAELALQAGNEdlaR 88
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7662234  536 EKSIEIENLQTRLQQLDEENSELRSCTPCLKANIERLEEEKQKLLDEIESLTLRLSEE--QENKRRMGDRLSHER--HQF 611
Cdd:COG1842  89 EALEEKQSLEDLAKALEAELQQAEEQVEKLKKQLAALEQKIAELRAKKEALKARKAAAkaQEKVNRSLGGGSSSSamAAF 168
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 7662234  612 QR--DKEATQELIEDLRKQLEHLQLLKLEAEQRrgrsssmglQEYHSRARESELEQEVRRLKQDN 674
Cdd:COG1842 169 ERmeEKIEEREARAEAAAELAEGSGDDLDKEFA---------QAGAQSAVDSRLAALKARMKGPA 224
EF-hand_7 pfam13499
EF-hand domain pair;
212-263 5.51e-06

EF-hand domain pair;


Pssm-ID: 257819 [Multi-domain]  Cd Length: 60  Bit Score: 44.68  E-value: 5.51e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 7662234    212 DALDGDGDGFVRIEDFIQFATVYGA--------EQVKDLTKYLDPSGLGVISFEDFYQGI 263
Cdd:pfam13499   1 KLLDKDGDGYIDVEELRKLLKALGLkltdeeveELLEYDFNEFDKDGDGRISFEEFLEAY 60
Chromosome_partition_protein_Smc TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
470-742 2.99e-15

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: 78.56  E-value: 2.99e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7662234     470 ERRVLELEKDTAATGEQHSRLRQENLQLVHRANALEEQL---------KEQELRACEMVLEETRRQKELLCKMEREKSIE 540
Cdd:TIGR02168  676 RREIEELEEKIEELEEKIAELEKALAELRKELEELEEELeqlrkeleeLSRQISALRKDLARLEAEVEQLEERIAQLSKE 755
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7662234     541 IENLQTRLQQLDEENSELRSCTPCLKANIERLEEEKQKLLDEIESLTLRLSEEQENKRRMGDR---LSHERHQFQRDKEA 617
Cdd:TIGR02168  756 LTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEaanLRERLESLERRIAA 835
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7662234     618 TQELIEDLRKQLEHL--QLLKLEAEQRRGRSS--------------SMGLQEYHSRARE--SELEQEVRRLKQDNRNLKE 679
Cdd:TIGR02168  836 TERRLEDLEEQIEELseDIESLAAEIEELEELieeleseleallneRASLEEALALLRSelEELSEELRELESKRSELRR 915
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 7662234     680 QNEELNGQI--ITLSIQGAKSLFstafsESLAAEISSVSRDELMEAIQKQEEINFRLQDYIDRII 742
Cdd:TIGR02168  916 ELEELREKLaqLELRLEGLEVRI-----DNLQERLSEEYSLTLEEAEALENKIEDDEEEARRRLK 975
Smc COG1196
Chromosome segregation ATPases [Cell division and chromosome partitioning]
435-754 1.08e-14

Chromosome segregation ATPases [Cell division and chromosome partitioning]


Pssm-ID: 224117 [Multi-domain]  Cd Length: 1163  Bit Score: 77.06  E-value: 1.08e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7662234   435 YLHQSGALTMEALEDPSPELMEGPEEDIADKVVFLERRVLELEKDTAATGEQHSRLRQ--ENLQLVHRANALEEQLKEQE 512
Cdd:COG1196  645 LVEPSGSITGGSRNKRSSLAQKRELKELEEELAELEAQLEKLEEELKSLKNELRSLEDllEELRRQLEELERQLEELKRE 724
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7662234   513 LRACEMVLEETRRQKELLCKMEREKSIEIENLQTRLQQLDEENSELRSCTPCLKANIERLEEEKQKLLDEIESLTLRLSE 592
Cdd:COG1196  725 LAALEEELEQLQSRLEELEEELEELEEELEELQERLEELEEELESLEEALAKLKEEIEELEEKRQALQEELEELEEELEE 804
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7662234   593 EQENKRRMGDRLSHERHQFQRDKEATQELIEDLRKQLEHLQLLKLEAEQRRGRSSSMGLQEYHSRARESELEQEVRRLKQ 672
Cdd:COG1196  805 AERRLDALERELESLEQRRERLEQEIEELEEEIEELEEKLDELEEELEELEKELEELKEELEELEAEKEELEDELKELEE 884
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7662234   673 DNRNLKEQNEELNGQI--ITLSIQGAKSLFSTAFSESLAAEISSVSRDELMEAIQKQEEINF--RLQDYIDRIIVAIMET 748
Cdd:COG1196  885 EKEELEEELRELESELaeLKEEIEKLRERLEELEAKLERLEVELPELEEELEEEYEDTLETEleREIERLEEEIEALGPV 964

                 ....*.
gi 7662234   749 NPSILE 754
Cdd:COG1196  965 NLRAIE 970
chromosome_segregation_protein_related_ptotein TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
455-737 8.94e-14

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: 73.95  E-value: 8.94e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7662234     455 MEGPEEDIADKVVFLERRVLELEKDTAATGEQHSRLRQENLQLVHRANALEEQLKEQE--LRACEMVLEETRRQKELLCK 532
Cdd:TIGR02169  686 LKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEedLSSLEQEIENVKSELKELEA 765
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7662234     533 MEREKSIEIENLQTRLQQLdeENSELRSCTPCLKANIERLEEEKQKL---LDEIESLTLRLSEEQEnkrrmgdRLSHERH 609
Cdd:TIGR02169  766 RIEELEEDLHKLEEALNDL--EARLSHSRIPEIQAELSKLEEEVSRIearLREIEQKLNRLTLEKE-------YLEKEIQ 836
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7662234     610 QFQRDKEATQELIEDLRKQLEHLQLLKLEAEQRRGRSSsmgLQEYHSRARESELEQEVRRLKQDNRNLKEQNEELNGQII 689
Cdd:TIGR02169  837 ELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELE---AALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIE 913
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 7662234     690 TLSIQGA--KSLFSTAFS-----ESLAAEISSVS------------RDELMEAIQKQEEINFR-LQDY 737
Cdd:TIGR02169  914 KKRKRLSelKAKLEALEEelseiEDPKGEDEEIPeeelsledvqaeLQRVEEEIRALEPVNMLaIQEY 981
Smc COG1196
Chromosome segregation ATPases [Cell division and chromosome partitioning]
459-692 9.39e-13

Chromosome segregation ATPases [Cell division and chromosome partitioning]


Pssm-ID: 224117 [Multi-domain]  Cd Length: 1163  Bit Score: 70.51  E-value: 9.39e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7662234   459 EEDIADKVVFLERRVLELEKDTAATGEQHSRLRQENLQLVHRANALEEQLK--EQELRACEMVLEETRRQKELLCKM--- 533
Cdd:COG1196  283 LEELQEELLELKEEIEELEGEISLLRERLEELENELEELEERLEELKEKIEalKEELEERETLLEELEQLLAELEEAkee 362
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7662234   534 -EREKSIEIENLQTRLQQLDEENSELRsctpclkANIERLEEEKQKLLDEIESLtlrlSEEQENKRRMGDRLSHERHQFQ 612
Cdd:COG1196  363 lEEKLSALLEELEELFEALREELAELE-------AELAEIRNELEELKREIESL----EERLERLSERLEDLKEELKELE 431
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7662234   613 RDKEATQELIEDLRKQLEHLQLLKLEAEQRRgrsssmglqeyhsrareSELEQEVRRLKQDNRNLKEQNEELNGQIITLS 692
Cdd:COG1196  432 AELEELQTELEELNEELEELEEQLEELRDRL-----------------KELERELAELQEELQRLEKELSSLEARLDRLE 494
Chromosome_partition_protein_Smc TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
491-740 9.80e-13

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: 70.47  E-value: 9.80e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7662234     491 RQENLQLVHRANA---LEEQLKEQE--LRACEMVLEETRRQKELLCKMEREKSIEIENLQTRLQQLDEENSELRSCTPCL 565
Cdd:TIGR02168  666 AKTNSSILERRREieeLEEKIEELEekIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQL 745
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7662234     566 KANIERLEEEKQKLLDEIESLTLRLSEEQENKRRMGDRLSHERHQFQRDKEATQELIEDLRKQLEHLQLLKLEAEQRRGR 645
Cdd:TIGR02168  746 EERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRER 825
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7662234     646 SSSMglqeyhsRARESELEQEVRRLKQDNRNLKEQNEELNGQIITLSIQGAKS-------LFSTAFSESLAAEISSvSRD 718
Cdd:TIGR02168  826 LESL-------ERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELeselealLNERASLEEALALLRS-ELE 897
                          250       260
                   ....*....|....*....|..
gi 7662234     719 ELMEAIQKQEEINFRLQDYIDR 740
Cdd:TIGR02168  898 ELSEELRELESKRSELRRELEE 919
Smc COG1196
Chromosome segregation ATPases [Cell division and chromosome partitioning]
500-741 1.01e-12

Chromosome segregation ATPases [Cell division and chromosome partitioning]


Pssm-ID: 224117 [Multi-domain]  Cd Length: 1163  Bit Score: 70.51  E-value: 1.01e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7662234   500 RANALEEQLKEQELRACEMVLEETRRQKELLckMEREKSIE--IENLQTRLQQLDEENSELRSCTPCLKANIERLEEEKQ 577
Cdd:COG1196  214 RYQELKAELRELELALLLAKLKELRKELEEL--EEELSRLEeeLEELQEELEEAEKEIEELKSELEELREELEELQEELL 291
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7662234   578 KLLDEIESLTL---RLSEEQENKRRMGDRLSHERHQFQRDKEATQELIEDLRKQLEHLQLLK------LEAEQRRGRSSS 648
Cdd:COG1196  292 ELKEEIEELEGeisLLRERLEELENELEELEERLEELKEKIEALKEELEERETLLEELEQLLaeleeaKEELEEKLSALL 371
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7662234   649 MGLQEYHSRARE----------------SELEQEVRRLKQDNRNLKEQNEELNGQIITLSIQGAKSLFSTafsESLAAEI 712
Cdd:COG1196  372 EELEELFEALREelaeleaelaeirnelEELKREIESLEERLERLSERLEDLKEELKELEAELEELQTEL---EELNEEL 448
                        250       260
                 ....*....|....*....|....*....
gi 7662234   713 SSVSrDELMEAIQKQEEINFRLQDYIDRI 741
Cdd:COG1196  449 EELE-EQLEELRDRLKELERELAELQEEL 476
Chromosome_partition_protein_Smc TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
500-694 1.01e-12

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: 70.47  E-value: 1.01e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7662234     500 RANALEEQLKEQELRACEMVLEETRRQKELLCKMEREKSIEIENLQTRLQQLDEENSELRSCTPCLKANIERLEEEKQKL 579
Cdd:TIGR02168  214 RYKELKAELRELELALLVLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYAL 293
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7662234     580 LDEIESLTLR---LSEEQENKRRMGDRLSHERHQFQRDKEATQELIEDLRKQLEHLQlLKLEAEQRRGRSSSMGLQEYHS 656
Cdd:TIGR02168  294 ANEISRLEQQkqiLRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELK-EELESLEAELEELEAELEELES 372
                          170       180       190
                   ....*....|....*....|....*....|....*...
gi 7662234     657 RAResELEQEVRRLKQDNRNLKEQNEELNGQIITLSIQ 694
Cdd:TIGR02168  373 RLE--ELEEQLETLRSKVAQLELQIASLNNEIERLEAR 408
Chromosome_partition_protein_Smc TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
460-740 3.02e-12

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: 68.93  E-value: 3.02e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7662234     460 EDIADKVVFLERRVLELEKDTAATGEQHSRLRQENLQLVHRANALEEQLKEQELracEMVLEETRRQKELLCKMEREKSI 539
Cdd:TIGR02168  708 EELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEA---EIEELEERLEEAEEELAEAEAEI 784
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7662234     540 E-----IENLQTRLQQLDEENSELRSCTPCLKANIERLEEEKQKLLDEIESLTLRLSEEQENKRRMGDRLSHERHQFqrd 614
Cdd:TIGR02168  785 EeleaqIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEI--- 861
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7662234     615 kEATQELIEDLRKQLEHL----------------QLLKLEAEQRRGRSSSMGLQEYHSRARES---------ELEQEVRR 669
Cdd:TIGR02168  862 -EELEELIEELESELEALlnerasleealallrsELEELSEELRELESKRSELRRELEELREKlaqlelrleGLEVRIDN 940
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 7662234     670 LKQdnrNLKEQneelngQIITLSIQGAKSLFSTAFSESLAAEISSVSR--DEL----MEAIQKQEEINFRLqDYIDR 740
Cdd:TIGR02168  941 LQE---RLSEE------YSLTLEEAEALENKIEDDEEEARRRLKRLENkiKELgpvnLAAIEEYEELKERY-DFLTA 1007
chromosome_segregation_protein_related_ptotein TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
445-685 3.99e-12

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: 68.56  E-value: 3.99e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7662234     445 EALEDPSPELMEGPEEDIADKVVFLERRVLELEKDTAATGEQHSRLRQENLQLVHranalEEQLKEQELRACEMVLEETR 524
Cdd:TIGR02169  779 EALNDLEARLSHSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEK-----EIQELQEQRIDLKEQIKSIE 853
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7662234     525 RQKELLCKMEREKSIEIENLQTRLQQLDEENSELRSCTPCLKANIERLEEEKQKLLDEIESLTLRLSEEQENKRRMGDRL 604
Cdd:TIGR02169  854 KEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEEL 933
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7662234     605 SHERHQFQRDKEATQEL--IEDLRKQLEhlqllKLEAEQRRGRSSSMG-LQEYH-SRARESELEQEVRRLKQDNRNLKEQ 680
Cdd:TIGR02169  934 SEIEDPKGEDEEIPEEElsLEDVQAELQ-----RVEEEIRALEPVNMLaIQEYEeVLKRLDELKEKRAKLEEERKAILER 1008

