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Conserved domains on  [gi|1608194202|ref|NP_001356285|]
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inner centromere protein isoform 1 [Mus musculus]

Protein Classification

INCENP_N and INCENP_ARK-bind domain-containing protein( domain architecture ID 10573525)

protein containing domains INCENP_N, GBP_C, and INCENP_ARK-bind

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
INCENP_ARK-bind pfam03941
Inner centromere protein, ARK binding region; This region of the inner centromere protein has ...
 795-849 6.13e-17

Inner centromere protein, ARK binding region; This region of the inner centromere protein has been found to be necessary and sufficient for binding to aurora-related kinase. This interaction has been implicated in the coordination of chromosome segregation with cell division in yeast.


:

Pssm-ID: 461100 [Multi-domain]  Cd Length: 53  Bit Score: 75.31  E-value: 6.13e-17
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1608194202 795 NSDDSTDDESHPRKPIPSWAKGTQLSQAIVHQYyhPPNILELFGSILPLDLEDIF 849
Cdd:pfam03941   1 NSDDEDDDEDEPRKPVPSWAQSPNLRQALIRQE--PIDPDEIFGPIPPLNLEEIF 53
INCENP_N pfam12178
Chromosome passenger complex (CPC) protein INCENP N terminal; This domain family is found in ...
 6-41 2.18e-13

Chromosome passenger complex (CPC) protein INCENP N terminal; This domain family is found in eukaryotes, and is approximately 40 amino acids in length. INCENP is a regulatory protein in the chromosome passenger complex. It is involved in regulation of the catalytic protein Aurora B. It performs this function in association with two other proteins - Survivin and Borealin. These proteins form a tight three-helical bundle. The N terminal domain is the domain involved in formation of this three helical bundle.


:

Pssm-ID: 463484 [Multi-domain]  Cd Length: 36  Bit Score: 64.64  E-value: 2.18e-13
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 1608194202   6 PGPICLLDLCDQKLLDFVCNVDNKDFMWLKEIEEEA 41
Cdd:pfam12178   1 SGPASLLEVCDQKLSEFLCEIDNKHLVWLEEIEEEA 36
PTZ00121 super family cl31754
MAEBL; Provisional
 513-656 3.47e-10

MAEBL; Provisional


The actual alignment was detected with superfamily member PTZ00121:

Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 64.39  E-value: 3.47e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608194202  513 ERQRLESLRRKEEAEQRRRQKVEEDKRRRLEEVKLKREErLRKVLQARERVEQMK--EEKKKQIEQKFAQIDEKTEKAKE 590
Cdd:PTZ00121  1573 EEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEE-AKKAEEAKIKAEELKkaEEEKKKVEQLKKKEAEEKKKAEE 1651

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1608194202  591 ERLAEKAKKKATAKKMEEVEARRKQEEEAR------RLRWLQQEEEERRHQEMLQRKKEEEQERRKAAEARR 656
Cdd:PTZ00121  1652 LKKAEEENKIKAAEEAKKAEEDKKKAEEAKkaeedeKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKK 1723
 
Name Accession Description Interval E-value
INCENP_ARK-bind pfam03941
Inner centromere protein, ARK binding region; This region of the inner centromere protein has ...
 795-849 6.13e-17

Inner centromere protein, ARK binding region; This region of the inner centromere protein has been found to be necessary and sufficient for binding to aurora-related kinase. This interaction has been implicated in the coordination of chromosome segregation with cell division in yeast.


Pssm-ID: 461100 [Multi-domain]  Cd Length: 53  Bit Score: 75.31  E-value: 6.13e-17
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1608194202 795 NSDDSTDDESHPRKPIPSWAKGTQLSQAIVHQYyhPPNILELFGSILPLDLEDIF 849
Cdd:pfam03941   1 NSDDEDDDEDEPRKPVPSWAQSPNLRQALIRQE--PIDPDEIFGPIPPLNLEEIF 53
INCENP_N pfam12178
Chromosome passenger complex (CPC) protein INCENP N terminal; This domain family is found in ...
 6-41 2.18e-13

Chromosome passenger complex (CPC) protein INCENP N terminal; This domain family is found in eukaryotes, and is approximately 40 amino acids in length. INCENP is a regulatory protein in the chromosome passenger complex. It is involved in regulation of the catalytic protein Aurora B. It performs this function in association with two other proteins - Survivin and Borealin. These proteins form a tight three-helical bundle. The N terminal domain is the domain involved in formation of this three helical bundle.


Pssm-ID: 463484 [Multi-domain]  Cd Length: 36  Bit Score: 64.64  E-value: 2.18e-13
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 1608194202   6 PGPICLLDLCDQKLLDFVCNVDNKDFMWLKEIEEEA 41
Cdd:pfam12178   1 SGPASLLEVCDQKLSEFLCEIDNKHLVWLEEIEEEA 36
PTZ00121 PTZ00121
MAEBL; Provisional
 513-656 3.47e-10

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 64.39  E-value: 3.47e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608194202  513 ERQRLESLRRKEEAEQRRRQKVEEDKRRRLEEVKLKREErLRKVLQARERVEQMK--EEKKKQIEQKFAQIDEKTEKAKE 590
Cdd:PTZ00121  1573 EEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEE-AKKAEEAKIKAEELKkaEEEKKKVEQLKKKEAEEKKKAEE 1651

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1608194202  591 ERLAEKAKKKATAKKMEEVEARRKQEEEAR------RLRWLQQEEEERRHQEMLQRKKEEEQERRKAAEARR 656
Cdd:PTZ00121  1652 LKKAEEENKIKAAEEAKKAEEDKKKAEEAKkaeedeKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKK 1723
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 510-744 3.60e-09

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 60.72  E-value: 3.60e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608194202 510 VEKERQRLESLRRKEEAEQRRRQKVEEDKRRRLEEVKLKREERLRKVLQARERVEQMKEEKKKQIEQKfAQIDEKTEKAK 589
Cdd:COG1196   244 LEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERR-RELEERLEELE 322

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608194202 590 EERLAEKAKKKATAKKMEEVEARRKQEEEARRLRwLQQEEEERRHQEMLQRKKEEEQERRKAAEARRLAEQREQERRREQ 669
Cdd:COG1196   323 EELAELEEELEELEEELEELEEELEEAEEELEEA-EAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQ 401

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1608194202 670 ERREQERREQERREQERKEQERREQEQERLRAKREMQEREKALRLQKERLQKELEEKKRKEEQQRLAEQQLQEEQ 744
Cdd:COG1196   402 LEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLE 476
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
 506-656 4.79e-08

Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.


Pssm-ID: 375164 [Multi-domain]  Cd Length: 722  Bit Score: 57.06  E-value: 4.79e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608194202 506 KCSFVEKERQR--------LESLRR-KEEAEQRRRQKVEEDKRRRLEEVKLKREERLRKVlqarERVEQMKEEKKKQieq 576
Cdd:pfam17380 403 KVKILEEERQRkiqqqkveMEQIRAeQEEARQREVRRLEEERAREMERVRLEEQERQQQV----ERLRQQEEERKRK--- 475

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608194202 577 kfaqideKTEKAKEERLAEKAKKKATAKKMEEVEARRKQEEEARRLRWLQQEEEERRhqemlQRKKEEEQERRKAAEARR 656
Cdd:pfam17380 476 -------KLELEKEKRDRKRAEEQRRKILEKELEERKQAMIEEERKRKLLEKEMEER-----QKAIYEEERRREAEEERR 543
tolA_full TIGR02794
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ...
 510-658 4.46e-05

TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]


Pssm-ID: 274303 [Multi-domain]  Cd Length: 346  Bit Score: 46.76  E-value: 4.46e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608194202 510 VEKERQRLESLRRKEEAEQR--RRQKVEEDKRRRLEEVKLKR-EERLRKVLQARErveqmKEEKKKQIEQKFAQIDEKTE 586
Cdd:TIGR02794  52 ANRIQQQKKPAAKKEQERQKklEQQAEEAEKQRAAEQARQKElEQRAAAEKAAKQ-----AEQAAKQAEEKQKQAEEAKA 126

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1608194202 587 KAKEERlaekaKKKatakkmEEVEARRKQEEEARRLRWLQqeeeerrhqemlQRKKEEEQERRKAAEARRLA 658
Cdd:TIGR02794 127 KQAAEA-----KAK------AEAEAERKAKEEAAKQAEEE------------AKAKAAAEAKKKAEEAKKKA 175
GBP_C cd16269
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal ...
 519-623 1.26e-04

Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal domain. Guanylate-binding proteins (GBPs) are synthesized after activation of the cell by interferons. The biochemical properties of GBPs are clearly different from those of Ras-like and heterotrimeric GTP-binding proteins. They bind guanine nucleotides with low affinity (micromolar range), are stable in their absence, and have a high turnover GTPase. In addition to binding GDP/GTP, they have the unique ability to bind GMP with equal affinity and hydrolyze GTP not only to GDP, but also to GMP. This C-terminal domain has been shown to mediate inhibition of endothelial cell proliferation by inflammatory cytokines.


Pssm-ID: 293879 [Multi-domain]  Cd Length: 291  Bit Score: 44.88  E-value: 1.26e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608194202 519 SLRRKEEAEQRRRQKVEEDKRRRLEEvklkREERLRKVLQARERveqMKEEKKKQIEQKFAQIDEKTEKAKEERLAEKAK 598
Cdd:cd16269   194 TEKEKEIEAERAKAEAAEQERKLLEE----QQRELEQKLEDQER---SYEEHLRQLKEKMEEERENLLKEQERALESKLK 266

                          90       100
                  ....*....|....*....|....*
gi 1608194202 599 KKATAKKMEEVEARRKQEEEARRLR 623
Cdd:cd16269   267 EQEALLEEGFKEQAELLQEEIRSLK 291
 
Name Accession Description Interval E-value
INCENP_ARK-bind pfam03941
Inner centromere protein, ARK binding region; This region of the inner centromere protein has ...
 795-849 6.13e-17

Inner centromere protein, ARK binding region; This region of the inner centromere protein has been found to be necessary and sufficient for binding to aurora-related kinase. This interaction has been implicated in the coordination of chromosome segregation with cell division in yeast.


Pssm-ID: 461100 [Multi-domain]  Cd Length: 53  Bit Score: 75.31  E-value: 6.13e-17
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1608194202 795 NSDDSTDDESHPRKPIPSWAKGTQLSQAIVHQYyhPPNILELFGSILPLDLEDIF 849
Cdd:pfam03941   1 NSDDEDDDEDEPRKPVPSWAQSPNLRQALIRQE--PIDPDEIFGPIPPLNLEEIF 53
INCENP_N pfam12178
Chromosome passenger complex (CPC) protein INCENP N terminal; This domain family is found in ...
 6-41 2.18e-13

Chromosome passenger complex (CPC) protein INCENP N terminal; This domain family is found in eukaryotes, and is approximately 40 amino acids in length. INCENP is a regulatory protein in the chromosome passenger complex. It is involved in regulation of the catalytic protein Aurora B. It performs this function in association with two other proteins - Survivin and Borealin. These proteins form a tight three-helical bundle. The N terminal domain is the domain involved in formation of this three helical bundle.


Pssm-ID: 463484 [Multi-domain]  Cd Length: 36  Bit Score: 64.64  E-value: 2.18e-13
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 1608194202   6 PGPICLLDLCDQKLLDFVCNVDNKDFMWLKEIEEEA 41
Cdd:pfam12178   1 SGPASLLEVCDQKLSEFLCEIDNKHLVWLEEIEEEA 36
PTZ00121 PTZ00121
MAEBL; Provisional
 513-656 3.47e-10

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 64.39  E-value: 3.47e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608194202  513 ERQRLESLRRKEEAEQRRRQKVEEDKRRRLEEVKLKREErLRKVLQARERVEQMK--EEKKKQIEQKFAQIDEKTEKAKE 590
Cdd:PTZ00121  1573 EEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEE-AKKAEEAKIKAEELKkaEEEKKKVEQLKKKEAEEKKKAEE 1651

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1608194202  591 ERLAEKAKKKATAKKMEEVEARRKQEEEAR------RLRWLQQEEEERRHQEMLQRKKEEEQERRKAAEARR 656
Cdd:PTZ00121  1652 LKKAEEENKIKAAEEAKKAEEDKKKAEEAKkaeedeKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKK 1723
PTZ00121 PTZ00121
MAEBL; Provisional
 509-656 4.96e-10

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 63.62  E-value: 4.96e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608194202  509 FVEKERQRLESLRRKEEAEQRRRQ-KVEEDKRRRLEEVKLKREERLRKVLQARERVEQMK-----EEKKKQIEQKFAQID 582
Cdd:PTZ00121  1601 YEEEKKMKAEEAKKAEEAKIKAEElKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKikaaeEAKKAEEDKKKAEEA 1680

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1608194202  583 EKTEKAKEERLAEKAKKKATAKKMEEVeaRRKQEEEARRLRWLQQEEEERRHQEMlQRKKEEEQERRKAAEARR 656
Cdd:PTZ00121  1681 KKAEEDEKKAAEALKKEAEEAKKAEEL--KKKEAEEKKKAEELKKAEEENKIKAE-EAKKEAEEDKKKAEEAKK 1751
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 510-744 3.60e-09

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 60.72  E-value: 3.60e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608194202 510 VEKERQRLESLRRKEEAEQRRRQKVEEDKRRRLEEVKLKREERLRKVLQARERVEQMKEEKKKQIEQKfAQIDEKTEKAK 589
Cdd:COG1196   244 LEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERR-RELEERLEELE 322

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608194202 590 EERLAEKAKKKATAKKMEEVEARRKQEEEARRLRwLQQEEEERRHQEMLQRKKEEEQERRKAAEARRLAEQREQERRREQ 669
Cdd:COG1196   323 EELAELEEELEELEEELEELEEELEEAEEELEEA-EAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQ 401

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1608194202 670 ERREQERREQERREQERKEQERREQEQERLRAKREMQEREKALRLQKERLQKELEEKKRKEEQQRLAEQQLQEEQ 744
Cdd:COG1196   402 LEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLE 476
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 510-744 3.16e-08

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 57.64  E-value: 3.16e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608194202 510 VEKERQRLESLRRKEEAEQRRRQKVEEDKrRRLEEVKLKREERLRKVLQARERVEQMKEEKKKQIEQKFAQIDEKTEKAK 589
Cdd:COG1196   269 LEELRLELEELELELEEAQAEEYELLAEL-ARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELE 347

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608194202 590 --EERLAEKAKKKATAKKMEEVEARRKQEEEARRLRWLQQEEEERRHQEMLQRKKEEEQERRKAAEARRLAEQREQERRR 667
Cdd:COG1196   348 eaEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELE 427

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1608194202 668 EQERREQERREQERREQERKEQERREQEQERLRAKREMQEREKALRLQKERLQKELEEKKRKEEQQRLAEQQLQEEQ 744
Cdd:COG1196   428 EALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYE 504
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
 506-656 4.79e-08

Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.


Pssm-ID: 375164 [Multi-domain]  Cd Length: 722  Bit Score: 57.06  E-value: 4.79e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608194202 506 KCSFVEKERQR--------LESLRR-KEEAEQRRRQKVEEDKRRRLEEVKLKREERLRKVlqarERVEQMKEEKKKQieq 576
Cdd:pfam17380 403 KVKILEEERQRkiqqqkveMEQIRAeQEEARQREVRRLEEERAREMERVRLEEQERQQQV----ERLRQQEEERKRK--- 475

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608194202 577 kfaqideKTEKAKEERLAEKAKKKATAKKMEEVEARRKQEEEARRLRWLQQEEEERRhqemlQRKKEEEQERRKAAEARR 656
Cdd:pfam17380 476 -------KLELEKEKRDRKRAEEQRRKILEKELEERKQAMIEEERKRKLLEKEMEER-----QKAIYEEERRREAEEERR 543
PTZ00121 PTZ00121
MAEBL; Provisional
 511-717 6.62e-08

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 56.69  E-value: 6.62e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608194202  511 EKERQRLESLRRKEE----------AEQRRR----QKVEEDKR----RRLEEVK----LKREERLRKVLQARERVEQMKE 568
Cdd:PTZ00121  1493 EEAKKKADEAKKAAEakkkadeakkAEEAKKadeaKKAEEAKKadeaKKAEEKKkadeLKKAEELKKAEEKKKAEEAKKA 1572

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608194202  569 EKKKQIEQKFAQIDEKTEKAKEE---RLAEKAKKKATAKKMEEVEAR------RKQEEEARRLRWLQQEEEERRHQEMLQ 639
Cdd:PTZ00121  1573 EEDKNMALRKAEEAKKAEEARIEevmKLYEEEKKMKAEEAKKAEEAKikaeelKKAEEEKKKVEQLKKKEAEEKKKAEEL 1652

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1608194202  640 RKKEEEQERRKAAEARRlaeqrEQERRREQERREQERREQERREQERKEQERREQEQERLRaKREMQEREKALRLQKE 717
Cdd:PTZ00121  1653 KKAEEENKIKAAEEAKK-----AEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELK-KKEAEEKKKAEELKKA 1724
PTZ00121 PTZ00121
MAEBL; Provisional
 511-739 1.13e-07