                   ....*
gi 7662234     681 NEELN 685
Cdd:TIGR02169 1009 IEEYE 1013
Chromosome_partition_protein_Smc TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
469-685 9.98e-12

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: 67.39  E-value: 9.98e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7662234     469 LERRV--LELEKDTAatgEQHSRLRQENLQLVHRANALEEQLKEQELRACEMVLEETRRQKELLCKMEREKSIEIENLQT 546
Cdd:TIGR02168  198 LERQLksLERQAEKA---ERYKELKAELRELELALLVLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRL 274
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7662234     547 RLQQLDEENSELRSCTPCLKANIERLEEEKQKLLDEIESLT---LRLSEEQENKRRMGDRLSHERHQFQRDKEATQELIE 623
Cdd:TIGR02168  275 EVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLErqlEELEAQLEELESKLDELAEELAELEEKLEELKEELE 354
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 7662234     624 DLRKQLEHLQLLKLEAEQR-----------RGRSSSMGLQEYHSRARESELEQEVRRLKQDNRNLKEQNEELN 685
Cdd:TIGR02168  355 SLEAELEELEAELEELESRleeleeqletlRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELL 427
SbcC COG0419
ATPase involved in DNA repair [DNA replication, recombination, and repair]
453-741 3.16e-11

ATPase involved in DNA repair [DNA replication, recombination, and repair]


Pssm-ID: 223496 [Multi-domain]  Cd Length: 908  Bit Score: 65.55  E-value: 3.16e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7662234  453 ELMEGPEEDIADkvvfLERRVLELEKDTAA---TGEQHSRLRQENLQLVHRANALEEQLKEQELRACEMVLEETRRQKEL 529
Cdd:COG0419 147 AFLKSKPKERKE----ILDELFGLEKYEKLselLKEVIKEAKAKIEELEGQLSELLEDIEDLLEALEEELKELKKLEEIQ 222
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7662234  530 LCKMEREKSIEIENLQTRLQQLDEENSELRSCTPCLK----------ANIERLEEEKQKLLDEIESLTLRLSEEQENKRR 599
Cdd:COG0419 223 EEQEEEELEQEIEALEERLAELEEEKERLEELKARLLeieslelealKIREEELRELERLLEELEEKIERLEELEREIEE 302
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7662234  600 ------MGDRLSHERHQFQRDKEATQELIEDLRKQLEHLQLLKLEAEQRRGRSSSMgLQEYHS--RARESELEQEVRRLK 671
Cdd:COG0419 303 leeeleGLRALLEELEELLEKLKSLEERLEKLEEKLEKLESELEELAEEKNELAKL-LEERLKelEERLEELEKELEKAL 381
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7662234  672 QDNRNLKEQNEELNgqiitlsiqgakslfstAFSESLAAEISSVsRDELMEAIQKQEEINFRLQDYIDRI 741
Cdd:COG0419 382 ERLKQLEEAIQELK-----------------EELAELSAALEEI-QEELEELEKELEELERELEELEEEI 433
PRK03918 PRK03918
chromosome segregation protein; Provisional
459-697 4.69e-11

chromosome segregation protein; Provisional


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 65.09  E-value: 4.69e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7662234   459 EEDIADKVVFLERRVLELEKdtaaTGEQHSRLRQENLQLVHRANALEEQLKEQELRacemvLEETRRQKELLCKMEREkS 538
Cdd:PRK03918 216 LPELREELEKLEKEVKELEE----LKEEIEELEKELESLEGSKRKLEEKIRELEER-----IEELKKEIEELEEKVKE-L 285
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7662234   539 IEIENLQTRLQQLDEENSELRSCTPCLKANIERLEEEK---QKLLDEIESLTLRLSEEQENKRRMGDRLS--HERHQFQR 613
Cdd:PRK03918 286 KELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEIngiEERIKELEEKEERLEELKKKLKELEKRLEelEERHELYE 365
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7662234   614 DKEATQELIEDLRKQLEHLQLLKLEAEQrrgrsssmglqEYHSRAREsELEQEVRRLKQDNRNLKEQNEELNGQIITLsi 693
Cdd:PRK03918 366 EAKAKKEELERLKKRLTGLTPEKLEKEL-----------EELEKAKE-EIEEEISKITARIGELKKEIKELKKAIEEL-- 431

                 ....
gi 7662234   694 QGAK 697
Cdd:PRK03918 432 KKAK 435
PRK03918 PRK03918
chromosome segregation protein; Provisional
460-747 6.11e-11

chromosome segregation protein; Provisional


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 64.70  E-value: 6.11e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7662234   460 EDIADKVVfleRRVLELEK-----DTAATGEQHSRLRQENLQ-LVHRANALEEQLKEQELRacemvLEETRRQKELLCKM 533
Cdd:PRK03918 144 DESREKVV---RQILGLDDyenayKNLGEVIKEIKRRIERLEkFIKRTENIEELIKEKEKE-----LEEVLREINEISSE 215
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7662234   534 EREKSIEIENLQTRLQQLD---EENSELRSCTPCLKANIERLEEEKQKLLDEIESLTLRLSEEQENKRRMGD-------- 602
Cdd:PRK03918 216 LPELREELEKLEKEVKELEelkEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKElkekaeey 295
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7662234   603 -RLSHERHQFQRDKEATQELIEDLRKQLEHLQLLKLEAEQRRGRsssmgLQEYhsRARESELEQEVRRLK------QDNR 675
Cdd:PRK03918 296 iKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEER-----LEEL--KKKLKELEKRLEELEerhelyEEAK 368
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 7662234   676 NLKEQNEELNGQIITLSIqgakslfstafsESLAAEISSVSR--DELMEAIQKQEEINFRLQDYIDRIIVAIME 747
Cdd:PRK03918 369 AKKEELERLKKRLTGLTP------------EKLEKELEELEKakEEIEEEISKITARIGELKKEIKELKKAIEE 430
Smc COG1196
Chromosome segregation ATPases [Cell division and chromosome partitioning]
509-735 8.79e-11

Chromosome segregation ATPases [Cell division and chromosome partitioning]


Pssm-ID: 224117 [Multi-domain]  Cd Length: 1163  Bit Score: 64.35  E-value: 8.79e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7662234   509 KEQELRACEMVLEETRRQKELLcKMEREKSIEIENLQTRLQQLDEEnselrsctpCLKANIERLEEEKQKLLDEIESLTL 588
Cdd:COG1196  184 TEENLERLEDLLEELEKQLEKL-ERQAEKAERYQELKAELRELELA---------LLLAKLKELRKELEELEEELSRLEE 253
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7662234   589 RLSEEQENKRRMGDRLSHERHQFqrdkeatQELIEDLRKQLEHLQLLKLEAEQRRGRSSSMGLQEYHSRARESELEQEVR 668
Cdd:COG1196  254 ELEELQEELEEAEKEIEELKSEL-------EELREELEELQEELLELKEEIEELEGEISLLRERLEELENELEELEERLE 326
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 7662234   669 RLKQDNRNLKEQNEELNGQIITLS-----IQGAKSLFSTAFSESLAAEIS--SVSRDELMEAIQKQEEINFRLQ 735
Cdd:COG1196  327 ELKEKIEALKEELEERETLLEELEqllaeLEEAKEELEEKLSALLEELEElfEALREELAELEAELAEIRNELE 400
conserved_hypothetical_protein TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
472-748 4.44e-10

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: 61.57  E-value: 4.44e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7662234    472 RVLELEKDTAAtgEQHSRLRQENLQ-------LVHRANALEEQLK---------EQELRACEMVLEETRRQKELLCKMER 535
Cdd:TIGR04523 415 KKLQQEKELLE--KEIERLKETIIKnnseikdLTNQDSVKELIIKnldntreslETQLKVLSRSINKIKQNLEQKQKELK 492
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7662234    536 EKSIEIENLQTRLQQLDEENSELRSCTPCLKANIERLEEEKQKLLDEIESLTLRLSEEQENKRRmgDRLSHERHQFQRDK 615
Cdd:TIGR04523 493 SKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDELNKDDFELKK--ENLEKEIDEKNKEI 570
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7662234    616 EATQELIEDLRKQLEHLQLL--KLEAEQRRGRSssmGLQEYHSRAreSELEQEVrrlkqdnRNLKEQNEELNGQIITlsI 693
Cdd:TIGR04523 571 EELKQTQKSLKKKQEEKQELidQKEKEKKDLIK---EIEEKEKKI--SSLEKEL-------EKAKKENEKLSSIIKN--I 636
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 7662234    694 QGAKslfstafsESLAAEISSVsRDELMEAIQKQEEINFRLQDYIDRI--IVAIMET 748
Cdd:TIGR04523 637 KSKK--------NKLKQEVKQI-KETIKEIRNKWPEIIKKIKESKTKIddIIELMKD 684
SCP-1 pfam05483
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ...
453-747 6.99e-10

Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.


Pssm-ID: 114219 [Multi-domain]  Cd Length: 787  Bit Score: 61.28  E-value: 6.99e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7662234    453 ELMEGPEEDIADKVVFLERRV--LELEKDTAATGEQH---------SRLRQE---NLQLVHRANALEEQLKEQELRACEM 518
Cdd:pfam05483 432 EELKGKEQELIFLLQAREKEIhdLEIQLTAIKTSEEHylkevedlkTELEKEklkNIELTAHCDKLLLENKELTQEASDM 511
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7662234    519 VLEETRRQKELL-CKMEREKSI-EIENLQTRLQQLDEEnselrsctpclkanIERLEEEKQKLLDEIESltlRLSEEQEN 596
Cdd:pfam05483 512 TLELKKHQEDIInCKKQEERMLkQIENLEEKEMNLRDE--------------LESVREEFIQKGDEVKC---KLDKSEEN 574
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7662234    597 KRRMGDRLSHERHQFQRDKEATQEL---IEDLRKQLEHLQlLKLEAEQRRGRSSSMGLQEYHSRARESELEQEvrrlkqd 673
Cdd:pfam05483 575 ARSIEYEVLKKEKQMKILENKCNNLkkqIENKNKNIEELH-QENKALKKKGSAENKQLNAYEIKVNKLELELA------- 646
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 7662234    674 nrNLKEQNEElngqiITLSIQgaKSLFSTAFSESLAAEISSVSRDELMEAIQKQEEINFRLQDYIDRiIVAIME 747
Cdd:pfam05483 647 --SAKQKFEE-----IIDNYQ--KEIEDKKISEEKLLEEVEKAKAIADEAVKLQKEIDKRCQHKIAE-MVALME 710
SbcC COG0419
ATPase involved in DNA repair [DNA replication, recombination, and repair]
503-756 7.41e-10

ATPase involved in DNA repair [DNA replication, recombination, and repair]


Pssm-ID: 223496 [Multi-domain]  Cd Length: 908  Bit Score: 60.93  E-value: 7.41e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7662234  503 ALEEQLKEQELRAcEMVLEETRRQKELLCKMEREksiEIENLQTRLQQLDEENS-ELRSCTPCLKANIERLEEEKQKL-- 579
Cdd:COG0419 171 KLSELLKEVIKEA-KAKIEELEGQLSELLEDIED---LLEALEEELKELKKLEEiQEEQEEEELEQEIEALEERLAELee 246
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7662234  580 -LDEIESLTLRLSEEQENKRRMGDRLSHERHQFQRDKEATQELIEDLRKQLEHLQLLKLEAEQRRGRSSSmgLQEYHSRA 658
Cdd:COG0419 247 eKERLEELKARLLEIESLELEALKIREEELRELERLLEELEEKIERLEELEREIEELEEELEGLRALLEE--LEELLEKL 324
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7662234  659 ResELEQEVRRLKQDNRNLKEQNEELngqiITLSIQGAKSLfsTAFSESLAAEIssvsrDELMEAIQKQEEINFRLQDYI 738
Cdd:COG0419 325 K--SLEERLEKLEEKLEKLESELEEL----AEEKNELAKLL--EERLKELEERL-----EELEKELEKALERLKQLEEAI 391
                       250
                ....*....|....*...
gi 7662234  739 DRIIVAIMETNPSILEVK 756
Cdd:COG0419 392 QELKEELAELSAALEEIQ 409
Smc COG1196
Chromosome segregation ATPases [Cell division and chromosome partitioning]
460-706 8.63e-10

Chromosome segregation ATPases [Cell division and chromosome partitioning]


Pssm-ID: 224117 [Multi-domain]  Cd Length: 1163  Bit Score: 60.88  E-value: 8.63e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7662234   460 EDIADKVVFLERRVLELEKDTAATGEQHSRLRQENLQLVHRANALEEQLKEQELRACEMV--LEETRRQKELLCKMEREK 537
Cdd:COG1196  768 ESLEEALAKLKEEIEELEEKRQALQEELEELEEELEEAERRLDALERELESLEQRRERLEqeIEELEEEIEELEEKLDEL 847
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7662234   538 SIEIENLQTRLQQLDEENSELRSCTPCLKANIERLEEEKQKL---LDEIESLTLRLSEEQENKRRMGDRLSHERHQFQRD 614
Cdd:COG1196  848 EEELEELEKELEELKEELEELEAEKEELEDELKELEEEKEELeeeLRELESELAELKEEIEKLRERLEELEAKLERLEVE 927
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7662234   615 KEATQELIEDLRKQLEHLQLL----KLEAEQRR-GRSSSMGLQEY-HSRARESELEQEVRRLKQDNRNLKEQNEELNGQI 688
Cdd:COG1196  928 LPELEEELEEEYEDTLETELEreieRLEEEIEAlGPVNLRAIEEYeEVEERYEELKSQREDLEEAKEKLLEVIEELDKEK 1007
                        250
                 ....*....|....*...
gi 7662234   689 itlsiqgaKSLFSTAFSE 706
Cdd:COG1196 1008 --------RERFKETFDK 1017
MAD pfam05557
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ...
445-684 8.64e-10

Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.