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 55.92  E-value: 1.13e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608194202  511 EKERQRLESLRRKEEAEQRRRQKVEEDKR-----RRLEEVK----LKREERLRKVLQARERVEQMKEEKKKQIEQKFAQI 581
Cdd:PTZ00121  1506 AEAKKKADEAKKAEEAKKADEAKKAEEAKkadeaKKAEEKKkadeLKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEE 1585

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608194202  582 DEKTEKAKEE---RLAEKAKKKATAKKMEEVEAR------RKQEEEARRLRWLQQEEEERRHQEMLQRKKEEEQERRKAA 652
Cdd:PTZ00121  1586 AKKAEEARIEevmKLYEEEKKMKAEEAKKAEEAKikaeelKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAE 1665

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608194202  653 EARRLAEQREQERRREQERREQERREQERREQERKEQERREQEQERLRAKREMQEREKALRLQK---ERLQKELEEKKRK 729
Cdd:PTZ00121  1666 EAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKikaEEAKKEAEEDKKK 1745

                          250
                   ....*....|
gi 1608194202  730 EEQQRLAEQQ 739
Cdd:PTZ00121  1746 AEEAKKDEEE 1755
PTZ00121 PTZ00121
MAEBL; Provisional
 511-744 2.70e-07

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 54.76  E-value: 2.70e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608194202  511 EKERQRLESLRRKEEAEQRR---RQKVEEDKRRRlEEVKlKREERLRKVLQARERVEQMK--EEKKKQIEQKfAQIDEKT 585
Cdd:PTZ00121  1374 EEAKKKADAAKKKAEEKKKAdeaKKKAEEDKKKA-DELK-KAAAAKKKADEAKKKAEEKKkaDEAKKKAEEA-KKADEAK 1450

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608194202  586 EKAKEERLAEKAKKKATAKKMEEvEARRKQeEEARRLRWLQQEEEERRHQEMLQRKKEEEQ----ERRKAAEARRLAEQR 661
Cdd:PTZ00121  1451 KKAEEAKKAEEAKKKAEEAKKAD-EAKKKA-EEAKKADEAKKKAEEAKKKADEAKKAAEAKkkadEAKKAEEAKKADEAK 1528

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608194202  662 EQERRREQERREQERREQERREQERKEQERREQEQERLRAKREMQEREKALRLQKERLQKELEEKKRKEEQQRLAEQQLQ 741
Cdd:PTZ00121  1529 KAEEAKKADEAKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMK 1608


                   ...
gi 1608194202  742 EEQ 744
Cdd:PTZ00121  1609 AEE 1611
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 511-744 3.22e-07

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 54.17  E-value: 3.22e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608194202 511 EKERQrLESLRRkeEAEQ-RRRQKVEEDKRRRLEEVKLKREERLRKVLQARERVEQMKEEKKKQIEQKFAQIDEKTEKAK 589
Cdd:COG1196   197 ELERQ-LEPLER--QAEKaERYRELKEELKELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELR 273

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608194202 590 EERLAEKAKKKATAKKMEEVEAR-------------RKQEEEARRLRWLQQEEEERRHQEMLQRKKEEEQERRKAAEARR 656
Cdd:COG1196   274 LELEELELELEEAQAEEYELLAElarleqdiarleeRRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEEL 353

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608194202 657 LAEQREQERRREQERREQERREQERREQERKEQERREQEQERLRAKREMQEREKALRLQKERLQKELEEKKRKEEQQRLA 736
Cdd:COG1196   354 EEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAEL 433


                  ....*...
gi 1608194202 737 EQQLQEEQ 744
Cdd:COG1196   434 EEEEEEEE 441
PTZ00121 PTZ00121
MAEBL; Provisional
 511-654 5.83e-07

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 53.61  E-value: 5.83e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608194202  511 EKERQRLESLRRKEEAEQRRRQKV---EEDKRRRLEEVKLKREERLRKVLQAR--ERVEQMKEEKKKQIEQKFAQIDEKT 585
Cdd:PTZ00121  1629 EEEKKKVEQLKKKEAEEKKKAEELkkaEEENKIKAAEEAKKAEEDKKKAEEAKkaEEDEKKAAEALKKEAEEAKKAEELK 1708

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1608194202  586 EKAKEERLAEKAKKKATAKKMEEVEARRKQEEEARRlRWLQQEEEERRHQEMLQRKKEEE---QERRKAAEA 654
Cdd:PTZ00121  1709 KKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKK-KAEEAKKDEEEKKKIAHLKKEEEkkaEEIRKEKEA 1779
PTZ00121 PTZ00121
MAEBL; Provisional
 512-744 1.77e-06

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 52.07  E-value: 1.77e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608194202  512 KERQRLESLRRKEEAEQRRRQKVEEDKRRRLEEVKLKREERLRKVLQARERVEQMK---EEKKKQIEQKFAQIDEKTEKA 588
Cdd:PTZ00121  1287 EEKKKADEAKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKKADAAKKKAEEAKkaaEAAKAEAEAAADEAEAAEEKA 1366

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608194202  589 KEERLAEKAKKKATAKKMEEVEARRKQEEEARRLRwlQQEEEERRHQEMLQRKKEEEQERRKAAEARRLAEQREQERRRE 668
Cdd:PTZ00121  1367 EAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAE--EDKKKADELKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEAK 1444

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1608194202  669 QERREQERREQERREQERKEQERREQEQERLRAKREMQEREKALRLQKERLQKELEEKKRKEEQQRLAEQQLQEEQ 744
Cdd:PTZ00121  1445 KADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEE 1520
PTZ00121 PTZ00121
MAEBL; Provisional
 511-656 2.02e-06

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 52.07  E-value: 2.02e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608194202  511 EKERQRLESLRRKEE---AEQRRR----QKVEEDKR----RRLEEVK----LKREERLRKVLQARERVEQMKEEKKKQIE 575
Cdd:PTZ00121  1118 EEAKKKAEDARKAEEarkAEDARKaeeaRKAEDAKRveiaRKAEDARkaeeARKAEDAKKAEAARKAEEVRKAEELRKAE 1197

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608194202  576 QkfAQIDEKTEKAKEERLAEKAKKKATAKKMEEV---EARRKQEEEARRLRWLQQEEEERRHQEMLQRKKEEEQERRKAA 652
Cdd:PTZ00121  1198 D--ARKAEAARKAEEERKAEEARKAEDAKKAEAVkkaEEAKKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAE 1275


                   ....
gi 1608194202  653 EARR 656
Cdd:PTZ00121  1276 EARK 1279
PTZ00121 PTZ00121
MAEBL; Provisional
 512-717 3.82e-06

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 50.91  E-value: 3.82e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608194202  512 KERQRLESLRRKEEAEQRRRQKVEEDKRRRLEEVKLKREERLRKVLQARE--RVEQMK--EEKKKQIEQKFAQIDEKTEK 587
Cdd:PTZ00121  1227 EAVKKAEEAKKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEarKADELKkaEEKKKADEAKKAEEKKKADE 1306

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608194202  588 AK---EERLAEKAKKKATAKKMEEVEARRKQEEEARRLRWLQQEEEERRHQEMLQRKKEEEQERRKAAEARRLAEQREQE 664
Cdd:PTZ00121  1307 AKkkaEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKK 1386

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1608194202  665 RRREQERREQERREQERREQERKEQERREQEQERLRAKREMQEREKALRLQKE 717
Cdd:PTZ00121  1387 AEEKKKADEAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKKKADEAKKK 1439
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
 511-718 6.46e-06

Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.


Pssm-ID: 375164 [Multi-domain]  Cd Length: 722  Bit Score: 50.12  E-value: 6.46e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608194202 511 EKERQRLESLRRKEEAEQRRRQK--VEEDKRRRLEEVKLKRE---ERLRKVLQARERVEQMKEEKKKQIEQKFAQIDEKT 585
Cdd:pfam17380 347 ERELERIRQEERKRELERIRQEEiaMEISRMRELERLQMERQqknERVRQELEAARKVKILEEERQRKIQQQKVEMEQIR 426

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608194202 586 EKAKEERlaekakkkatakkmeEVEARRKQEEEARRLrwlqqeeeerrhqemlQRKKEEEQERRKAAEARRLAEQREQER 665
Cdd:pfam17380 427 AEQEEAR---------------QREVRRLEEERAREM----------------ERVRLEEQERQQQVERLRQQEEERKRK 475

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608194202 666 RREQERREQERREQERREQERKEQERREQEQERLRAKR-------EMQEREKALRLQKER 718
Cdd:pfam17380 476 KLELEKEKRDRKRAEEQRRKILEKELEERKQAMIEEERkrkllekEMEERQKAIYEEERR 535
PRK12704 PRK12704
phosphodiesterase; Provisional
 508-590 9.62e-06

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 49.01  E-value: 9.62e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608194202 508 SFVEKERQRLESLRRKEEAE-----QRRRQKVEEDKRRRLEEVK------LKREERLRKVLQARERVEQMKEEKKKQIEQ 576
Cdd:PRK12704   42 RILEEAKKEAEAIKKEALLEakeeiHKLRNEFEKELRERRNELQklekrlLQKEENLDRKLELLEKREEELEKKEKELEQ 121

                          90
                  ....*....|....
gi 1608194202 577 KFAQIDEKTEKAKE 590
Cdd:PRK12704  122 KQQELEKKEEELEE 135
PTZ00121 PTZ00121
MAEBL; Provisional
 511-656 1.06e-05

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 49.37  E-value: 1.06e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608194202  511 EKERQRLESLRRKEEAEQRRRQKVEEDKrrrlEEVKLKREERLRKVLQARERVEQMK--EEKKKQIEQKFAQIDEKTEKA 588
Cdd:PTZ00121  1339 EEAKKAAEAAKAEAEAAADEAEAAEEKA----EAAEKKKEEAKKKADAAKKKAEEKKkaDEAKKKAEEDKKKADELKKAA 1414

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1608194202  589 KEERLAEKAKKKATAKkmEEVEARRKQEEEARRLRWLQQEEEERRHQEMLQRKKEE----EQERRKAAEARR 656
Cdd:PTZ00121  1415 AAKKKADEAKKKAEEK--KKADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEakkaDEAKKKAEEAKK 1484
PTZ00121 PTZ00121
MAEBL; Provisional
 512-744 1.11e-05

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 49.37  E-value: 1.11e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608194202  512 KERQRLESLRRKEEAEQRRRQKVE--EDKRRRLEEVKLKREERlRKVLQARERVEQMK--EEKKKQIEQKfAQIDEKTEK 587
Cdd:PTZ00121  1388 EEKKKADEAKKKAEEDKKKADELKkaAAAKKKADEAKKKAEEK-KKADEAKKKAEEAKkaDEAKKKAEEA-KKAEEAKKK 1465

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608194202  588 AKEERLAEKAKKKATAKKMEEvEARRKQEEEARRLRWLQQEEEerrhqemlQRKKEEE----QERRKAAEARRLAEQREQ 663
Cdd:PTZ00121  1466 AEEAKKADEAKKKAEEAKKAD-EAKKKAEEAKKKADEAKKAAE--------AKKKADEakkaEEAKKADEAKKAEEAKKA 1536

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608194202  664 ERRREQERREQERREQERREQERKEQERREQEQERLRAKREMQEREKALRLQKERLQKELEEKKRKEEQQRLAEQQLQEE 743
Cdd:PTZ00121  1537 DEAKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAE 1616


                   .
gi 1608194202  744 Q 744
Cdd:PTZ00121  1617 E 1617
PTZ00121 PTZ00121
MAEBL; Provisional
 511-746 1.75e-05

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 48.98  E-value: 1.75e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608194202  511 EKERQRLESLRRKEEAEQRRRQKVEEDKRRRLEEVKLKREERLRKVLQARERVEQMK---EEKKKQIEQKFAQIDEKTEK 587
Cdd:PTZ00121  1447 DEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEAKkaaEAKKKADEAKKAEEAKKADE 1526

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608194202  588 AKEERLAEKAKKKATAKKMEEVEARRKQEE--EARRLRWLQQEEEERRHQEMLQRKKEEEqerRKAAEARRLAEQREQER 665
Cdd:PTZ00121  1527 AKKAEEAKKADEAKKAEEKKKADELKKAEElkKAEEKKKAEEAKKAEEDKNMALRKAEEA---KKAEEARIEEVMKLYEE 1603

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608194202  666 RREQERREQERREQERREQERKEQERREQEQERLRAKREMQEREKALRLQKERLQKELEEKKrkeeqqrlaEQQLQEEQA 745
Cdd:PTZ00121  1604 EKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAE---------EAKKAEEDK 1674


                   .
gi 1608194202  746 K 746
Cdd:PTZ00121  1675 K 1675
tolA PRK09510
cell envelope integrity inner membrane protein TolA; Provisional
 512-658 2.23e-05

cell envelope integrity inner membrane protein TolA; Provisional


Pssm-ID: 236545 [Multi-domain]  Cd Length: 387  Bit Score: 47.88  E-value: 2.23e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608194202 512 KERQRLESLRRKEEaeqrRRQKVEEDKRRRLEEVKLKREERLRKVLQARERveqmKEEKKKQIEQKFAQIDEKTEKAKEE 591
Cdd:PRK09510   66 RQQQQQKSAKRAEE----QRKKKEQQQAEELQQKQAAEQERLKQLEKERLA----AQEQKKQAEEAAKQAALKQKQAEEA 137

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1608194202 592 RlaekakkkatakKMEEVEARRKQEEEARRLRWLQQEEEERRhqemlQRKKEEEQERRKAAEARRLA 658
Cdd:PRK09510  138 A------------AKAAAAAKAKAEAEAKRAAAAAKKAAAEA-----KKKAEAEAAKKAAAEAKKKA 187
PTZ00121 PTZ00121
MAEBL; Provisional
 511-742 2.58e-05

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 48.21  E-value: 2.58e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608194202  511 EKERQRLESLRRKEEAEQRRRqkveEDKRRRLEEVKLKREERlRKVLQARERVEQMK----EEKKKQIEQKFAqiDEKTE 586
Cdd:PTZ00121  1353 EAAADEAEAAEEKAEAAEKKK----EEAKKKADAAKKKAEEK-KKADEAKKKAEEDKkkadELKKAAAAKKKA--DEAKK 1425

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608194202  587 KAKEERlaEKAKKKATAKKMEEVEARRKQEEEARRLRWLQQEEEERRHQEMLQRKKEE----EQERRKAAEARRLAEQRE 662
Cdd:PTZ00121  1426 KAEEKK--KADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEakkaDEAKKKAEEAKKKADEAK 1503

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608194202  663 QERRREQERREQERREQERREQERKEQERREQEQERLRA--KREMQEREKALRLQKERLQKELEEKKRKEEQQRLAEQQL 740
Cdd:PTZ00121  1504 KAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAeeKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKA 1583


                   ..
gi 1608194202  741 QE 742
Cdd:PTZ00121  1584 EE 1585
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
 511-617 3.14e-05

Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.


Pssm-ID: 375164 [Multi-domain]  Cd Length: 722  Bit Score: 47.81  E-value: 3.14e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608194202 511 EKERQRLESLRRK---EEAEQRRRQKVEEDKRRRLEEVKLkrEERLRKVLQARERVEQMKEEKKKQIEQKFAQIDEKTEK 587
Cdd:pfam17380 483 KRDRKRAEEQRRKileKELEERKQAMIEEERKRKLLEKEM--EERQKAIYEEERRREAEEERRKQQEMEERRRIQEQMRK 560

                          90       100       110
                  ....*....|....*....|....*....|
gi 1608194202 588 AKEERLAEKAKKKATAKKMEEVEARRKQEE 617
Cdd:pfam17380 561 ATEERSRLEAMEREREMMRQIVESEKARAE 590
YqiK COG2268
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
517-658 3.41e-05

Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];


Pssm-ID: 441869 [Multi-domain]  Cd Length: 439  Bit Score: 47.17  E-value: 3.41e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608194202 517 LESLRRKEEAEQRRRQKVEEDKRRRLEEVKLK---REERLRKVLQARERVEQMKEEKKKQIEQKFAQIDEKTEKAKEERl 593
Cdd:COG2268   186 LDALGRRKIAEIIRDARIAEAEAERETEIAIAqanREAEEAELEQEREIETARIAEAEAELAKKKAEERREAETARAEA- 264

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1608194202 594 aekakkkatakkmeeVEARRKQEEEARRLRWLQQEEEERRHQEMLQRKKEEEQER------RKAAEARRLA 658
Cdd:COG2268   265 ---------------EAAYEIAEANAEREVQRQLEIAEREREIELQEKEAEREEAeleadvRKPAEAEKQA 320
MAP7 pfam05672
MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is ...
 513-654 3.44e-05

MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is presumably controlled by tissue-specific microtubule-associated proteins (MAPs). The 115-kDa epithelial MAP (E-MAP-115/MAP7) has been identified as a microtubule-stabilising protein predominantly expressed in cell lines of epithelial origin. The binding of this microtubule associated protein is nucleotide independent.