Pssm-ID: 253253 [Multi-domain]  Cd Length: 722  Bit Score: 60.71  E-value: 8.64e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7662234    445 EALEDPSPELMEGPEEDI--ADKVVFLERRVleleKDTAATGEQHSRLRQENLQLVHRANaLEEQLKEQELRACEMVLEE 522
Cdd:pfam05557   1 DDGESNTTVMADGGNQSIlrSDLPKFLSQPL----EGSHHLGVSTSALSSLQKQVEESMT-LLQRAELIRSKSKLIQLEN 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7662234    523 TRRQKELLCKMERE----------KSIEIEN-----LQTRLQQLDEEN----SELRSCTPCLKANIERLEEEKQKLLDEI 583
Cdd:pfam05557  76 ELMQKELEHKRAQIelerkastlaENYERELdrnleLEVRLKALEELEkkaeNEAAEAEEEAKLLKDKLDAESLKLQNEK 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7662234    584 EsltLRLSEEQENKRRMGDRLSHERHQFQRDK---EATQELIEDLRKQLEHLQLLKLEAEQRRGRSSSMGLQEYHSRARE 660
Cdd:pfam05557 156 E---DQLKEAKESISRIKNDLSEMQCRAQNADtelKLLESELEELREQLEECQKELAEAEKKLQSLTSEQASSADNSVKI 232
                         250       260
                  ....*....|....*....|....
gi 7662234    661 SELEQEVRRLKQDNRNLKEQNEEL 684
Cdd:pfam05557 233 KHLEEELKRYEQDAEVVKSMKEQL 256
PRK03918 PRK03918
chromosome segregation protein; Provisional
460-684 1.13e-09

chromosome segregation protein; Provisional


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 60.46  E-value: 1.13e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7662234   460 EDIADKVVFLERRVLELEKdtaaTGEQHSRLRQeNLQLVHRANALEEQLKEQELRACEMVLEETRRQKELLCKMEREksi 539
Cdd:PRK03918 469 KEIEEKERKLRKELRELEK----VLKKESELIK-LKELAEQLKELEEKLKKYNLEELEKKAEEYEKLKEKLIKLKGE--- 540
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7662234   540 eIENLQTRLQQLDEENSELRSctpcLKANIERLEEEKQKLLDEIESLTLRLSEEQENK---------------------R 598
Cdd:PRK03918 541 -IKSLKKELEKLEELKKKLAE----LEKKLDELEEELAELLKELEELGFESVEELEERlkelepfyneylelkdaekelE 615
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7662234   599 RMGDRLSHERHQFQRDKEATQEL---IEDLRKQLEHLQLLKLEAEQRRGRSSSMGLQEYHSRARE--SELEQEVRRLKQD 673
Cdd:PRK03918 616 REEKELKKLEEELDKAFEELAETekrLEELRKELEELEKKYSEEEYEELREEYLELSRELAGLRAelEELEKRREEIKKT 695
                        250
                 ....*....|.
gi 7662234   674 NRNLKEQNEEL 684
Cdd:PRK03918 696 LEKLKEELEER 706
chromosome_segregation_protein_related_ptotein TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
469-668 1.31e-09

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: 60.47  E-value: 1.31e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7662234     469 LERRVLELEKDTAATGEQHSRLRQENLQLVHRANALEEQLKE--QELRACEMVLEETRRQKEllckmerEKSIEIENLQT 546
Cdd:TIGR02169  341 LEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAEtrDELKDYREKLEKLKREIN-------ELKRELDRLQE 413
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7662234     547 RLQQLDEENSELRsctpclkANIERLEEEKQKLLDEIESLTLRLSEEQENKRRMGDRLSHERHQFqRDKEATQELIEDLR 626
Cdd:TIGR02169  414 ELQRLSEELADLN-------AAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQEL-YDLKEEYDRVEKEL 485
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|..
gi 7662234     627 KQLEhLQLLKLEAEQRRGRSSSMGlqeyhSRARESELEQEVR 668
Cdd:TIGR02169  486 SKLQ-RELAEAEAQARASEERVRG-----GRAVEEVLKASIQ 521
SbcC COG0419
ATPase involved in DNA repair [DNA replication, recombination, and repair]
459-741 5.11e-09

ATPase involved in DNA repair [DNA replication, recombination, and repair]


Pssm-ID: 223496 [Multi-domain]  Cd Length: 908  Bit Score: 58.23  E-value: 5.11e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7662234  459 EEDIADKVVFLERRVLELEKDTAATGEQHSRLrQENLQLVHRANALEEQLKEQELRACEMVLEETRRQKELLCKMEREKS 538
Cdd:COG0419 349 AEEKNELAKLLEERLKELEERLEELEKELEKA-LERLKQLEEAIQELKEELAELSAALEEIQEELEELEKELEELERELE 427
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7662234  539 I---EIENLQTRLQQLDEENSELRSCT----PCLKANIERLEEEKQKLLD----EIESLTLRLSEEQEnKRRMGDRLSHE 607
Cdd:COG0419 428 EleeEIKKLEEQINQLESKELMIAELAgageKCPVCGQELPEEHEKELLElyelELEELEEELSREKE-EAELREEIEEL 506
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7662234  608 RHQFQRDKEATQELIE-------DLRKQLEHLQLLKLEAEQRRGRSSSMGLQEYhsRARESELEQEVRRLKQDNRNLKEQ 680
Cdd:COG0419 507 EKELRELEEELIELLEleealkeELEEKLEKLENLLEELEELKEKLQLQQLKEE--LRQLEDRLQELKELLEELRLLRTR 584
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 7662234  681 NEELngQIITLSIQGAKSLFSTAfSESLAAEISSVSRDELMEAIQKQEEINFRLQDYIDRI 741
Cdd:COG0419 585 KEEL--EELRERLKELKKKLKEL-EERLSQLEELLQSLELSEAENELEEAEEELESELEKL 642
PRK03918 PRK03918
chromosome segregation protein; Provisional
453-688 5.98e-09

chromosome segregation protein; Provisional


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 58.15  E-value: 5.98e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7662234   453 ELMEGPEEDIAD------KVVFLERRVLELEKDTAATGEQHsRLRQENLQLVHRANALEEQLKEQELRACEMVLEETRRQ 526
Cdd:PRK03918 321 EEINGIEERIKEleekeeRLEELKKKLKELEKRLEELEERH-ELYEEAKAKKEELERLKKRLTGLTPEKLEKELEELEKA 399
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7662234   527 KELLCKMEREKSIEIENLQTRLQQLDEENSELRS----CTPC---------------LKANIERLEEEKQKLLDEIESLT 587
Cdd:PRK03918 400 KEEIEEEISKITARIGELKKEIKELKKAIEELKKakgkCPVCgrelteehrkelleeYTAELKRIEKELKEIEEKERKLR 479
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7662234   588 LRLsEEQENKRRMGDRLSHERHQFQRDKEATQEL----IEDLRKQLEHLQLLKLEAEQRRGRSSSMGlqeyHSRARESEL 663
Cdd:PRK03918 480 KEL-RELEKVLKKESELIKLKELAEQLKELEEKLkkynLEELEKKAEEYEKLKEKLIKLKGEIKSLK----KELEKLEEL 554
                        250       260
                 ....*....|....*....|....*
gi 7662234   664 EQEVRRLKQDNRNLKEQNEELNGQI 688
Cdd:PRK03918 555 KKKLAELEKKLDELEEELAELLKEL 579
SbcC COG0419
ATPase involved in DNA repair [DNA replication, recombination, and repair]
444-685 6.78e-09

ATPase involved in DNA repair [DNA replication, recombination, and repair]


Pssm-ID: 223496 [Multi-domain]  Cd Length: 908  Bit Score: 57.85  E-value: 6.78e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7662234  444 MEALEDPSPELMEGPEEDIADKVVFLERRVLELEKDTAATGEQHSRLRQENLQLVHRANALEEQlkeqelracemvLEET 523
Cdd:COG0419 219 EEIQEEQEEEELEQEIEALEERLAELEEEKERLEELKARLLEIESLELEALKIREEELRELERL------------LEEL 286
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7662234  524 RRQKELLCKMEREKSIEIENLQTR---LQQLDEENSELRSctpcLKANIERLEEEKQKLLDEIESLTLRLSEEQENKRRM 600
Cdd:COG0419 287 EEKIERLEELEREIEELEEELEGLralLEELEELLEKLKS----LEERLEKLEEKLEKLESELEELAEEKNELAKLLEER 362
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7662234  601 GDRLSHERHQFQRDKEATQELIEDLRKQLEhLQLLKLEAEQRRGRSSSMGLQEyhSRARESELEQEVRRLKQDNRNLKEQ 680
Cdd:COG0419 363 LKELEERLEELEKELEKALERLKQLEEAIQ-ELKEELAELSAALEEIQEELEE--LEKELEELERELEELEEEIKKLEEQ 439

                ....*
gi 7662234  681 NEELN 685
Cdd:COG0419 440 INQLE 444
conserved_hypothetical_protein TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
485-688 9.23e-09

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: 57.34  E-value: 9.23e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7662234    485 EQHSRLrQENLQLVHRANALEEQLKEQElracemvleetrrqkellcKMEREKSIEIENLQTRLQQLDEENSELRSCTPC 564
Cdd:TIGR04523 378 ENQSYK-QEIKNLESQINDLESKIQNQE-------------------KLNQQKDEQIKKLQQEKELLEKEIERLKETIIK 437
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7662234    565 LKANIERLEEEKQKLLDEIESLTlRLSEEQENKRrmgDRLSHERHQFQRDKEATQELIEDLRKqlehlQLLKLEAEQrrg 644
Cdd:TIGR04523 438 NNSEIKDLTNQDSVKELIIKNLD-NTRESLETQL---KVLSRSINKIKQNLEQKQKELKSKEK-----ELKKLNEEK--- 505
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 7662234    645 rsssmglqeyhsrareSELEQEVRRLKQDNRNLKEQNEELNGQI 688
Cdd:TIGR04523 506 ----------------KELEEKVKDLTKKISSLKEKIEKLESEK 533
conserved_hypothetical_protein TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
460-731 1.38e-08

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: 56.95  E-value: 1.38e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7662234    460 EDIADKvvflERRVLELEKDTAATGEQHSRLRQEnlqlvhrANALEEQLKEQELracemvlEETRRQKELlckmeREKSI 539
Cdd:TIGR04523 314 SELKNQ----EKKLEEIQNQISQNNKIISQLNEQ-------ISQLKKELTNSES-------ENSEKQREL-----EEKQN 370
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7662234    540 EIE---------------------NLQTRLQQLDEENSELRSctpclkaNIERLEEEKQKLLDEIEsltlRLSEEQENKR 598
Cdd:TIGR04523 371 EIEklkkenqsykqeiknlesqinDLESKIQNQEKLNQQKDE-------QIKKLQQEKELLEKEIE----RLKETIIKNN 439
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7662234    599 RMGDRLSHERHQFQRDKEATQELIEDLRKQLEHLQL----LKLEAEQRRgrsssmglQEYHSRARE-SELEQEVRRLKQD 673
Cdd:TIGR04523 440 SEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRsinkIKQNLEQKQ--------KELKSKEKElKKLNEEKKELEEK 511
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 7662234    674 NRNLKEQNEELNGQIITLSIQgaKSLFSTAFSeSLAAEISS----VSRDELMEAIQ-KQEEIN 731
Cdd:TIGR04523 512 VKDLTKKISSLKEKIEKLESE--KKEKESKIS-DLEDELNKddfeLKKENLEKEIDeKNKEIE 571
chromosome_segregation_protein_related_ptotein TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
470-741 1.60e-08

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: 57.00  E-value: 1.60e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7662234     470 ERRVLELEKDTAATGEQHSRLRQENLQLVhRANALEEQLKEQELRACEMVLEETRRQKELLCKMEREKSIEIENLQTRLQ 549
Cdd:TIGR02169  183 EENIERLDLIIDEKRQQLERLRREREKAE-RYQALLKEKREYEGYELLKEKEALERQKEAIERQLASLEEELEKLTEEIS 261
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7662234     550 QLDEENSELRSCTPCLKANIERL-EEEKQKLLDEIESLTLRLSE----EQENKRRMGDrLSHERHQFQRDKEATQELIED 624
Cdd:TIGR02169  262 ELEKRLEEIEQLLEELNKKIKDLgEEEQLRVKEKIGELEAEIASlersIAEKERELED-AEERLAKLEAEIDKLLAEIEE 340
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7662234     625 LRKQLEHLQLLK-----------------------LEAEQRRGRSSSMGLQEYHSRARE--SELEQEVRRLKQDNRNLKE 679
Cdd:TIGR02169  341 LEREIEEERKRRdklteeyaelkeeledlraeleeVDKEFAETRDELKDYREKLEKLKReiNELKRELDRLQEELQRLSE 420
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 7662234     680 QNEELNGQIItlSIQGAKSLFSTAfSESLAAEISSvSRDELMEAIQKQEEIN---FRLQDYIDRI 741
Cdd:TIGR02169  421 ELADLNAAIA--GIEAKINELEEE-KEDKALEIKK-QEWKLEQLAADLSKYEqelYDLKEEYDRV 481
chromosome_segregation_protein_related_ptotein TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
441-688 1.79e-08

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: 56.61  E-value: 1.79e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7662234     441 ALTMEALEDPSPELMEGPEEDIADKVVFLERRVLELEKDTAATGEQHSRLRQENLQLVHRANALEEQLKEQ--ELRACEM 518
Cdd:TIGR02169  264 EKRLEEIEQLLEELNKKIKDLGEEEQLRVKEKIGELEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLlaEIEELER 343
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7662234     519 VLEETRRQKELLCKMEREKSIEIENLQTRLQQLDEENSELRSCTPCLKANIERLEEEKQKLLDEIESL---TLRLSEEQE 595
Cdd:TIGR02169  344 EIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLqeeLQRLSEELA 423
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7662234     596 NKRRMGDRLSHERHQFQRDKEATQELIEDLRKQLEHLQ--LLKLEAEQRRGRSSSMGLQ-EYHSRARE-SELEQEVRRLK 671
Cdd:TIGR02169  424 DLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAadLSKYEQELYDLKEEYDRVEkELSKLQRElAEAEAQARASE 503
                          250
                   ....*....|....*..
gi 7662234     672 QDNRNLKEQNEELNGQI 688
Cdd:TIGR02169  504 ERVRGGRAVEEVLKASI 520
PspA_IM30 pfam04012
PspA/IM30 family; This family includes PspA a protein that suppresses sigma54-dependent ...
459-641 5.97e-08