Pssm-ID: 461709 [Multi-domain]  Cd Length: 153  Bit Score: 44.65  E-value: 3.44e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608194202 513 ERQRLesLRRKEEAEQRRRQKVEEDKRRRLEEVKLKREErlrKVLQARERVEQMKEEKKKQIEQkfaQIDEKTEKAKEER 592
Cdd:pfam05672  18 EKRRQ--AREQREREEQERLEKEEEERLRKEELRRRAEE---ERARREEEARRLEEERRREEEE---RQRKAEEEAEERE 89

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1608194202 593 LAEKAKKKATAKKMEEVEARRKQEEEARRLrwlqqeeeerRHQEMLQRKKEEEQERRKAAEA 654
Cdd:pfam05672  90 QREQEEQERLQKQKEEAEAKAREEAERQRQ----------EREKIMQQEEQERLERKKRIEE 141
tolA_full TIGR02794
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ...
 510-658 4.46e-05

TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]


Pssm-ID: 274303 [Multi-domain]  Cd Length: 346  Bit Score: 46.76  E-value: 4.46e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608194202 510 VEKERQRLESLRRKEEAEQR--RRQKVEEDKRRRLEEVKLKR-EERLRKVLQARErveqmKEEKKKQIEQKFAQIDEKTE 586
Cdd:TIGR02794  52 ANRIQQQKKPAAKKEQERQKklEQQAEEAEKQRAAEQARQKElEQRAAAEKAAKQ-----AEQAAKQAEEKQKQAEEAKA 126

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1608194202 587 KAKEERlaekaKKKatakkmEEVEARRKQEEEARRLRWLQqeeeerrhqemlQRKKEEEQERRKAAEARRLA 658
Cdd:TIGR02794 127 KQAAEA-----KAK------AEAEAERKAKEEAAKQAEEE------------AKAKAAAEAKKKAEEAKKKA 175
PTZ00121 PTZ00121
MAEBL; Provisional
 512-656 4.75e-05

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 47.44  E-value: 4.75e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608194202  512 KERQRLESLRRKEEAeqrrrQKVEEDKR----RRLEEVKlKREERLRKVLQARERVEQMKEEKKKQIEQKFAQIDEKTE- 586
Cdd:PTZ00121  1203 EAARKAEEERKAEEA-----RKAEDAKKaeavKKAEEAK-KDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEe 1276

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1608194202  587 --KAKEERLAEKAKKKATAKKMEE---VEARRKQEEEARRLRWLQQEEEERRHQEMLQRKKEEeqERRKAAEARR 656
Cdd:PTZ00121  1277 arKADELKKAEEKKKADEAKKAEEkkkADEAKKKAEEAKKADEAKKKAEEAKKKADAAKKKAE--EAKKAAEAAK 1349
GBP_C cd16269
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal ...
 519-623 1.26e-04

Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal domain. Guanylate-binding proteins (GBPs) are synthesized after activation of the cell by interferons. The biochemical properties of GBPs are clearly different from those of Ras-like and heterotrimeric GTP-binding proteins. They bind guanine nucleotides with low affinity (micromolar range), are stable in their absence, and have a high turnover GTPase. In addition to binding GDP/GTP, they have the unique ability to bind GMP with equal affinity and hydrolyze GTP not only to GDP, but also to GMP. This C-terminal domain has been shown to mediate inhibition of endothelial cell proliferation by inflammatory cytokines.


Pssm-ID: 293879 [Multi-domain]  Cd Length: 291  Bit Score: 44.88  E-value: 1.26e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608194202 519 SLRRKEEAEQRRRQKVEEDKRRRLEEvklkREERLRKVLQARERveqMKEEKKKQIEQKFAQIDEKTEKAKEERLAEKAK 598
Cdd:cd16269   194 TEKEKEIEAERAKAEAAEQERKLLEE----QQRELEQKLEDQER---SYEEHLRQLKEKMEEERENLLKEQERALESKLK 266

                          90       100
                  ....*....|....*....|....*
gi 1608194202 599 KKATAKKMEEVEARRKQEEEARRLR 623
Cdd:cd16269   267 EQEALLEEGFKEQAELLQEEIRSLK 291
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
 511-654 1.27e-04

Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.


Pssm-ID: 375164 [Multi-domain]  Cd Length: 722  Bit Score: 45.88  E-value: 1.27e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608194202 511 EKERQRLESLRRKEEAEqRRRQKVEEDKRRRLEEVKLKR-----EERLRKVLQA--RERVEQMKEEKKKQIEQKFAQIDE 583
Cdd:pfam17380 447 EMERVRLEEQERQQQVE-RLRQQEEERKRKKLELEKEKRdrkraEEQRRKILEKelEERKQAMIEEERKRKLLEKEMEER 525

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1608194202 584 KTEKAKEERLAEKAKKKATAKKMEEveaRRKQEEEARRLRWLQQEEEERRHQEMLQRKKEEEQERRKAAEA 654
Cdd:pfam17380 526 QKAIYEEERRREAEEERRKQQEMEE---RRRIQEQMRKATEERSRLEAMEREREMMRQIVESEKARAEYEA 593
PTZ00121 PTZ00121
MAEBL; Provisional
 510-656 1.69e-04

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 45.52  E-value: 1.69e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608194202  510 VEKERQRLESLRRKEEAEQRRRQKVEEDKRRRLEEVKL---KREERLRKVLQARERVEQMKEEKKKQIEQkfAQIDEKTE 586
Cdd:PTZ00121  1111 AEEARKAEEAKKKAEDARKAEEARKAEDARKAEEARKAedaKRVEIARKAEDARKAEEARKAEDAKKAEA--ARKAEEVR 1188

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608194202  587 KAKEERlaekakkkaTAKKMEEVEARRKQEEEARrlrwlQQEEEERRHQEMLQRKKEEEQERRKAAEARR 656
Cdd:PTZ00121  1189 KAEELR---------KAEDARKAEAARKAEEERK-----AEEARKAEDAKKAEAVKKAEEAKKDAEEAKK 1244
PRK00409 PRK00409
recombination and DNA strand exchange inhibitor protein; Reviewed
 527-621 3.66e-04

recombination and DNA strand exchange inhibitor protein; Reviewed


Pssm-ID: 234750 [Multi-domain]  Cd Length: 782  Bit Score: 44.43  E-value: 3.66e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608194202 527 EQRRRQkveEDKRRRLEEvKLKREERLRKVLQAR-ERVEQMKEEKKKQIEQKFAQIdekTEKAKEErLAEKAKKKATAKK 605
Cdd:PRK00409  527 ELEREL---EQKAEEAEA-LLKEAEKLKEELEEKkEKLQEEEDKLLEEAEKEAQQA---IKEAKKE-ADEIIKELRQLQK 598

                          90
                  ....*....|....*.
gi 1608194202 606 MEEVEARRKQEEEARR 621
Cdd:PRK00409  599 GGYASVKAHELIEARK 614
MRP-S26 pfam14943
Mitochondrial ribosome subunit S26; This family of proteins corresponds to mitochondrial ...
 511-588 3.73e-04

Mitochondrial ribosome subunit S26; This family of proteins corresponds to mitochondrial ribosomal subunit S26 in eukaryotes


Pssm-ID: 464391 [Multi-domain]  Cd Length: 168  Bit Score: 42.23  E-value: 3.73e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608194202 511 EKERQRL------ESLRRKEEAEQRRRQKVEEDKRRRLEEVKLKREERLRKVLQARERVEQMKEEKKKQIEQKfaQIDEK 584
Cdd:pfam14943  70 EEEHRELmawneeWNAEIAKLREERLAKEAEEREEEILERIEEKEEKEEEKKERAEEEVRQEKEESKTFITRE--NLDAA 147


                  ....
gi 1608194202 585 TEKA 588
Cdd:pfam14943 148 IEEA 151
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 511-658 4.83e-04

chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 43.90  E-value: 4.83e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608194202  511 EKERQRLESLRRKEEAEQRRR----------QKVEEDKRRRLEEVKLKREERLRKVLQARERVEQMKEEK---------- 570
Cdd:TIGR02169  332 DKLLAEIEELEREIEEERKRRdklteeyaelKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREInelkreldrl 411

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608194202  571 ---KKQIEQKFAQIDEKTEKAKEERLAEKAKKKATAKKMEEVEARRKQ--------EEEARRLRwlqqeeeerRHQEMLQ 639
Cdd:TIGR02169  412 qeeLQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQlaadlskyEQELYDLK---------EEYDRVE 482