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


Pssm-ID: 252314 [Multi-domain]  Cd Length: 220  Bit Score: 52.77  E-value: 5.97e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7662234    459 EEDIADKVVFLERRVLELEKDtaatgeqHSRLRQENLQLVHRANALEEQLKEQELRACEmvLEEtrRQKELLCKME---- 534
Cdd:pfam04012  18 LDKAEDPEKMLEQAIRDMQSE-------LGKARQALAQVIARQKQLERKLEEQKEQAKK--LEN--KARAALTKGNeela 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7662234    535 REKSIEIENLQTRLQQLDEENSELRSCTPCLKANIERLEEEKQKLLDEIESLTLRLS----EEQENKRRMGDRLSHERHQ 610
Cdd:pfam04012  87 REALAEIATLEKQAEALETQLTQQRSAVEQLRKQLAALETKIQQLKAKKTALKARLKaakaQEAVNTSLGSASTESATDS 166
                         170       180       190
                  ....*....|....*....|....*....|...
gi 7662234    611 FQR--DKEATQELIEDLRKQLEHLQLLKLEAEQ 641
Cdd:pfam04012 167 FERieEKIEEREARADAAAELASAQDLDAKLEA 199
SMC_N pfam02463
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...
433-756 7.20e-08

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


Pssm-ID: 251311 [Multi-domain]  Cd Length: 1162  Bit Score: 54.59  E-value: 7.20e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7662234     433 ARYLHQSGALTMEALEDPSPELMEGPEEDIADKVVFLER---RVLELEKDTAATGEQHSRLRQENLQLVHRANALEEQLK 509
Cdd:pfam02463  603 ALNLAQLNKATLEADEDDKRAKVVEGILKDTELTKLLESakaKESGLRKGVSLEEGLAEKSELKASLSELTKELLAEQEL 682
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7662234     510 EQELRACEMVLEETRRQKELLCK------MEREKSIEIENLQTRLQQLDEENSELRSCTPCLKANIERLEEEKQKLLDEI 583
Cdd:pfam02463  683 QEKAESELAKNEILRRQEEIKKKeqrikeELKKLKLEKEELLADKVQEAQDKINEELKLLEQKIKEKEEEEEKSRLKKEE 762
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7662234     584 ESLTLRLSEEQENKRRMGDRLSHERHQFQRDKEATQELIEDLRKQLEHLQLLKLEAEQRRGRSSSMGLQEYHSRARESEL 663
Cdd:pfam02463  763 EEEEKSELSLKEKELAEEEEKTEKLKVEEEKEEKLKAQEEELRALEEELKEEAELLEEEQLLIEQEEKIKEEELEELALE 842
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7662234     664 EQEVRRLKQDNRNLKEQNEELNGQIITLSIQGAKSLfSTAFSESLAAEISSVSRDELMEAIQKQEEINFRLQDYIDRIIV 743
Cdd:pfam02463  843 LKEEQKLEKLAEEELERLEEEITKEELLQELLLKEE-ELEEQKLKDELESKEEKEKEEKKELEEESQKDNLLEEKENEIE 921
                          330
                   ....*....|...
gi 7662234     744 AIMETNPSILEVK 756
Cdd:pfam02463  922 ERIAEEAIILLKY 934
COG4487 COG4487
Uncharacterized protein conserved in bacteria [Function unknown]
469-678 9.62e-08

Uncharacterized protein conserved in bacteria [Function unknown]


Pssm-ID: 226889 [Multi-domain]  Cd Length: 438  Bit Score: 53.67  E-value: 9.62e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7662234  469 LERRVLELEKDTAATGEQHSRLRQENL--QLVHRANALEEQLKEQELracemVLEETRRQKELLCKMEREKSIEIENLQT 546
Cdd:COG4487  47 FEKEANEKRAQYRSAKKKELSQLEEQLinQKKEQKNLFNEQIKQFEL-----ALQDEIAKLEALELLNLEKDKELELLEK 121
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7662234  547 RLQQLDEENSELRSctpcLKANIERLEEEKQKlldeiESLTLRLSEEQENKrrmgDRLSHERHQFQRDKEATQELIEDLR 626
Cdd:COG4487 122 ELDELSKELQKQLQ----NTAEIIEKKRENNK-----NEERLKFENEKKLE----ESLELEREKFEEQLHEANLDLEFKE 188
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....
gi 7662234  627 KQlEHLQLLKLEAE--QRRGRSSSMGLQeyhSRARESELEQEVRRLKQDNRNLK 678
Cdd:COG4487 189 NE-EQRESKWAILKklKRRAELGSQQVQ---GEALELPNESFIRSKFPSDINEK 238
conserved_hypothetical_protein TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
509-738 1.03e-07

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: 53.87  E-value: 1.03e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7662234    509 KEQELRACEMVLEETRRQKELLckmEREKSI---EIENLQTR-----------------LQQLDEENSELRSCTPCLKAN 568
Cdd:TIGR04523 150 KEKELEKLNNKYNDLKKQKEEL---ENELNLlekEKLNIQKNidkiknkllklelllsnLKKKIQKNKSLESQISELKKQ 226
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7662234    569 IERLEEEKQKLLDEIESLTLRLSEEQENKRRMGDRLSHERHQF---QRDKEATQELIEDLRKQLEHL--QLLKLEAEQRR 643
Cdd:TIGR04523 227 NNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLsekQKELEQNNKKIKELEKQLNQLksEISDLNNQKEQ 306
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7662234    644 GRSSSMG---------LQEYHSRARE-----SELEQEVRRLKQ-------DNRNLKEQNEELNGQIITLSIQGAKSLFSt 702
Cdd:TIGR04523 307 DWNKELKselknqekkLEEIQNQISQnnkiiSQLNEQISQLKKeltnsesENSEKQRELEEKQNEIEKLKKENQSYKQE- 385
                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 7662234    703 afSESLAAEISsvsrdELMEAIQKQEEINFRLQDYI 738
Cdd:TIGR04523 386 --IKNLESQIN-----DLESKIQNQEKLNQQKDEQI 414
Smc COG1196
Chromosome segregation ATPases [Cell division and chromosome partitioning]
532-741 1.30e-07

Chromosome segregation ATPases [Cell division and chromosome partitioning]


Pssm-ID: 224117 [Multi-domain]  Cd Length: 1163  Bit Score: 53.95  E-value: 1.30e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7662234   532 KMEREKS-IEIENLQTRLQQLDEENSELRSctpclkaNIERLEEEKQKLLDEiesltLRLSEEqenKRRMGDRLSHERH- 609
Cdd:COG1196  171 KERKEEAeRKLERTEENLERLEDLLEELEK-------QLEKLERQAEKAERY-----QELKAE---LRELELALLLAKLk 235
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7662234   610 QFQRDKEATQELIEDLRKQLEHLQLLKLEAEQRrgrsssmgLQEYhsRARESELEQEVRRLKQDNRNLKEQNEELNGQII 689
Cdd:COG1196  236 ELRKELEELEEELSRLEEELEELQEELEEAEKE--------IEEL--KSELEELREELEELQEELLELKEEIEELEGEIS 305
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 7662234   690 TLSIQgAKSLFSTAFSESLAAEISSVSRDELMEAIQKQEEINFRLQDYIDRI 741
Cdd:COG1196  306 LLRER-LEELENELEELEERLEELKEKIEALKEELEERETLLEELEQLLAEL 356
HOOK pfam05622
HOOK protein; This family consists of several HOOK1, 2 and 3 proteins from different ...
435-734 1.81e-07

HOOK protein; This family consists of several HOOK1, 2 and 3 proteins from different eukaryotic organisms. The different members of the human gene family are HOOK1, HOOK2 and HOOK3. Different domains have been identified in the three human HOOK proteins, and it was demonstrated that the highly conserved NH2-domain mediates attachment to microtubules, whereas the central coiled-coil motif mediates homodimerization and the more divergent C-terminal domains are involved in binding to specific organelles (organelle-binding domains). It has been demonstrated that endogenous HOOK3 binds to Golgi membranes, whereas both HOOK1 and HOOK2 are localized to discrete but unidentified cellular structures. In mice the Hook1 gene is predominantly expressed in the testis. Hook1 function is necessary for the correct positioning of microtubular structures within the haploid germ cell. Disruption of Hook1 function in mice causes abnormal sperm head shape and fragile attachment of the flagellum to the sperm head.


Pssm-ID: 253283 [Multi-domain]  Cd Length: 713  Bit Score: 53.26  E-value: 1.81e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7662234    435 YLHQSGALTMEALEDPSPELMEGPE---EDIADKVVfLERRVLELEKDTAATGEQHSRLRQENLQLVHRANALE------ 505
Cdd:pfam05622 155 SKEQGSSPSRESAGNLDQQLKKALEdlkEAQEEKDE-LAQRCHELDKQVLLLQEEKNSLQQENEKLQERLAQLEgsslgp 233
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7662234    506 ---------------EQLKEQELRAcemvleETRRQKELLCKMEREKSI--------EIENLQTRLQQLDEENSELRSCT 562
Cdd:pfam05622 234 nqlgskkynllqsqlEQLQEENFRL------EAARDDYRIKCEELEKELaelqhrndELTSLAAESQALKDEIDVLRESS 307
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7662234    563 PCLKANIERLEEEKQKLLD------EIESLtlrlseEQENKRRMGDRLSHERHqfQRDKEATQELIEDLRKQLEHLQlLK 636
Cdd:pfam05622 308 DKAKKLEAQVETYKKKLEDlndlrrQVKLL------EERNAMYMQNTVQLEEE--LKKANAARGQLETYKRQVQELH-AK 378
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7662234    637 LEAEQRRGRSSSM---GLQEYHsrareSELEQEVRRLKQDNRNLKEQNEEL---NGQIITLSIQGAKSLFStafSESLAA 710
Cdd:pfam05622 379 LSEESKKADKLEFeykRLEEKL-----EALQKEKERLLAERDSLRETNEELrcgQAQQDQLTQADAGTSPS---GDNLAA 450
                         330       340
                  ....*....|....*....|....
gi 7662234    711 EISSVsrdELMEAIQKQEEINFRL 734
Cdd:pfam05622 451 ELLPS---EYREKLIRLQHENKML 471
SMC_N pfam02463
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...
475-732 2.37e-07

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


Pssm-ID: 251311 [Multi-domain]  Cd Length: 1162  Bit Score: 53.05  E-value: 2.37e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7662234     475 ELEKDTAATGEQHSRLRQENLQLVHRANALEEQLKEQELRACEMVL-----------------EETRRQKELLCKMEREK 537
Cdd:pfam02463  182 ETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEENLlyldylklneeridllqELLRDEQEEIESSKQEL 261
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7662234     538 SIEIENLQTRLQQLDEENSELRSCTPCLKANIERLEEEKQKLLDEIESLTLRLSEEQENKRRMG-------------DRL 604
Cdd:pfam02463  262 EKEEEILAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDEEKLKESEKELKklekelkkekeeiEEL 341
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7662234     605 SHERHQFQRDKEATQELIEDLRKQLEHLQLLKLEAEQRRGRSSSM------GLQEYHSRA----RESELEQEVRRLKQDn 674
Cdd:pfam02463  342 EKELKELEIKREAEEEEEEQLEKLQEKLEQLEEELLAKKKLESERlssaakLKEEELELKneeeKEAKLLLELSEQEED- 420
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 7662234     675 RNLKEQNEELNGQIITLSIQGAKSLFSTAFSESLAAEISSVSRDELMEaiqKQEEINF 732
Cdd:pfam02463  421 LLKEEKKEELKIVEELEESLETKQGKLTEEKEELEKQALKLLKDKLEL---KKSEDLL 475
DUF4659 pfam15558
Domain of unknown function (DUF4659); This family of proteins is found in eukaryotes. Proteins ...
468-693 2.74e-07

Domain of unknown function (DUF4659); This family of proteins is found in eukaryotes. Proteins in this family are typically between 427 and 674 amino acids in length. There are two completely conserved residues (D and I) that may be functionally important.


Pssm-ID: 259689 [Multi-domain]  Cd Length: 376  Bit Score: 52.05  E-value: 2.74e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7662234    468 FLERRVLELEKDTAATGEQHSRLRQENLQLVHRANALEEQLKEQELRACEMVLEETRRQKELLcKMEREKSIEienlQTR 547
Cdd:pfam15558  85 DRQAKIAEKESRWREQLEDQENLRQEKLERAKTQAEHRKQCQEQNLKEQEEMLRALREQNELQ-LQRRLEQAC----RKR 159
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7662234    548 LQQLDEENSELRsctpcLKANIERLEEEKQKLLDEI----ESLTLRLSEEQ--------------ENKRRMGDRLSHERH 609
Cdd:pfam15558 160 QKHETEGQKKVQ-----ENNLSSLLNHQARKVLMDCqakaEELLLRLSLEQshqrsqenyeqlikERHRELREKAQKEEE 234
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7662234    610 QFQRDKEATQELIEDLRKQLEHLQLLKLEAEQRRGRSSSMGLQEYHSRARESELEQEvrRLKQDNRNLKEQNEELNGQII 689
Cdd:pfam15558 235 QFQRAKWRAEEKEEERKEHKEALAELADQKIQQARSIAHKTVQDKAQRARELRLLRE--KNQHILKLKVEKEEKCHREGI 312

                  ....
gi 7662234    690 TLSI 693
Cdd:pfam15558 313 KEAI 316
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
485-688 3.09e-07

Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.


Pssm-ID: 144972 [Multi-domain]  Cd Length: 859  Bit Score: 52.74  E-value: 3.09e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7662234    485 EQHSRLRQENLQLVHRANALEEQLK---------EQELRACEMVLEETRRQKELLCKMEREKSIEIENLQTRLQQLDEEN 555
Cdd:pfam01576 208 SQKSRLQSENSDLTRQLEEAEAQVSnlsklksqlESQLEEAKRSLEEESRERANLQAQLRQLEHDLDSLREQLEEESEAK 287
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7662234    556 SELRSctPCLKANIE------RLEEEKQKLLDEIESLTLRLSEEQENKRRMGDRLSHERHQFQRDKEATQELIEDLRKQL 629
Cdd:pfam01576 288 AELER--QLSKANAEiqqwrsKFESEGALRAEELEELKKKLNQKISELEEAAEAANAKCDSLEKTKSRLQSELEDLQIEL 365
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 7662234    630 EHLQLLKLEAEqRRGRSSSMGLQEYhsRARESELEQEVRRLKQDNRNLKEQNEELNGQI 688
Cdd:pfam01576 366 ERANAAASELE-KKQKNFDKILAEW--KRKVDELQAELDTAQREARNLSTELFRLKNEL 421
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
469-692 3.14e-07

Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.


Pssm-ID: 144972 [Multi-domain]  Cd Length: 859  Bit Score: 52.74  E-value: 3.14e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7662234    469 LERRVLELEKDTAATGEQHSRLRQENLQLVHRANALEEQLKEQElracemvlEETRRQKELLCKMEREksieienLQTRL 548
Cdd:pfam01576  44 LEARIRELEEELEAERAARAKAEKARADLSRELEELSERLEEAG--------GATAAQIELNKKREAE-------LAKLR 108
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7662234    549 QQLDEENselrsctpclKANIERLEEEKQKLLDEIESLtlrlSEEQENKRRMGDRLSHERHQFQRDkeatqelIEDLRKQ 628
Cdd:pfam01576 109 KDLEEAN----------LQHEEALATLRKKHQDAINEL----SEQIEQLQKQKAKAEKEKSQLQAE-------VDDLLAQ 167
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 7662234    629 LEHLQLLKLEAEQRRGRSSSMgLQEYHSRARE-----SELEQEVRRLKQDNRNLKEQNEELNGQIITLS 692
Cdd:pfam01576 168 LDQIAKAKLNAEKKAKQLESQ-LSELQVKLDElqrqlNDLTSQKSRLQSENSDLTRQLEEAEAQVSNLS 235
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
471-678 5.52e-07

Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.


Pssm-ID: 144972 [Multi-domain]  Cd Length: 859  Bit Score: 51.58  E-value: 5.52e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7662234    471 RRVLELEKDTAATGEQHSRLRQ---ENLQLV-HRANALEEQLKEqeLRACEMVLEETRRQKEllckmereksieienlqT 546
Cdd:pfam01576 577 KKYQQQVKELQTQVEEEQRAREdarEQLAVAeRRATALEAELEE--LRSALEQAERARKQAE-----------------T 637
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7662234    547 RLQQLDEENSELRSCTPCLKANIERLEEEKQKLLDEIESLT--LRLSEEQENK-----RRMGDRLSHERHQFQRdkeatq 619
Cdd:pfam01576 638 ELAEASERVNELTAQNSSLIAQKRKLEGELAALQSDLDEAVneLKAAEERAKKaqadaARLAEELRQEQEHSQH------ 711
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 7662234    620 elIEDLRKQLE------HLQLLKLEAEQRRGRSSSMGLQEYHSRARESELEQEVRRLKQDNRNLK 678
Cdd:pfam01576 712 --LERLRKQLEsqvkelQVRLDEAEAAALKGGKKMIQKLEARVRELEAELDGEQRRHAETQKNLR 774
PRK03918 PRK03918
chromosome segregation protein; Provisional
444-686 7.20e-07

chromosome segregation protein; Provisional


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 51.22  E-value: 7.20e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7662234   444 MEALEDPSPELMEGPEEDIADKVVFLERRVLELEKDTAATGEQHSRLRQENLQLVHRANALEEqlKEQELRACEMVLEET 523
Cdd:PRK03918 371 KEELERLKKRLTGLTPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKK--AKGKCPVCGRELTEE 448
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7662234   524 RRqKELLckmeREKSIEIENLQTRLQQLDEENSELRSctPCLKANIERLEEEK----QKLLDEIESLTLRLS-------- 591
Cdd:PRK03918 449 HR-KELL----EEYTAELKRIEKELKEIEEKERKLRK--ELRELEKVLKKESEliklKELAEQLKELEEKLKkynleele 521
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7662234   592 ---EEQENKRRMGDRLSHERHQFQRDKEATQELIEDLRKQLEHLQLLKLEAEQRRGRSSSMG-------------LQEYH 655
Cdd:PRK03918 522 kkaEEYEKLKEKLIKLKGEIKSLKKELEKLEELKKKLAELEKKLDELEEELAELLKELEELGfesveeleerlkeLEPFY 601
                        250       260       270
                 ....*....|....*....|....*....|....*.
gi 7662234   656 SR-----ARESELEQEVRRLKQDNRNLKEQNEELNG 686
Cdd:PRK03918 602 NEylelkDAEKELEREEKELKKLEEELDKAFEELAE 637
COG4942 COG4942
Membrane-bound metallopeptidase [Cell division and chromosome partitioning]
459-673 7.99e-07

Membrane-bound metallopeptidase [Cell division and chromosome partitioning]


Pssm-ID: 227278 [Multi-domain]  Cd Length: 420  Bit Score: 50.88  E-value: 7.99e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7662234  459 EEDIADkvvfLERRVLELEKDTAATGEQHSRLRQENLQLVHRANALEEQLKEQELRACEMV--LEETRRQKELLCKMERE 536
Cdd:COG4942  65 EKQLKS----LETEIASLEAQLIETADDLKKLRKQIADLNARLNALEVQEREQRRRLAEQLaaLQRSGRNPPPALLVSPE 140
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7662234  537 KSIEIENLQTRLQQLdeeNSELRSCTPCLKANIERLEEEKQKLLDEIESLTLRLSEEQENKRRMgDRLSHERhqfQRDKE 616
Cdd:COG4942 141 DAQRSVRLAIYYGAL---NPARAERIDALKATLKQLAAVRAEIAAEQAELTTLLSEQRAQQAKL-AQLLEER---KKTLA 213
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 7662234  617 ATQELIEDLRKQLEHLQLLK--LEAEQRRGRSSSMGLQEyhsrARESELEQEVRRLKQD 673
Cdd:COG4942 214 QLNSELSADQKKLEELRANEsrLKNEIASAEAAAAKARE----AAAAAEAAAARARAAE 268
PTZ00121 PTZ00121
MAEBL; Provisional
453-754 9.50e-07

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 51.30  E-value: 9.50e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7662234    453 ELMEGPEEDIADKVvfleRRVLELEKDTAATGEQHSRLRQENLQLVHRANALEEQLKEQELRACEMVLEETRRQKELLCK 532
Cdd:PTZ00121 1538 EAKKAEEKKKADEL----KKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAK 1613
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7662234    533 MEREKSIEIENLQtrlqqldeENSELRSCTPCLKanieRLEEEKQKLLDEIESltlrlsEEQENKRRMGDRLSHERHQFQ 612
Cdd:PTZ00121 1614 KAEEAKIKAEELK--------KAEEEKKKVEQLK----KKEAEEKKKAEELKK------AEEENKIKAAEEAKKAEEDKK 1675
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7662234    613 RDKEATQELiEDLRKQLEhlQLLKLEAEQRRGRSSSMGLQEYHSRARESELEQEVRRLKQDNRNLKEQNEELNGQIITLS 692
Cdd:PTZ00121 1676 KAEEAKKAE-EDEKKAAE--ALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKD 1752
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 7662234    693 IQGAKSLFSTAFSESLAAEISSVSRDELMEAIQKQEEINFRLQdyIDRIIVAIMETNPSILE 754
Cdd:PTZ00121 1753 EEEKKKIAHLKKEEEKKAEEIRKEKEAVIEEELDEEDEKRRME--VDKKIKDIFDNFANIIE 1812
SCP-1 pfam05483
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ...
510-731 9.80e-07

Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.


Pssm-ID: 114219 [Multi-domain]  Cd Length: 787  Bit Score: 50.88  E-value: 9.80e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7662234    510 EQELRACEMVLEETRRQKELLCKMEREKSIEIENLQTRLQQLDEENSEL-------------------RSCTPCLKANIE 570
Cdd:pfam05483  98 EAELKQKENKLQENRKIIEAQRKAIQELQFENEKVSLKLEEEIQENKDLikennatrhlcnllketcaRSAEKTKKYEYE 177
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7662234    571 RlEEEKQKLLD---EIESLTLRLSE---EQENKR-RMGDRLSHERHQFQRDKEATQELIEDLRKQLEhLQLLKLEAEQRR 643
Cdd:pfam05483 178 R-EETRQVYMDlnnNIEKMILAFEElrvQAENARlEMHFKLKEDHEKIQHLEEEYKKEINDKEKQVS-LLLIQITEKENK 255
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7662234    644 GRSSSMGLQEyhSRARESELEQEVRRLKQDNRNLKEQNEELNGQI--ITLSIQGAKSLfSTAFSESLaaEISSVSRDELM 721
Cdd:pfam05483 256 MKDLTFLLEE--SRDKANQLEEKTKLQDENLKELIEKKDHLTKELedIKMSLQRSMST-QKALEEDL--QIATKTICQLT 330
                         250
                  ....*....|.
gi 7662234    722 EAIQKQ-EEIN 731
Cdd:pfam05483 331 EEKEAQmEELN 341
HAP1_N pfam04849
HAP1 N-terminal conserved region; This family represents an N-terminal conserved region found ...
485-672 9.81e-07

HAP1 N-terminal conserved region; This family represents an N-terminal conserved region found in several huntingtin-associated protein 1 (HAP1) homologues. HAP1 binds to huntingtin in a polyglutamine repeat-length-dependent manner. However, its possible role in the pathogenesis of Huntington's disease is unclear. This family also includes a similar N-terminal conserved region from hypothetical protein products of ALS2CR3 genes found in the human juvenile amyotrophic lateral sclerosis critical region 2q33-2q34.


Pssm-ID: 191111 [Multi-domain]  Cd Length: 307  Bit Score: 49.82  E-value: 9.81e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7662234    485 EQHSRLRQENLQLVHRANALEEQL----KEQELRACEMVLEETRRQKEllCKMEREKSIEIENLQTRLQQLDEENSELRS 560
Cdd:pfam04849 105 EQLGKARDEILQLRHELNLKDELLqfysDADEESEDESSESTPLRPQE--SSSSSHGCFQLEALQEKLKLLEEENEHLRS 182
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7662234    561 CTPCLKANIERLEEEKQKLldeIESLTLRLSEEQENKRRMGDRLSHERHQFQRDKEATQEL---IEDLRKQL-------E 630
Cdd:pfam04849 183 EASHLKTETVTYEEKEQQL---VNDCVKQLREANDQIASLSEELAKKTEDLERQQEEITHLlsqIVDLQKKCksyalenE 259
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 7662234    631 HLQLLkLEAEQRRGRSSSMGLQEYHSRARE-----SELEQEVRRLKQ 672
Cdd:pfam04849 260 ELQQH-LAAAKDAQRQLQAELQELQDKYAEcmemlHEAQEELKNLRN 305
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
489-745 1.02e-06

Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.


Pssm-ID: 144972 [Multi-domain]  Cd Length: 859  Bit Score: 50.81  E-value: 1.02e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7662234    489 RLRQENLQLVHRANALEEQLKEQELRACEMVLEETRRQKE---LLCKMEREKSiEIENLQTRLQQLDEENSEL------- 558
Cdd:pfam01576 367 RANAAASELEKKQKNFDKILAEWKRKVDELQAELDTAQREarnLSTELFRLKN-ELEELKDQVEALRRENKNLqdeihdl 445
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7662234    559 --------RSCTPcLKANIERLEEEKQKLLDEIESLTLRLSEEQENKRRMGDRLSHERHQFQRDKEATQELIEDLRK--- 627
Cdd:pfam01576 446 tdqlgeggRNVHE-LEKARRRLEAEKDELQAALEEAEAALELEESKVLRAQVELSQIRSEIERRLAEKEEEFENTRKnhq 524
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7662234    628 -QLEHLQlLKLEAEQrRGRSSSMGLQEyhsraresELEQEVRRLKQDNRNLKEQNEELNGQIITLSiQGAKSLfstafse 706
Cdd:pfam01576 525 rAIESLQ-ATLEAEA-KGKAEASRLKK--------KLEGDINELEIALDHANKANAEAQKNVKKYQ-QQVKEL------- 586
                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 7662234    707 SLAAEISSVSRDELMEAIQKQEEINFRLQDYIDRIIVAI 745
Cdd:pfam01576 587 QTQVEEEQRAREDAREQLAVAERRATALEAELEELRSAL 625
MAD pfam05557
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ...
484-687 1.04e-06

Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.