                          170
                   ....*....|....*....
gi 1608194202  640 RKKEEEQERRKAAEARRLA 658
Cdd:TIGR02169  483 KELSKLQRELAEAEAQARA 501
RNase_Y_N pfam12072
RNase Y N-terminal region;
518-616 1.14e-03

RNase Y N-terminal region;


Pssm-ID: 463456 [Multi-domain]  Cd Length: 201  Bit Score: 41.02  E-value: 1.14e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608194202 518 ESLRRKEEAEQRRRQKveEDKRRRLEEVKLKREERLRKVLQARERVEQMKEEKKKQIEQKFAQIDEKTEKAKE------- 590
Cdd:pfam12072  61 EIHKLRAEAERELKER--RNELQRQERRLLQKEETLDRKDESLEKKEESLEKKEKELEAQQQQLEEKEEELEElieeqrq 138

                          90       100
                  ....*....|....*....|....*...
gi 1608194202 591 --ERLAEKAKKKATAKKMEEVEARRKQE 616
Cdd:pfam12072 139 elERISGLTSEEAKEILLDEVEEELRHE 166
ERM_helical pfam20492
Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related ...
 511-623 1.31e-03

Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related proteins, ezrin, radixin and moesin. Ezrin was first identified as a constituent of microvilli, radixin as a barbed, end-capping actin-modulating protein from isolated junctional fractions, and moesin as a heparin binding protein. A tumour suppressor molecule responsible for neurofibromatosis type 2 (NF2) is highly similar to ERM proteins and has been designated merlin (moesin-ezrin-radixin-like protein). ERM molecules contain 3 domains, an N-terminal globular domain, an extended alpha-helical domain and a charged C-terminal domain (pfam00769). Ezrin, radixin and merlin also contain a polyproline linker region between the helical and C-terminal domains. The N-terminal domain is highly conserved and is also found in merlin, band 4.1 proteins and members of the band 4.1 superfamily, designated the FERM domain. ERM proteins crosslink actin filaments with plasma membranes. They co-localize with CD44 at actin filament plasma membrane interaction sites, associating with CD44 via their N-terminal domains and with actin filaments via their C-terminal domains. This is the alpha-helical domain, which is involved in intramolecular masking of protein-protein interaction sites, regulating the activity of this proteins.


Pssm-ID: 466641 [Multi-domain]  Cd Length: 120  Bit Score: 39.52  E-value: 1.31e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608194202 511 EKERQRLE-SLRRKEEAEQRRRQKVE---------EDKRRRLEEVKLKREERLRKVLQARERVEQMKEEKKKQIEQKFAQ 580
Cdd:pfam20492   5 EREKQELEeRLKQYEEETKKAQEELEeseetaeelEEERRQAEEEAERLEQKRQEAEEEKERLEESAEMEAEEKEQLEAE 84

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1608194202 581 IDEKTEKAkeERLaekakkkatakkmeeVEARRKQEEEARRLR 623
Cdd:pfam20492  85 LAEAQEEI--ARL---------------EEEVERKEEEARRLQ 110
rne PRK10811
ribonuclease E; Reviewed
 510-588 1.70e-03

ribonuclease E; Reviewed


Pssm-ID: 236766 [Multi-domain]  Cd Length: 1068  Bit Score: 42.33  E-value: 1.70e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608194202  510 VEKERQRLESLRRKEEAEQRRRQkveEDKRRRLEEVK-LKREERLRKVLQARERVEQ-MKEEKKKQIEQKFAQIDEKTEK 587
Cdd:PRK10811   662 TEKARTQDEQQQAPRRERQRRRN---DEKRQAQQEAKaLNVEEQSVQETEQEERVQQvQPRRKQRQLNQKVRIEQSVAEE 738


                   .
gi 1608194202  588 A 588
Cdd:PRK10811   739 A 739
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 510-657 1.92e-03

chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 41.98  E-value: 1.92e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608194202  510 VEKERQRLESLRRKEEAEQRRRQKVEEDK----RRRLEEVKLKREERLRKVLQARERVEQMKEEKKK---QIEQKFAQID 582
Cdd:TIGR02169  260 ISELEKRLEEIEQLLEELNKKIKDLGEEEqlrvKEKIGELEAEIASLERSIAEKERELEDAEERLAKleaEIDKLLAEIE 339

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1608194202  583 EKTEKAKEERLAEKAKKKATAKKMEEVEA--RRKQEEEARRLRWLQQEEEERRHQEMLQRKKEEEQ--ERRKAAEARRL 657
Cdd:TIGR02169  340 ELEREIEEERKRRDKLTEEYAELKEELEDlrAELEEVDKEFAETRDELKDYREKLEKLKREINELKreLDRLQEELQRL 418
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 508-656 2.05e-03

chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 41.97  E-value: 2.05e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608194202  508 SFVEKERQRLESLRRKEEAEQRRRQKVEEDKRRRLEEVKLKREERLRKVLQARERVEQMKEEKKKQIEQKFAQIDEKTE- 586
Cdd:TIGR02168  736 ARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLl 815

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1608194202  587 ----KAKEERLAEKAKKKATAKKMEEVEARRKQEEEARRLRWLQQEEEERRHQEMLQRKKEEEQERRKAAEARR 656
Cdd:TIGR02168  816 neeaANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEAL 889
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 511-592 2.43e-03

Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];


Pssm-ID: 441187 [Multi-domain]  Cd Length: 236  Bit Score: 40.68  E-value: 2.43e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608194202 511 EKERQRLEslrrKEEAEQRRRQKVEEDKRRRLEEVKLKREERLRKVLQARERVEQMKEEKKKQIEQKFAQIDEKTEKAKE 590
Cdd:COG1579    88 NKEYEALQ----KEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEA 163


                  ..
gi 1608194202 591 ER 592
Cdd:COG1579   164 ER 165
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
 513-658 2.45e-03

Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. 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). The family is in the trichohyalin-plectin-homology domain.


Pssm-ID: 464007 [Multi-domain]  Cd Length: 341  Bit Score: 41.06  E-value: 2.45e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608194202 513 ERQRLESLRRKEEAEQRRRQKVEEDKRRRLEEVKLKREERLRKVLQARERVEQMKEEKKKQIEQKFAQIDEKTEKAKEER 592
Cdd:pfam13868  50 EEERERALEEEEEKEEERKEERKRYRQELEEQIEEREQKRQEEYEEKLQEREQMDEIVERIQEEDQAEAEEKLEKQRQLR 129

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1608194202 593 lAEKAKKKATAKKMEEVEARRKQEEEARRLRWLQQEEEErrhqemlQRKKEEEQERRKAAEARRLA 658
Cdd:pfam13868 130 -EEIDEFNEEQAEWKELEKEEEREEDERILEYLKEKAER-------EEEREAEREEIEEEKEREIA 187
PTZ00121 PTZ00121
MAEBL; Provisional
 496-744 2.53e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 41.67  E-value: 2.53e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608194202  496 KRNTPLRVDPKCSFVEKERQR---LESLRRKEEAEQRRRQKVEEDkrRRLEEVKlKREERLRKVLQARERVEQMK-EEKK 571
Cdd:PTZ00121  1070 EGLKPSYKDFDFDAKEDNRADeatEEAFGKAEEAKKTETGKAEEA--RKAEEAK-KKAEDARKAEEARKAEDARKaEEAR 1146

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608194202  572 KQIEQKFAQIDEKTEKAKE-ERLAEKAKKKATAKKMEEVEARRKQE----EEARRLRWLQQEEEERRHQEMlqRKKEEEq 646
Cdd:PTZ00121  1147 KAEDAKRVEIARKAEDARKaEEARKAEDAKKAEAARKAEEVRKAEElrkaEDARKAEAARKAEEERKAEEA--RKAEDA- 1223

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608194202  647 erRKAAEARRLAEQREQERRREQERREQERREQERREQERKEQERREQEQERLRAKREMQEREKALRLQKERLQKELEEK 726
Cdd:PTZ00121  1224 --KKAEAVKKAEEAKKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKAEEKKKADEAKKAEEK 1301

                          250
                   ....*....|....*...
gi 1608194202  727 KRKEEQQRLAEQQLQEEQ 744
Cdd:PTZ00121  1302 KKADEAKKKAEEAKKADE 1319
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
 511-657 2.54e-03

Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. 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). The family is in the trichohyalin-plectin-homology domain.