Pssm-ID: 253253 [Multi-domain]  Cd Length: 722  Bit Score: 50.70  E-value: 1.04e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7662234    484 GEQHSRLRQENLQLVHRANALEEQLKEQELRACEMVLEETrrQKELLCKMERekSIEIENLQTRLQQLDEENSELRSCTP 563
Cdd:pfam05557 292 DLQSRLERFEKMREKLADLELEKEKLENELKSWKSLLQDI--GLNLRTPDDL--SRRIVVLQNEELQLKEKNGSISSSAK 367
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7662234    564 CLKANIERLEEEKQKLLDEIESLTLRLSEEQENKRRMGDRLSherhQFQRDKEATQELIEDLRKQLEHLQlLKLEAEQRR 643
Cdd:pfam05557 368 QLETTLQQLQLERQKAVSEILELKKKLEALKALVRRLQRRLT----LVTKERDGLRAILNSYDKELTETS-VSGQLMKRL 442
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 7662234    644 GRSSSM--GLQEYHSR--ARESELEQEVRRLKQDNRNLKEQNEELNGQ 687
Cdd:pfam05557 443 EEAEDLvqKVQSHLAKmeNQLSELEEDVGQQKDRNNTLETEIKLLKEQ 490
COG4372 COG4372
Uncharacterized protein conserved in bacteria with the myosin-like domain [Function unknown]
472-694 1.11e-06

Uncharacterized protein conserved in bacteria with the myosin-like domain [Function unknown]


Pssm-ID: 226809 [Multi-domain]  Cd Length: 499  Bit Score: 50.41  E-value: 1.11e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7662234  472 RVLELEKDTAATGEQHSRLRQENLQLVHRANALEEQLKEQELRACEMvlEETRRQKELlckmeREKSIEIENLQTRLQQL 551
Cdd:COG4372  84 RALRTELGTAQGEKRAAETEREAARSELQKARQEREAVRQELAAARQ--NLAKAQQEL-----ARLTKQAQDLQTRLKTL 156
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7662234  552 DEENSELRSCTPCLKANIERLeeekQKLLDEIESLTLRLSEEQEnkrrmgdRLSHERHQFQRDKEATQELIEDLRKQLEH 631
Cdd:COG4372 157 AEQRRQLEAQAQSLQASQKQL----QASATQLKSQVLDLKLRSA-------QIEQEAQNLATRANAAQARTEELARRAAA 225
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7662234  632 LQLLKLEAEQRRGRSSSMGLQ---------EYHSRARESE-----LEQEVRRLK---QDNRNLKEQNEEL-NGQIITLSI 693
Cdd:COG4372 226 AQQTAQAIQQRDAQISQKAQQiaaraeqirERERQLQRLEtaqarLEQEVAQLEayyQAYVRLRQQAAATqRGQVLAGAA 305

                .
gi 7662234  694 Q 694
Cdd:COG4372 306 Q 306
SbcC COG0419
ATPase involved in DNA repair [DNA replication, recombination, and repair]
469-741 1.19e-06

ATPase involved in DNA repair [DNA replication, recombination, and repair]


Pssm-ID: 223496 [Multi-domain]  Cd Length: 908  Bit Score: 50.53  E-value: 1.19e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7662234  469 LERRVLELEKDTAATGEQHSRLRQENLQLVHRANALEEQLKEQELRACEMVLEETRRQKELLCKMER--EKSIEIENLQT 546
Cdd:COG0419 401 LSAALEEIQEELEELEKELEELERELEELEEEIKKLEEQINQLESKELMIAELAGAGEKCPVCGQELpeEHEKELLELYE 480
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7662234  547 RLQQLDEENSELRSCtpclkanIERLEEEKQKLLDEIESL-TLRLSEEQENKRRMGDrlsherhqFQRDKEATQELIEDL 625
Cdd:COG0419 481 LELEELEEELSREKE-------EAELREEIEELEKELRELeEELIELLELEEALKEE--------LEEKLEKLENLLEEL 545
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7662234  626 RKQLEHLQLLKLEAEQRRGRSSsmgLQEYHS----RARESELEQEVRRLKQDNRNLKEQNEELNGQIITLsiqgaKSLFS 701
Cdd:COG0419 546 EELKEKLQLQQLKEELRQLEDR---LQELKElleeLRLLRTRKEELEELRERLKELKKKLKELEERLSQL-----EELLQ 617
                       250       260       270       280
                ....*....|....*....|....*....|....*....|..
gi 7662234  702 TAFSESLAAEISSVSRD--ELMEAIQKQEEINFRLQDYIDRI 741
Cdd:COG0419 618 SLELSEAENELEEAEEEleSELEKLNLQAELEELLQAALEEL 659
Chromosome_partition_protein_Smc TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
460-633 1.23e-06

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: 50.83  E-value: 1.23e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7662234     460 EDIADKVVFLERRVLELEKDTAATGEQHSRLRQENLQLVHRANALEEQLKEQELRACEMVLEETRRQKELlckmeREKSI 539
Cdd:TIGR02168  333 DELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEI-----ERLEA 407
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7662234     540 EIENLQTRLQQLDEENSELRS--CTPCLKANIERLEEEKQKLLDEIESLTlRLSEEQENKRRMGDRLSHERHQFQRDKEA 617
Cdd:TIGR02168  408 RLERLEDRRERLQQEIEELLKklEEAELKELQAELEELEEELEELQEELE-RLEEALEELREELEEAEQALDAAERELAQ 486
                          170
                   ....*....|....*.
gi 7662234     618 TQELIEDLRKQLEHLQ 633
Cdd:TIGR02168  487 LQARLDSLERLQENLE 502
Nuclease_SbcCD_subunit_C TIGR00618
exonuclease SbcC; All proteins in this family for which functions are known are part of an ...
462-694 1.24e-06

exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]


Pssm-ID: 129705 [Multi-domain]  Cd Length: 1042  Bit Score: 50.74  E-value: 1.24e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7662234     462 IADKVVFLERRVL-----ELEKDTAATGEQHSRLRQENLQLVHRANALEEQLKEQELRACEMVLEETrrQKELLCKMERE 536
Cdd:TIGR00618  585 DIPNLQNITVRLQdltekLSEAEDMLACEQHALLRKLQPEQDLQDVRLHLQQCSQELALKLTALHAL--QLTLTQERVRE 662
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7662234     537 KSI-----EIENLQTRLQQLDEENSELRSCTPCLkaniERLEEeKQKLLDEIESLTLRLSEEQEnkrrmgdRLSHERHQF 611
Cdd:TIGR00618  663 HALsirvlPKELLASRQLALQKMQSEKEQLTYWK----EMLAQ-CQTLLRELETHIEEYDREFN-------EIENASSSL 730
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7662234     612 QRDKEATQELIEDLRKQLEHLQLLKL----EAEQRRGRSSSMGLQeyhsrareseLEQEVRRLKQDNRNLKEQNEELNGQ 687
Cdd:TIGR00618  731 GSDLAAREDALNQSLKELMHQARTVLkartEAHFNNNEEVTAALQ----------TGAELSHLAAEIQFFNRLREEDTHL 800

                   ....*..
gi 7662234     688 IITLSIQ 694
Cdd:TIGR00618  801 LKTLEAE 807
Nuclease_SbcCD_subunit_C TIGR00618
exonuclease SbcC; All proteins in this family for which functions are known are part of an ...
464-672 1.26e-06

exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]


Pssm-ID: 129705 [Multi-domain]  Cd Length: 1042  Bit Score: 50.74  E-value: 1.26e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7662234     464 DKVVFLERRVLELEKDTAATGEQHSRLRQEnLQLVHRANALEEQLKE-----QELRACEMVLEETRRQKELLCKMER--- 535
Cdd:TIGR00618  219 ERKQVLEKELKHLREALQQTQQSHAYLTQK-REAQEEQLKKQQLLKQlrariEELRAQEAVLEETQERINRARKAAPlaa 297
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7662234     536 -EKSIE-----IENLQTRLQQLDEENSELRSCTPCLKANIERLEEEKQKL--LDEIESLTLRLSEEQENKRRMGDR---L 604
Cdd:TIGR00618  298 hIKAVTqieqqAQRIHTELQSKMRSRAKLLMKRAAHVKQQSSIEEQRRLLqtLHSQEIHIRDAHEVATSIREISCQqhtL 377
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 7662234     605 SHERHQFQRDKEATQELIEDLRKQLEHLQLLKLEAEQRRGRSSSMGLQEYHSRAREsELEQEVRRLKQ 672
Cdd:TIGR00618  378 TQHIHTLQQQKTTLTQKLQSLCKELDILQREQATIDTRTSAFRDLQGQLAHAKKQQ-ELQQRYAELCA 444
PRK02224 PRK02224
chromosome segregation protein; Provisional
439-683 1.34e-06

chromosome segregation protein; Provisional


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 50.42  E-value: 1.34e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7662234   439 SGALTMEALEDPSPELMEGPEEDIADKVVFLERRVLELEKDTAATGEQHSRLRQENLQLVHRANALEEQLK--EQELRAC 516
Cdd:PRK02224 296 DDLLAEAGLDDADAEAVEARREELEDRDEELRDRLEECRVAAQAHNEEAESLREDADDLEERAEELREEAAelESELEEA 375
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7662234   517 EMVLEETRRQKELLCKMEREKS-------IEIENLQTRLQQLDEENSELRSCTPCLKANIERLE---EEKQKLLDE---- 582
Cdd:PRK02224 376 REAVEDRREEIEELEEEIEELRerfgdapVDLGNAEDFLEELREERDELREREAELEATLRTARervEEAEALLEAgkcp 455
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7662234   583 ---------------------IESLTLRLSEEQENKRRMGDRlsHERHQFQRDKEATQELIEDLRKQLEHLqllkleAEQ 641
Cdd:PRK02224 456 ecgqpvegsphvetieedrerVEELEAELEDLEEEVEEVEER--LERAEDLVEAEDRIERLEERREDLEEL------IAE 527
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|..
gi 7662234   642 RRGRSSSMGLQEYHSRARESELEQEVRRLKQDNRNLKEQNEE 683
Cdd:PRK02224 528 RRETIEEKRERAEELRERAAELEAEAEEKREAAAEAEEEAEE 569
TPR_MLP1_2 pfam07926
TPR/MLP1/MLP2-like protein; The sequences featured in this family are similar to a region of ...
540-692 1.37e-06

TPR/MLP1/MLP2-like protein; The sequences featured in this family are similar to a region of human TPR protein and to yeast myosin-like proteins 1 (MLP1) and 2 (MLP2). These proteins share a number of features; for example, they all have coiled-coil regions and all three are associated with nuclear pores. TPR is thought to be a component of nuclear pore complex- attached intra-nuclear filaments, and is implicated in nuclear protein import. Moreover, its N-terminal region is involved in the activation of oncogenic kinases, possibly by mediating the dimerization of kinase domains or by targeting these kinases to the nuclear pore complex. MLP1 and MLP2 are involved in the process of telomere length regulation, where they are thought to interact with proteins such as Tel1p and modulate their activity.


Pssm-ID: 254520 [Multi-domain]  Cd Length: 132  Bit Score: 47.29  E-value: 1.37e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7662234    540 EIENLQTRLQQLDEEnselrsctpclkanIERLEEEKQKLLDEIESLTLRLSEEQENkrrmgdrlsHERhQFQRDKEATQ 619
Cdd:pfam07926   4 EKSSLQAELKRLLEK--------------KEDAEAKIQKLQEDLEEQAEIANEAQQK---------YER-ELVKHAEDIE 59
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 7662234    620 ELIEdLRKQLEHLQL----LKLEAEQRRgrsSSMGLQEYHSRARESELEQEVRRLKQDNRNLKEQNEELNGQIITLS 692
Cdd:pfam07926  60 ELQA-LREQLNELKKeiaqLKAEAESAQ---AELSEAEESWEEQKKMLEDELSELEKRIEELQEQNKLLHDQIELLS 132
SCP-1 pfam05483
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ...
473-731 1.62e-06

Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.


Pssm-ID: 114219 [Multi-domain]  Cd Length: 787  Bit Score: 50.11  E-value: 1.62e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7662234    473 VLELEKDTAATGEQHSRLRQENL-QLVHRANALEEQLKE-----QELRACEMVLEETRR-QKELLCKMEREKSIEIENLQ 545
Cdd:pfam05483 262 LLEESRDKANQLEEKTKLQDENLkELIEKKDHLTKELEDikmslQRSMSTQKALEEDLQiATKTICQLTEEKEAQMEELN 341
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7662234    546 TRLQQLDEENSELRSCTPCLKaniERLEEEKQKL---LDEIESLTLRLSEEQENKRRMGDRLSHERHQFQRDKE--ATQE 620
Cdd:pfam05483 342 KAKAAHSFVVTEFEATTCSLE---ELLRTEQQRLeknEDQLKIITMELQKKSSELEEMTKFKNNKEVELEELKKilAEDE 418
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7662234    621 LIEDLRKQLEHL--------QLLKLEAEQRRGRSSSMGLQEYHSRARESELEQEVRRLKQDNRNLKEQNEELNGQIITLS 692
Cdd:pfam05483 419 KLLDEKKQFEKIaeelkgkeQELIFLLQAREKEIHDLEIQLTAIKTSEEHYLKEVEDLKTELEKEKLKNIELTAHCDKLL 498
                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 7662234    693 IQGAKslfstafsesLAAEISsvsrDELMEAIQKQEEIN 731
Cdd:pfam05483 499 LENKE----------LTQEAS----DMTLELKKHQEDII 523
COG2433 COG2433
Uncharacterized conserved protein [Function unknown]
513-645 2.99e-06

Uncharacterized conserved protein [Function unknown]


Pssm-ID: 225288 [Multi-domain]  Cd Length: 652  Bit Score: 49.32  E-value: 2.99e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7662234  513 LRACEMVLEETRRQKELLCKMEREKSI------EIENLQTRLQQLDEENSELRSCTPCLKANIERLEEEKQKLLDEIESl 586
Cdd:COG2433 390 LAEALSKVKEEERPREKEGTEEEERREitvyekRIKKLEETVERLEEENSELKRELEELKREIEKLESELERFRREVRD- 468
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 7662234  587 TLRLSEEQENKRRMGDRLsherhqfQRDKEATQELIEDLRKQLEhlQLLKLEAEQRRGR 645
Cdd:COG2433 469 KVRKDREIRARDRRIERL-------EKELEEKKKRVEELERKLA--ELRKMRKLELSGK 518
CALCOCO1 pfam07888
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ...
485-597 3.44e-06

Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.


Pssm-ID: 116500 [Multi-domain]  Cd Length: 546  Bit Score: 48.83  E-value: 3.44e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7662234    485 EQHSRLRQENLQLVHRANALEEQLKE--QELRACEMVLEETRRQKEllcKMEREKSIEIENLQTRLQQLDEENSELRSCT 562
Cdd:pfam07888 350 EGQSQWAQERETLRQSAEADKDRIQKlsAELLKLEEWLQEERSQRE---KLEVELGIEKDCNRVQLSENRRELSELRSAL 426
                          90       100       110
                  ....*....|....*....|....*....|....*
gi 7662234    563 PCLKANIERLEEEKQKLLDEIESLTLRLSEEQENK 597
Cdd:pfam07888 427 RVLQKEKEQLQEEKQELLDYIRVLELRLDKEADEK 461
Cast pfam10174
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ...
477-684 4.62e-06

RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.


Pssm-ID: 255805 [Multi-domain]  Cd Length: 774  Bit Score: 48.85  E-value: 4.62e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7662234    477 EKDTA-ATGEQHSRLRQENLQLVHRANALEEQLKEQELRACEMVLEETRRQKEllcKMER------EKSIEIENLQTRLQ 549
Cdd:pfam10174 235 EKDTKiKEFEKMLEKAENEIYRLQSRCDTSEADRNRLDKEVEAERSALAAMKA---KCDRaaqelsRKKTELLGLQTELE 311
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7662234    550 QLDEENSELRSCTPCLKANIERLEEEKQKLLDEIESLTLRLseeqENKRRMGDRLSHERHQFQRDKEATQELIEDLRKQL 629
Cdd:pfam10174 312 TLANQDSDMRQHLDKLKEDLTRAEQEKAILQTEVDALRYEL----ERKHNTLTKKTASLQAAQEEKATYAGEIEDMRDRY 387
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 7662234    630 EhlqllKLEAEQRRGRSSSMGLQEYHSRaRESELEQEVRRLK--QDNRNLKEQNEEL 684
Cdd:pfam10174 388 E-----KTERKLRVLQKKIENLQETFRR-KERRLKEEKERLRslQTDTNTDTALEKL 438
Spc7 smart00787
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ...
493-636 4.89e-06

Spc7 kinetochore protein; This domain is found in cell division proteins which are required for kinetochore-spindle association.


Pssm-ID: 197874 [Multi-domain]  Cd Length: 312  Bit Score: 47.70  E-value: 4.89e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7662234     493 ENLQLVHRANAL----EEQLKE--QELRACEMVLEETRRQ-KELLCKMEREKSIEIENLQTRLQQLDEENSELRSctpcl 565
Cdd:smart00787 151 ENLEGLKEDYKLlmkeLELLNSikPKLRDRKDALEEELRQlKQLEDELEDCDPTELDRAKEKLKKLLQEIMIKVK----- 225
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 7662234     566 kaNIERLEEEKQKLLDEIESLTLRLSEEQenkrrmgDRLSHERHQFQRDKEATQELIEDLRKQLEHLQLLK 636
Cdd:smart00787 226 --KLEELEEELQELESKIEDLTNKKSELN-------TEIAEAEKKLEQCRGFTFKEIEKLKEQLKLLQSLT 287
RAD50_homologue_ceRAD50 TIGR00606
rad50; All proteins in this family for which functions are known are involvedin recombination, ...
485-673 5.48e-06

rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).


Pssm-ID: 129694 [Multi-domain]  Cd Length: 1311  Bit Score: 48.50  E-value: 5.48e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7662234     485 EQHSRLRQENLQLVHRANALEEQLKEQELRACEMVLEETRRQKELLC--KMEREKSIEIENLQTRLQQLDEENSELRSCT 562
Cdd:TIGR00606  189 ETLRQVRQTQGQKVQEHQMELKYLKQYKEKACEIRDQITSKEAQLESsrEIVKSYENELDPLKNRLKEIEHNLSKIMKLD 268
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7662234     563 PCLKAnIERLEEEKQKLLDEIESLTLR--------LSEEQENKRRMGDRLSHERHQFQRDkeatqelIEDLRKQLEHLQL 634
Cdd:TIGR00606  269 NEIKA-LKSRKKQMEKDNSELELKMEKvfqgtdeqLNDLYHNHQRTVREKERELVDCQRE-------LEKLNKERRLLNQ 340
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|
gi 7662234     635 LKLEAEQRRGRSS-SMGLQEYHSRARESELEQEVRRLKQD 673
Cdd:TIGR00606  341 EKTELLVEQGRLQlQADRHQEHIRARDSLIQSLATRLELD 380
Trichoplein pfam13868
tumor suppressor, Mitostatin; Trichoplein or mitostatin, was first defined as a ...
472-683 5.69e-06

tumor suppressor, Mitostatin; Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs).


Pssm-ID: 258135 [Multi-domain]  Cd Length: 350  Bit Score: 47.60  E-value: 5.69e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7662234    472 RVLELEKDTAATGEQHSRLRQENLQLVHRAnALEEQLKEQELRAcemVLEETRRQKELLCKMEREKSIEIENLQTRLQQL 551
Cdd:pfam13868  45 EMMEEERLKALAEEEERERKRKEERREGRA-VLQEQIEEREKRR---QEEYEERLQEREQMDEIVERIQEEDEAEAQEKR 120
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7662234    552 DEENSELRSCTPCLKANIERLEEEKQKLLDEIESLTLRLSEEQENKRRMgdrlsheRHQFQRDKEATQELIEDLRKQLEH 631
Cdd:pfam13868 121 EKQKRLREEIDEFNEERIEWKEEEKEREREEEEKILEYQREKAEREEER-------EAERRERREEKEREVARLRAQQEE 193
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 7662234    632 LQLLKLEAEQRRGRSssmgLQEYHSRARESELEQEVRRLKQDNRNLKEQNEE 683
Cdd:pfam13868 194 AEDEREELDELRADL----YQEEYERKERQKEKEEAEKRRRQKQELQRAREE 241
SbcC COG0419
ATPase involved in DNA repair [DNA replication, recombination, and repair]
469-636 6.41e-06

ATPase involved in DNA repair [DNA replication, recombination, and repair]


Pssm-ID: 223496 [Multi-domain]  Cd Length: 908  Bit Score: 48.22  E-value: 6.41e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7662234  469 LERRVLELEKDTAATGEQHSRLRQENLQLVHRANALEEQLKEQELRACEMVLEETRRQKELLCKMEREKSIEIENLQTRL 548
Cdd:COG0419 591 LRERLKELKKKLKELEERLSQLEELLQSLELSEAENELEEAEEELESELEKLNLQAELEELLQAALEELEEKVEELEAEI 670
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7662234  549 QQLDEENSELRSctpclkanIERLEEEKQKLLDEIESLTLRLSEEQENKRRMGDRLSHERHQfQRDKEATQELIEDLRKQ 628
Cdd:COG0419 671 RRELQRIENEEQ--------LEEKLEELEQLEEELEQLREELEELLKKLGEIEQLIEELESR-KAELEELKKELEKLEKA 741

                ....*...
gi 7662234  629 LEHLQLLK 636
Cdd:COG0419 742 LELLEELR 749
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
3-223 6.62e-06

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 48.06  E-value: 6.62e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7662234     3 SAPPASPPGSEPPGPDPEPGGPDGPGAAQLAPGPAELRLGAPVGGPDPQSPGLDEPAPGAAADGGARWSAGPAPGLEGGP 82
Cdd:PRK07764 591 APGAAGGEGPPAPASSGPPEEAARPAAPAAPAAPAAPAPAGAAAAPAEASAAPAPGVAAPEHHPKHVAVPDASDGGDGWP 670
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7662234    83 RDPGPSAPPPRSGPRGQLASPDAPGPGPRSEAPLPeldplfSWTEEPEecgPASCPESAPfRLQGSSSSHRARGEVDVFS 162
Cdd:PRK07764 671 AKAGGAAPAAPPPAPAPAAPAAPAGAAPAQPAPAP------AATPPAG---QADDPAAQP-PQAAQGASAPSPAADDPVP 740
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 7662234   163 PFPAPTAGELALEQGPGSPPQPSDLSQTHPLPSEPVGSQEDGPRLRAvfDALDGDGDGFVR 223
Cdd:PRK07764 741 LPPEPDDPPDPAGAPAQPPPPPAPAPAAAPAAAPPPSPPSEEEEMAE--DDAPSMDDEDRR 799
conserved_hypothetical_protein TIGR02680
TIGR02680 family protein; Members of this protein family belong to a conserved gene four-gene ...
470-710 7.10e-06

TIGR02680 family protein; Members of this protein family belong to a conserved gene four-gene neighborhood found sporadically in a phylogenetically broad range of bacteria: Nocardia farcinica, Symbiobacterium thermophilum, and Streptomyces avermitilis (Actinobacteria), Geobacillus kaustophilus (Firmicutes), Azoarcus sp. EbN1 and Ralstonia solanacearum (Betaproteobacteria). Proteins in this family average over 1400 amino acids in length. [Hypothetical proteins, Conserved]


Pssm-ID: 274256 [Multi-domain]  Cd Length: 1353  Bit Score: 48.26  E-value: 7.10e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7662234     470 ERRVLELEKDTAATGEQHSRLRQENLQLVHRANALEEQLK----EQELRACEMVLEETRRQKEL----LCKMEREKSIEI 541
Cdd:TIGR02680  741 LRRIAELDARLAAVDDELAELARELRALGARQRALADELAgapsDRSLRAAHRRAAEAERQAESaereLARAARKAAAAA 820
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7662234     542 ENLQTRLQQLDEENSELRsctpcLKANIERLEEEKQKLLDEIESL-TLRlseeqenKRRMGDRLSHERHQFQRDKEATQE 620
Cdd:TIGR02680  821 AAWKQARRELERDAADLD-----LPTDPDALEAVGLALKRFGDHLhTLE-------VAVRELRHAATRAAEQRARAARAE 888
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7662234     621 LieDLRKQLEHLQLLKLEAEQRRGR----SSSMGLQEYHSRARESELEQEVRRLKQDNRNLKEQNEELNGQIITLSiQGA 696
Cdd:TIGR02680  889 S--DAREAAEDAAEARAEAEEASLRlrtlEESVGAMVDEIRARLAETRAALASGGRELPRLAEALATAEEARGRAE-EKR 965
                          250
                   ....*....|....
gi 7662234     697 KSLFSTAFSESLAA 710
Cdd:TIGR02680  966 AEADATLDERAEAR 979
DUF4515 pfam14988
Domain of unknown function (DUF4515); This family of proteins is found in bacteria and ...
470-586 7.55e-06

Domain of unknown function (DUF4515); This family of proteins is found in bacteria and eukaryotes. Proteins in this family are typically between 198 and 469 amino acids in length. There are two completely conserved L residues that may be functionally important.


Pssm-ID: 259125 [Multi-domain]  Cd Length: 206  Bit Score: 46.24  E-value: 7.55e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7662234    470 ERRVLELEKDTAATGEQHSRLRQE-NLQLVHRANALEEQLKEQELR-ACEMVLEETRRQKELLCKM------EREKSIEI 541
Cdd:pfam14988  84 EREIQTLEEELEKTQAETAEKLREaHLQFLKEKAHLEKQLSELDILsLGKRATKELNMKAQALKLAakqalsEFTRSIKR 163
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 7662234    542 EN--LQTRLQQLDEEnselrscTPCLKANIERLEEEKQKLLDEIESL 586
Cdd:pfam14988 164 ENqeLRKELLQLIQE-------TQKLEAIKSKLEEQKQLLKEEQWYL 203
conserved_hypothetical_protein TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
509-736 7.90e-06

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: 48.09  E-value: 7.90e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7662234    509 KEQELRACEMVLEETRRQKELLckmerekSIEIENLQTRLQQLDEENSElrsctpcLKANIERLEEEKQKLLDEIESLtl 588
Cdd:TIGR04523 122 LEVELNKLEKQKKENKKNIDKF-------LTEIKKKEKELEKLNNKYND-------LKKQKEELENELNLLEKEKLNI-- 185
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7662234    589 rlseeqenkrrmgdrlsherhqfqrdkeatQELIEDLRKQLEHLQLLKLEaeqrrgrsssmgLQEYHSRAResELEQEVR 668
Cdd:TIGR04523 186 ------------------------------QKNIDKIKNKLLKLELLLSN------------LKKKIQKNK--SLESQIS 221
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 7662234    669 RLKQDNRNLKEQNEELNGQIitlsiqgakslfstafsESLAAEISSVsRDELMEAIQKQEEINFRLQD 736
Cdd:TIGR04523 222 ELKKQNNQLKDNIEKKQQEI-----------------NEKTTEISNT-QTQLNQLKDEQNKIKKQLSE 271
PRK02224 PRK02224
chromosome segregation protein; Provisional
442-684 8.32e-06

chromosome segregation protein; Provisional


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 48.11  E-value: 8.32e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7662234   442 LTMEALEDPSPELMEGPEEDIADKV-VFLERRVLELEKDTAATGEQHSRLRQENLQLVHRANALEEQLKE-----QELRA 515
Cdd:PRK02224 176 LGVERVLSDQRGSLDQLKAQIEEKEeKDLHERLNGLESELAELDEEIERYEEQREQARETRDEADEVLEEheerrEELET 255
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7662234   516 CEMVLEETRRQKELlCKMEREK-SIEIENLQTRLQQLDEENSELRSCTPCLKANIERLEEEKQKLLD------------- 581
Cdd:PRK02224 256 LEAEIEDLRETIAE-TEREREElAEEVRDLRERLEELEEERDDLLAEAGLDDADAEAVEARREELEDrdeelrdrleecr 334
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7662234   582 --------EIESLT---LRLSEEQENKRRMGDRLSHERHQFQRDKEATQELIEDLRKQLEHLQLLKLEAEQRRGRSSSM- 649
Cdd:PRK02224 335 vaaqahneEAESLRedaDDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFl 414
                        250       260       270
                 ....*....|....*....|....*....|....*.
gi 7662234   650 -GLQEYHSRARESELEQEVRRlkQDNRNLKEQNEEL 684
Cdd:PRK02224 415 eELREERDELREREAELEATL--RTARERVEEAEAL 448
DUF3584 pfam12128
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ...
481-692 9.23e-06

Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.