Pssm-ID: 464007 [Multi-domain]  Cd Length: 341  Bit Score: 41.06  E-value: 2.54e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608194202 511 EKERQRLESLRRKEEAEQRRRQKVEEDKRRRLEEVKLK-------REERLRKVLQARERVEQ---MKEEKKKQIEQK--F 578
Cdd:pfam13868 172 EAEREEIEEEKEREIARLRAQQEKAQDEKAERDELRAKlyqeeqeRKERQKEREEAEKKARQrqeLQQAREEQIELKerR 251

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1608194202 579 AQIDEKTEKAKEERLAEKAKKKATAKKMEEVEARRKQEEEARRLRWLQQEEEERRHQEMLQRKKEEEQERRKAAEARRL 657
Cdd:pfam13868 252 LAEEAEREEEEFERMLRKQAEDEEIEQEEAEKRRMKRLEHRRELEKQIEEREEQRAAEREEELEEGERLREEEAERRER 330
tolA_full TIGR02794
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ...
 532-658 2.60e-03

TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]


Pssm-ID: 274303 [Multi-domain]  Cd Length: 346  Bit Score: 40.98  E-value: 2.60e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608194202 532 QKVEEDKRRRLEEVKLKREERLRKVlQARERVEQMKEEKKKQiEQKFAQIDEKTEKAKEERLAEKAKKKATAKKMEEVEA 611
Cdd:TIGR02794  47 AVAQQANRIQQQKKPAAKKEQERQK-KLEQQAEEAEKQRAAE-QARQKELEQRAAAEKAAKQAEQAAKQAEEKQKQAEEA 124

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 1608194202 612 RRKQEEEArrlrwlqqeeeerrhqemlQRKKEEEQERRKAAEARRLA 658
Cdd:TIGR02794 125 KAKQAAEA-------------------KAKAEAEAERKAKEEAAKQA 152
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
 520-657 2.77e-03

Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. 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). The family is in the trichohyalin-plectin-homology domain.


Pssm-ID: 464007 [Multi-domain]  Cd Length: 341  Bit Score: 41.06  E-value: 2.77e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608194202 520 LRRKEEAEQRRRQKVEEDKRRRLEEVKLKREERLRKVLQARERVEQMKEEKKKQIEQKFAQIDEKTEKAKEERLAEKAKK 599
Cdd:pfam13868  82 IEEREQKRQEEYEEKLQEREQMDEIVERIQEEDQAEAEEKLEKQRQLREEIDEFNEEQAEWKELEKEEEREEDERILEYL 161

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1608194202 600 KATAKKMEEVEARRKQEEEARRLrwlqqeeeerrHQEMLQRKKEEEQERRKAAEARRL 657
Cdd:pfam13868 162 KEKAEREEEREAEREEIEEEKER-----------EIARLRAQQEKAQDEKAERDELRA 208
YqiK COG2268
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
511-623 2.89e-03

Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];


Pssm-ID: 441869 [Multi-domain]  Cd Length: 439  Bit Score: 41.01  E-value: 2.89e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608194202 511 EKERQRLESLRRKEEAEQRRRQKVEEDKRRRLE-EVKLKREERLRKVLQARERVEQMKEEKKKQIEQKFAQIDEKTEKAK 589
Cdd:COG2268   211 ETEIAIAQANREAEEAELEQEREIETARIAEAEaELAKKKAEERREAETARAEAEAAYEIAEANAEREVQRQLEIAERER 290

                          90       100       110
                  ....*....|....*....|....*....|....
gi 1608194202 590 EERLAEkakkkatakkmEEVEARRKQEEEARRLR 623
Cdd:COG2268   291 EIELQE-----------KEAEREEAELEADVRKP 313
DUF4670 pfam15709
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ...
 504-717 3.65e-03

Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins in this family are typically between 373 and 763 amino acids in length.


Pssm-ID: 464815 [Multi-domain]  Cd Length: 522  Bit Score: 40.71  E-value: 3.65e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608194202 504 DPKCSFVEKERQRLESLR--RKEEAEQRR----RQKVEEDKRRRLEEVKLKREERLRKVLQ--ARERVEQMKEEKKKQIE 575
Cdd:pfam15709 319 DPSKALLEKREQEKASRDrlRAERAEMRRleveRKRREQEEQRRLQQEQLERAEKMREELEleQQRRFEEIRLRKQRLEE 398

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608194202 576 QKFAQIDEKTEKAKEERlaekakkkatakkMEEVEARRKQEEEARRLRwlqqeeeerrhqeMLQRKKEEEQERRKAAEAR 655
Cdd:pfam15709 399 ERQRQEEEERKQRLQLQ-------------AAQERARQQQEEFRRKLQ-------------ELQRKKQQEEAERAEAEKQ 452

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1608194202 656 RLaeqreqeRRREQERREQERREQERREQERKEQERREQEQERlRAKREMQER----EKALRLQKE 717
Cdd:pfam15709 453 RQ-------KELEMQLAEEQKRLMEMAEEERLEYQRQKQEAEE-KARLEAEERrqkeEEAARLALE 510
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
511-658 3.66e-03

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 40.91  E-value: 3.66e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608194202 511 EKERQRLESLRRKEEAEQRRRQKVEEDKRRR---LEEVKLKRE--------ERLRKVLQARERVEQMKEEKKKQIEQKFA 579
Cdd:COG4717    98 EELEEELEELEAELEELREELEKLEKLLQLLplyQELEALEAElaelperlEELEERLEELRELEEELEELEAELAELQE 177

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1608194202 580 QIDEKTEkakEERLAEKAKKKATAKKMEEVEARRKQEEEARRlRWLQQEEEERRHQEMLQRKKEEEQERRKAAEARRLA 658
Cdd:COG4717   178 ELEELLE---QLSLATEEELQDLAEELEELQQRLAELEEELE-EAQEELEELEEELEQLENELEAAALEERLKEARLLL 252
DUF4659 pfam15558
Domain of unknown function (DUF4659); This family of proteins is found in eukaryotes. Proteins ...
 511-658 4.33e-03

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: 464768 [Multi-domain]  Cd Length: 374  Bit Score: 40.41  E-value: 4.33e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608194202 511 EKERQRL--ESLRRKE---EAEQRRRQKVEEDKRRRLEEVKLKREERLRKVLQARERVEQMKEEKKKQIEQKFAQIDEKT 585
Cdd:pfam15558  49 ERERRLLlqQSQEQWQaekEQRKARLGREERRRADRREKQVIEKESRWREQAEDQENQRQEKLERARQEAEQRKQCQEQR 128

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1608194202 586 EKAKEERLAEKAKKKATAKKMEEVEARRKQEEEARRLRWLQQEEEERRHQEMLQRKKEEEQERRKAAEARRLA 658
Cdd:pfam15558 129 LKEKEEELQALREQNSLQLQERLEEACHKRQLKEREEQKKVQENNLSELLNHQARKVLVDCQAKAEELLRRLS 201
PRK12704 PRK12704
phosphodiesterase; Provisional
 524-648 4.67e-03

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 40.53  E-value: 4.67e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608194202 524 EEAEQRRRQKVEEDKRrrleEVKLKREErlrKVLQARERVEQMKEEKKKQIEQKFAQID--EKTEKAKEERLaekakkka 601
Cdd:PRK12704   34 KEAEEEAKRILEEAKK----EAEAIKKE---ALLEAKEEIHKLRNEFEKELRERRNELQklEKRLLQKEENL-------- 98

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 1608194202 602 tAKKMEEVEaRRKQEEEARRLRWLQQEEEERRHQEMLQRKKEEEQER 648
Cdd:PRK12704   99 -DRKLELLE-KREEELEKKEKELEQKQQELEKKEEELEELIEEQLQE 143
AtpF COG0711
FoF1-type ATP synthase, membrane subunit b or b' [Energy production and conversion]; FoF1-type ...
 524-591 4.88e-03

FoF1-type ATP synthase, membrane subunit b or b' [Energy production and conversion]; FoF1-type ATP synthase, membrane subunit b or b' is part of the Pathway/BioSystem: FoF1-type ATP synthase


Pssm-ID: 440475 [Multi-domain]  Cd Length: 152  Bit Score: 38.62  E-value: 4.88e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608194202 524 EEAEQRRR--QKVEEDKRRRLEEVKLKREERLRkvlQARERVEQMKEEKKKQIEqkfAQIDEKTEKAKEE 591
Cdd:COG0711    41 AEAERAKEeaEAALAEYEEKLAEARAEAAEIIA---EARKEAEAIAEEAKAEAE---AEAERIIAQAEAE 104
Borrelia_P83 pfam05262
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins.
 512-623 5.31e-03

Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins.