Pssm-ID: 256862 [Multi-domain]  Cd Length: 1198  Bit Score: 47.76  E-value: 9.23e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7662234     481 AATGEQHSRLRQENLQLVHRanaleeqlkeQELRACEMVLEETRRQKEL-LCKMEREKSIEIENLQTRLQQLDEENSELR 559
Cdd:pfam12128  647 ARTALKQARLDLQRLQNEQQ----------SLKDKLELAIAERKQQAETqLRQLDAQLKQLLEQQQAFLEALKDDFRELR 716
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7662234     560 sctpclkanIERLEEEKQKLLDEIESLTlRLSEEQENKRRmgdrlSHERHQFQRDKEATQEL---------IEDLRKQLE 630
Cdd:pfam12128  717 ---------TERLAKWQVVEGELDNQLA-QLSAAIEAART-----QAKARLKELKKQYDRELasldvdpntVKELKRQIE 781
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 7662234     631 HLQLLKLEAEQRRGRsssmgLQEYHSRARES-----ELEQEVRRLKQDNRNLKEQNEELNGQIITLS 692
Cdd:pfam12128  782 ELETTIERIAVRRPE-----VREYRAFMQETwlhrdSLREERPNLAIQLRELESSAEELQQELTRLI 843
Nuclease_SbcCD_subunit_C TIGR00618
exonuclease SbcC; All proteins in this family for which functions are known are part of an ...
469-684 9.47e-06

exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]


Pssm-ID: 129705 [Multi-domain]  Cd Length: 1042  Bit Score: 47.66  E-value: 9.47e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7662234     469 LERRVLELEKdTAATGEQHSRLRQENLQLVHRANALEEQLKE----QELRACEMVLEETRRQKELLCKMEREKSIEIENl 544
Cdd:TIGR00618  417 SAFRDLQGQL-AHAKKQQELQQRYAELCAAAITCTAQCEKLEkihlQESAQSLKEREQQLQTKEQIHLQETRKKAVVLA- 494
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7662234     545 qtRLQQLDEENSELRSCT-------------PCLKANIERLEEEKQKLLDEIESLTLRLSEEQENKRRMGDRLSHERHQF 611
Cdd:TIGR00618  495 --RLLELQEEPCPLCGSCihpnparqdidnpGPLTRRMQRGEQTYAQLETSEEDVYHQLTSERKQRASLKEQMQEIQQSF 572
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 7662234     612 QRDKEATQELIEDLRKQLEHLQ-LLKLEAEQRRGRSSSMGLQEYHSRARESELEQEVRRLKQDNRNLKEQNEEL 684
Cdd:TIGR00618  573 SILTQCDNRSKEDIPNLQNITVrLQDLTEKLSEAEDMLACEQHALLRKLQPEQDLQDVRLHLQQCSQELALKLT 646
SMC_N pfam02463
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...
500-738 1.13e-05

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


Pssm-ID: 251311 [Multi-domain]  Cd Length: 1162  Bit Score: 47.66  E-value: 1.13e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7662234     500 RANALEEQLKEQE-LRACEMVLEETRRQKELLcKMEREKSIEIENLQTRLQQLDEENSELRSctpcLKANIERLEEEKQK 578
Cdd:pfam02463  172 KKERLKKLIEETEnLAELIIDLEELKLQELKL-KEQAKKALEYYQLKEKLELEEENLLYLDY----LKLNEERIDLLQEL 246
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7662234     579 LLDEIESLTLRLSEEQENKrrmgdRLSHERHQFQRDKEATQELIEDLRKQLE-HLQLLKLEAEQRRGRSSSMGLQEYHSR 657
Cdd:pfam02463  247 LRDEQEEIESSKQELEKEE-----EILAQVLKENKEEEKEKKLQEEELKLLAkEEEELKSELLKLERRKVDDEEKLKESE 321
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7662234     658 ARESELEQEVRRLKQDNRNLKEQNEELNGQIITLSIQGAKSL------------FSTAFSESLAAEISSVSRDELMEAIQ 725
Cdd:pfam02463  322 KELKKLEKELKKEKEEIEELEKELKELEIKREAEEEEEEQLEklqekleqleeeLLAKKKLESERLSSAAKLKEEELELK 401
                          250
                   ....*....|...
gi 7662234     726 KQEEINFRLQDYI 738
Cdd:pfam02463  402 NEEEKEAKLLLEL 414
DUF3584 pfam12128
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ...
540-741 1.17e-05

Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.


Pssm-ID: 256862 [Multi-domain]  Cd Length: 1198  Bit Score: 47.38  E-value: 1.17e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7662234     540 EIENLQTRLQQLDEENSELRSCTPCLKANIERLEEEKQKLLDEIESLTLRLseeqenkRRMGDRLSHERHQFQRDKEATQ 619
Cdd:pfam12128  247 EIEKLQEDFEQLLSLELRLQHLHGELVADEERLAEEQEERQEAKNRLRQQL-------RTLEDQLKEARDELNQELSAAN 319
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7662234     620 ELIEDLRKQLEHLQ------------LLKLEAEQRRGRSSSMGLQEYHSRARES---ELEQEVRRLKQ--DNRNLKEQnE 682
Cdd:pfam12128  320 AKLAADRSELELLEdqkgafedadieQLQADLDQLPSIRSELEEVEARLDALTGkhqDVQRKYERLKQkiKEQLERDL-E 398
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 7662234     683 ELNGQiiTLSIQGAKSLFSTAFSESLAAeISSVSRDELMEAIqkqEEINFRLQDYIDRI 741
Cdd:pfam12128  399 KNNER--LAAIREEKDRQKAAIEEDLQA-LESQLRQQLEAGK---LEFNEEEYELELRL 451
Macoilin pfam09726
Transmembrane protein; This entry is a highly conserved protein present in eukaryotes.
504-688 1.50e-05

Transmembrane protein; This entry is a highly conserved protein present in eukaryotes.


Pssm-ID: 255512 [Multi-domain]  Cd Length: 680  Bit Score: 46.84  E-value: 1.50e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7662234    504 LEEQLK--EQELRACEMVLEETRRQKELLCKMEReksieieNLQTRLQQLDEENSELRSctpclkaNIERLEEEKQKLLD 581
Cdd:pfam09726 411 LEQDIKklQAELQQARQNESELRNQISLLTSLER-------SLKSDLGQLKKENDMLQT-------KLNSMVSAKQKDKQ 476
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7662234    582 EIESLTLRLSEEQENkRRMGDRLSHERHQFQRDKEATQEliedlrkqlehlQLLKLEAEQRRGRSSSMglqeyhsRARES 661
Cdd:pfam09726 477 SMQSMEKRLKSEADS-RVNAEKQLAEEKKRKKEEEETAA------------RAAAQAAASREECAESL-------KQAKQ 536
                         170       180
                  ....*....|....*....|....*..
gi 7662234    662 ELEQEVRRLKQDNRNLKEQNEELNGQI 688
Cdd:pfam09726 537 DLEMEIKKLEHDLKLKEEECRMLEKEA 563
GAS pfam13851
Growth-arrest specific micro-tubule binding; This family is the highly conserved central ...
566-693 1.68e-05

Growth-arrest specific micro-tubule binding; This family is the highly conserved central region of a number of metazoan proteins referred to as growth-arrest proteins. In mouse, Gas8 is predominantly a testicular protein, whose expression is developmentally regulated during puberty and spermatogenesis. In humans, it is absent in infertile males who lack the ability to generate gametes. The localisation of Gas8 in the motility apparatus of post-meiotic gametocytes and mature spermatozoa, together with the detection of Gas8 also in cilia at the apical surfaces of epithelial cells lining the pulmonary bronchi and Fallopian tubes suggests that the Gas8 protein may have a role in the functioning of motile cellular appendages. Gas8 is a microtubule-binding protein localized to regions of dynein regulation in mammalian cells.


Pssm-ID: 258123 [Multi-domain]  Cd Length: 201  Bit Score: 44.91  E-value: 1.68e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7662234    566 KANIERLEEEKQKLLDEIESLTLRLSEEQENKRRMGDRLSHERHQFQRDKEATQELIEDLRKQLEHLQLLKLEAEQRRGR 645
Cdd:pfam13851  36 IAEMKKNEEHNEKLMAEISQENKRLTEPLKKAEEEVEELRKKLKDYEKDKQSLKNLKARLKELEKELKNLKWESEVLEQR 115
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 7662234    646 SSSM-------------GLQEYHSRA--RESELEQevrRLKQDNRNLKEQNEELNGQIITLSI 693
Cdd:pfam13851 116 FEKVererdelydkfeaAIQDVQQKTglKNLLLEQ---KLEALNEELEKKEAQLNEVLAAANL 175
Cast pfam10174
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ...
424-688 1.77e-05

RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.


Pssm-ID: 255805 [Multi-domain]  Cd Length: 774  Bit Score: 46.92  E-value: 1.77e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7662234    424 TKRLSSKKVARYLHQSGALTMEALEDPSPELMEgpEEDIADKVVFLERRVLELEKDTAAT----------------GEQH 487
Cdd:pfam10174 412 ERRLKEEKERLRSLQTDTNTDTALEKLEKALAE--KERIIERLKEQRDRDERYEQEEFETykkefedlkeevqnlqLKLS 489
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7662234    488 SRLRQENLQLVHRANALEEQLKEQ-ELRACEMVLEETRRQKELLCKmEREKSIEIENLQTRLQQLDEENSELRSCTPCLK 566
Cdd:pfam10174 490 ERELQLELLKEEVSKLASNQLKQRsDLERAHIELEKIREKHEKLEK-ELKRLRANPESADRGSAVDAGTSRSRADSAGAR 568
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7662234    567 ANIERLEEEKQKLLDEiesltlRLSEEQENKRRMGDRLSHERHQFQRDKEATQELIEDLRKQLE----HLQLLKLEAEQR 642
Cdd:pfam10174 569 NEVDRLLDRLEKAEQE------RDDTEMEAGRLAKELEKAQRHLTKQQEKTEATRIEFERKSAElleeAERLEKSEAEEE 642
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*.
gi 7662234    643 RGRSSSMglQEYHSRARESELEQEVRRLKQDNRNLKEQNEELNGQI 688
Cdd:pfam10174 643 TLRQSTQ--IGHAQAAAHNHIEHHVQKLESDLKQLRAEREQLVAQL 686
IncA pfam04156
IncA protein; Chlamydia trachomatis is an obligate intracellular bacterium that develops ...
513-641 1.94e-05

IncA protein; Chlamydia trachomatis is an obligate intracellular bacterium that develops within a parasitophorous vacuole termed an inclusion. The inclusion is non-fusogenic with lysosomes but intercepts lipids from a host cell exocytic pathway. Initiation of chlamydial development is concurrent with modification of the inclusion membrane by a set of C. trachomatis-encoded proteins collectively designated Incs. One of these Incs, IncA, is functionally associated with the homotypic fusion of inclusions. This family probably includes members of the wider Inc family rather than just IncA.


Pssm-ID: 252417 [Multi-domain]  Cd Length: 186  Bit Score: 44.76  E-value: 1.94e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7662234    513 LRACEMVLEETRRQKELLCKMEREKSIeIENLQTRLQQLDEENSELRSCTPCLKANIERLEEEKQKLLDEIESLTlrlSE 592
Cdd:pfam04156  61 LLKAPVQSVRPQKLEELQGELSELKQQ-LSELQEELEDLEERIAELESELEDLKEDLQLLRELLKSLEERLESLE---ES 136
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 7662234    593 EQENKRRMGDRLSHERHQFQRDKEATQELIEDLRKQLEHLQLLKLEAEQ 641
Cdd:pfam04156 137 IKELAKELRELRQDLREEVEELREELERLQENLQRLQEAIQELQSLLEQ 185
CAGE1 pfam15066
Cancer-associated gene protein 1 family; CAGE-1 is a family of proteins overexpressed in tumor ...
492-672 2.31e-05

Cancer-associated gene protein 1 family; CAGE-1 is a family of proteins overexpressed in tumor tissues compared with surrounding tissues. CAGE-1 gene showed testis-specific expression among normal tissues and displayed wide expression in a variety of cancer cell lines and cancer tissues. CAGE-1 is predominantly expressed during post-meiotic stages. It localizes to the acrosomal matrix and acrosomal granule showing it to be a component of the acrosome of mammalian spermatids and spermatozoa.


Pssm-ID: 259203 [Multi-domain]  Cd Length: 527  Bit Score: 46.15  E-value: 2.31e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7662234    492 QENLQLVHRANALEEQLKEQELRACEMVL---EETRRQKELLCKMEREKSIEIENLQTRLQQLDEENSELRSCTPCLKAN 568
Cdd:pfam15066 291 QENSLMPDREQSLESLQPLEEDMALNEVLqklKHTNKKQELQIQDLQGSNLYLERRVEELQMKTTKQQVFVDIINKLKVN 370
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7662234    569 IERLEEEKQKLLDEIESLTLRLSEEQENKRRMGDRLSHERhqfqRDKEATQELIEDLRKQLEHLQLLKLEAEQRRGRSSS 648
Cdd:pfam15066 371 VEELIEDKYRVILEKNDTNKTLQNLQEVLAHTQKHLQESK----NDKETLQLQLKKIKGNYVRLQERYMTEMQQKNKSVS 446
                         170       180
                  ....*....|....*....|....
gi 7662234    649 MGLQEYHSRareSELEQEVRRLKQ 672
Cdd:pfam15066 447 QCLEMDKTL---SKKEEEVERLQQ 467
PRK12323 PRK12323
DNA polymerase III subunits gamma and tau; Provisional
2-213 2.32e-05

DNA polymerase III subunits gamma and tau; Provisional


Pssm-ID: 237057 [Multi-domain]  Cd Length: 700  Bit Score: 46.41  E-value: 2.32e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7662234     2 ASAPPASPPGSEPPGPDPEPGGPDGPGAAQLAPGPAELRLGAPVGGPDPQSPGLdEPAPGAAADGGARWSAGPAPGLEGG 81
Cdd:PRK12323 377 AAAAPVAQPAPAAAAPAAAAPAPAAPPAAPAAAPAAAAAARAVAAAPARRSPAP-EALAAARQASARGPGGAPAPAPAPA 455
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7662234    82 PRdPGPSAPPPRSGPRGqlaSPDAPGPGPRSEAPL----PELDPLFSWTEEPEECGPASCPESAPFRLQGSSSSHRARGE 157
Cdd:PRK12323 456 AA-PAAAARPAAAGPRP---VAAAAAAAPARAAPAaapaPADDDPPPWEELPPEFASPAPAQPDAAPAGWVAESIPDPAT 531
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 7662234   158 VD