Pssm-ID: 114011 [Multi-domain]  Cd Length: 489  Bit Score: 40.37  E-value: 5.31e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608194202 512 KERQRLESLRRKEEAEQRRRQKVEE---------------DKRRRLEEVKLKREERLRK--VLQARERVEQMKEEKKKQI 574
Cdd:pfam05262 204 KERESQEDAKRAQQLKEELDKKQIDadkaqqkadfaqdnaDKQRDEVRQKQQEAKNLPKpaDTSSPKEDKQVAENQKREI 283

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1608194202 575 EQKFAQIDEKTE---KAKEERLAEKAKKKATAKKMEEvearrKQEEEARRLR 623
Cdd:pfam05262 284 EKAQIEIKKNDEealKAKDHKAFDLKQESKASEKEAE-----DKELEAQKKR 330
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 502-618 6.15e-03

chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 40.44  E-value: 6.15e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608194202  502 RVDPKCSFVEKERQRLESLRRKEEAEQRRRQKVEEDKRRRLEEVKLKREERLRKVLQARERVEQMKEE------KKKQIE 575
Cdd:TIGR02169  823 RLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKErdeleaQLRELE 902

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|...
gi 1608194202  576 QKFAQIDEKTEKAKEERLAEKAKKKATAKKMEEVEARRKQEEE 618
Cdd:TIGR02169  903 RKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDEE 945
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
 510-651 6.24e-03

Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. 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). The family is in the trichohyalin-plectin-homology domain.


Pssm-ID: 464007 [Multi-domain]  Cd Length: 341  Bit Score: 39.90  E-value: 6.24e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608194202 510 VEKERQRLESLRRKEEAEQRRRQK---------VEEDKRRRLEEVKLKREERlrkvLQARERVEQMKEEKKKQIEQKFaq 580
Cdd:pfam13868  49 MEEERERALEEEEEKEEERKEERKryrqeleeqIEEREQKRQEEYEEKLQER----EQMDEIVERIQEEDQAEAEEKL-- 122

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1608194202 581 idEKTEKAKEERLaekaKKKATAKKMEEVEARRKQEEEARRLRWLQQEEEERRHQEMLQRKKEEEQERRKA 651
Cdd:pfam13868 123 --EKQRQLREEID----EFNEEQAEWKELEKEEEREEDERILEYLKEKAEREEEREAEREEIEEEKEREIA 187
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
 511-656 6.24e-03

Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. 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). The family is in the trichohyalin-plectin-homology domain.


Pssm-ID: 464007 [Multi-domain]  Cd Length: 341  Bit Score: 39.90  E-value: 6.24e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608194202 511 EKERQRLEslrrKEEAEQRRRQKVEEDKRRRLEEVKLKREERLRKVLQARERVEQMKEEKKKQIEQKFAQIDEKTEKAKE 590
Cdd:pfam13868  84 EREQKRQE----EYEEKLQEREQMDEIVERIQEEDQAEAEEKLEKQRQLREEIDEFNEEQAEWKELEKEEEREEDERILE 159

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1608194202 591 ERLAEKAKKKATAKKMEEVEARRKQEEEARRLRWLQQEEEERRHQEMLQRKKEEEQE---RRKAAEARR 656
Cdd:pfam13868 160 YLKEKAEREEEREAEREEIEEEKEREIARLRAQQEKAQDEKAERDELRAKLYQEEQErkeRQKEREEAE 228
PRK12704 PRK12704
phosphodiesterase; Provisional
 511-591 6.88e-03

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 40.15  E-value: 6.88e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608194202 511 EKERQRLESLRRKEEAEQRRRQKVEEDKRR----------RLEEVKLKREERLRKVL--------QARERV-EQMKEEKK 571
Cdd:PRK12704   89 KRLLQKEENLDRKLELLEKREEELEKKEKEleqkqqelekKEEELEELIEEQLQELErisgltaeEAKEILlEKVEEEAR 168

                          90       100
                  ....*....|....*....|
gi 1608194202 572 KQIeqkFAQIDEKTEKAKEE 591
Cdd:PRK12704  169 HEA---AVLIKEIEEEAKEE 185
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 508-590 6.90e-03

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


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 39.75  E-value: 6.90e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608194202 508 SFVEKERQRLESLRRKEEAEQRRRQKVEEdKRRRLEEVKLKREERLRKVLQARERVEQMKEEKKKQIEQKFAQIDEKTEK 587
Cdd:COG4942   143 YLAPARREQAEELRADLAELAALRAELEA-ERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQE 221


                  ...
gi 1608194202 588 AKE 590
Cdd:COG4942   222 AEE 224
TolA COG3064
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis];
511-763 8.26e-03

Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 442298 [Multi-domain]  Cd Length: 485  Bit Score: 39.64  E-value: 8.26e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608194202 511 EKERQRLESLRRKEEAEQRRRQKVEEDKRRRLEEVKLKREERLRKVLQARERVEQMKEEKKKQIEQKFAQIDEKTEKAKE 590
Cdd:COG3064     5 LEEKAAEAAAQERLEQAEAEKRAAAEAEQKAKEEAEEERLAELEAKRQAEEEAREAKAEAEQRAAELAAEAAKKLAEAEK 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608194202 591 ERLAEKAKKKAtakkmEEVEARRKQEEEARRLRWLQQEEEERRHQemlQRKKEEEQERRKAAEARRLAEQREQERRREQE 670
Cdd:COG3064    85 AAAEAEKKAAA-----EKAKAAKEAEAAAAAEKAAAAAEKEKAEE---AKRKAEEEAKRKAEEERKAAEAEAAAKAEAEA 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608194202 671 RREQERREQERREQERKEQERREQEQERLRAKREMQEREKALRLQKERLQKELEEKKRKEEQQRLAEQQLQEEQAKKAKE 750
Cdd:COG3064   157 ARAAAAAAAAAAAAAARAAAGAAAALVAAAAAAVEAADTAAAAAAALAAAAAAAAADAALLALAVAARAAAASREAALAA 236

                         250
                  ....*....|...
gi 1608194202 751 VAAARKVLNMTVD 763
Cdd:COG3064   237 VEATEEAALGGAE 249
cdk7 TIGR00570
CDK-activating kinase assembly factor MAT1; All proteins in this family for which functions ...
 514-591 8.50e-03

CDK-activating kinase assembly factor MAT1; All proteins in this family for which functions are known are cyclin dependent protein kinases that are components of TFIIH, a complex that is involved in nucleotide excision repair and transcription initiation. Also known as MAT1 (menage a trois 1). 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: 129661 [Multi-domain]  Cd Length: 309  Bit Score: 39.40  E-value: 8.50e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1608194202 514 RQRLESLRRKEEAEQRRRQKVEEDKRRRLEEVKLKREERLRKVLQARERVEQMkEEKKKQIEQKFAQIDEKTEKAKEE 591
Cdd:TIGR00570 135 KNKEKSTREQEELEEALEFEKEEEEQRRLLLQKEEEEQQMNKRKNKQALLDEL-ETSTLPAAELIAQHKKNSVKLEMQ 211
SMC_N pfam02463
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...
 511-740 8.59e-03

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 metabolism and recombination.


Pssm-ID: 426784 [Multi-domain]  Cd Length: 1161  Bit Score: 39.95  E-value: 8.59e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608194202  511 EKERQRLESLRRKEEAEQRRRQKVEEDKRRRLEEVKLKREERLR----------KVLQARERVEQMKEEKKKQIEQKFAQ 580
Cdd:pfam02463  179 IEETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEeeyllyldylKLNEERIDLLQELLRDEQEEIESSKQ 258

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608194202  581 IDEKTEKAKEERLAEKAKKKATAKKMEEVEARRKQEEEARRLRWLQQEEEERRHQEMLQRKKEEEQERRKAAEARRLAEQ 660
Cdd:pfam02463  259 EIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDEEKLKESEKEKKKAEKELKKEKEEIE 338

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608194202  661 REQERRREQERREQERREQERREQERKEQERREQEQERLRAKREMQEREKALRLQKERLQKELEEKKRKEEQQRLAEQQL 740
Cdd:pfam02463  339 ELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEEELELKSEEEKEAQLLLELARQLE 418
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
510-654 9.20e-03

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 39.75  E-value: 9.20e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1608194202 510 VEKERQRLESLRRKEEAEQRRRQKVEEdKRRRLEEVKLKREErLRKVLQARERVEQMKE--EKKKQIEQKFAQIDEKTEK 587
Cdd:COG4717    73 LKELEEELKEAEEKEEEYAELQEELEE-LEEELEELEAELEE-LREELEKLEKLLQLLPlyQELEALEAELAELPERLEE 150

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1608194202 588 AKEERLAEKAKKKATAKKMEEVEARRKQEEEARRLRWLQQEEEerrhqemLQRKKEEEQERRKAAEA 654
Cdd:COG4717   151 LEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEE-------LQDLAEELEELQQRLAE 210
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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