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Conserved domains on  [gi|1720395138|ref|XP_030106759|]
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leucine zipper putative tumor suppressor 2 isoform X1 [Mus musculus]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Fez1 pfam06818
Fez1; This family represents the eukaryotic Fez1 protein. Fez1 contains a leucine-zipper ...
 441-638 1.55e-89

Fez1; This family represents the eukaryotic Fez1 protein. Fez1 contains a leucine-zipper region with similarity to the DNA-binding domain of the cAMP-responsive activating-transcription factor 5. There is evidence that Fez1 inhibits cancer cell growth through regulation of mitosis, and that its alterations result in abnormal cell growth. Note that some family members contain more than one copy of this region.


:

Pssm-ID: 462015 [Multi-domain]  Cd Length: 198  Bit Score: 277.26  E-value: 1.55e-89
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395138 441 TKWEVCQKSGEISLLKQQLKESQAELVQKGSELVALRVALREARATLRVSEGRARGLQEAARAREQELEACSQELQRYRQ 520
Cdd:pfam06818   1 TKWEVCQKSGEISLLKQQLKDSQAEVTQKLNEIVALRAQLRELRAKLEEKEEQIQELEDSLRSKTLELEVCENELQRKKN 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395138 521 EAERLREKAGHLDAEASGLRDPPVPPATTDPFLLAESDEAKVQRAAAGAGGSLRAQVERLRQELQREQRRGDEQRDSFEG 600
Cdd:pfam06818  81 EAELLREKVGKLEEEVSGLREALSDVSPSGYESVYESDEAKEQRQEEADLGSLRREVERLRAELREERQRRERQASSFEQ 160

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 1720395138 601 ERLAWQAEKEQVIRYQKQLQHNYIQMYRRNRQLEQELQ 638
Cdd:pfam06818 161 ERRTWQEEKEKVIRYQKQLQLNYVQMYRRNQALERELK 198
GAS super family cl25894
Growth-arrest specific micro-tubule binding; This family is the highly conserved central ...
 404-473 6.14e-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 localization 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.


The actual alignment was detected with superfamily member pfam13851:

Pssm-ID: 464001 [Multi-domain]  Cd Length: 200  Bit Score: 44.51  E-value: 6.14e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1720395138 404 RQLQDDFAQLLQEREQLERRCATFEREQRELGPRLEETKWEVCQKSG-EISLLKQQLKESQAELVQKGSEL 473
Cdd:pfam13851  95 KVLEKELKDLKWEHEVLEQRFEKVERERDELYDKFEAAIQDVQQKTGlKNLLLEKKLQALGETLEKKEAQL 165
 
Name Accession Description Interval E-value
Fez1 pfam06818
Fez1; This family represents the eukaryotic Fez1 protein. Fez1 contains a leucine-zipper ...
 441-638 1.55e-89

Fez1; This family represents the eukaryotic Fez1 protein. Fez1 contains a leucine-zipper region with similarity to the DNA-binding domain of the cAMP-responsive activating-transcription factor 5. There is evidence that Fez1 inhibits cancer cell growth through regulation of mitosis, and that its alterations result in abnormal cell growth. Note that some family members contain more than one copy of this region.


Pssm-ID: 462015 [Multi-domain]  Cd Length: 198  Bit Score: 277.26  E-value: 1.55e-89
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395138 441 TKWEVCQKSGEISLLKQQLKESQAELVQKGSELVALRVALREARATLRVSEGRARGLQEAARAREQELEACSQELQRYRQ 520
Cdd:pfam06818   1 TKWEVCQKSGEISLLKQQLKDSQAEVTQKLNEIVALRAQLRELRAKLEEKEEQIQELEDSLRSKTLELEVCENELQRKKN 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395138 521 EAERLREKAGHLDAEASGLRDPPVPPATTDPFLLAESDEAKVQRAAAGAGGSLRAQVERLRQELQREQRRGDEQRDSFEG 600
Cdd:pfam06818  81 EAELLREKVGKLEEEVSGLREALSDVSPSGYESVYESDEAKEQRQEEADLGSLRREVERLRAELREERQRRERQASSFEQ 160

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 1720395138 601 ERLAWQAEKEQVIRYQKQLQHNYIQMYRRNRQLEQELQ 638
Cdd:pfam06818 161 ERRTWQEEKEKVIRYQKQLQLNYVQMYRRNQALERELK 198
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 402-656 4.23e-14

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 76.13  E-value: 4.23e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395138 402 EKRQLQDDFAQLLQEREQLERRCATFEREQRELGPRLEETKWEVCQKSGEISLLKQQLKESQAELVQKGSELVALRVALR 481
Cdd:COG1196   233 KLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRR 312

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395138 482 EARATLRVSEGRARGLQEAARAREQELEACSQELQRYRQEAERLREKAGHLDAEASGLRdppvppATTDPFLLAESDEAK 561
Cdd:COG1196   313 ELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAE------AELAEAEEELEELAE 386

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395138 562 VQRAAAGAGGSLRAQVERLRQELQREQRRgdeqRDSFEGERLAWQAEKEQVIRYQKQLQHNYIQMYRRNRQLEQELQQLS 641
Cdd:COG1196   387 ELLEALRAAAELAAQLEELEEAEEALLER----LERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALL 462

                         250
                  ....*....|....*
gi 1720395138 642 LELEARELADLGLAE 656
Cdd:COG1196   463 ELLAELLEEAALLEA 477
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 330-653 3.09e-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: 70.09  E-value: 3.09e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395138  330 LEGKLRDREAELQQLRDSMDESEATVCQAfgarqrrwpRERGEDCAAQAQQATQRVQRAqqllqlqvfqlqqEKRQlqdd 409
Cdd:TIGR02168  689 LEEKIAELEKALAELRKELEELEEELEQL---------RKELEELSRQISALRKDLARL-------------EAEV---- 742

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395138  410 fAQLLQEREQLERRCATFEREQRELGPRLEETKWEVCQKSGEISLLKQQLKESQAELVQKGSELVALRVALREARATLRV 489
Cdd:TIGR02168  743 -EQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAAN 821

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395138  490 SEGRARGLQEAARAREQELEACSQELQRYRQEAERLREKAGHLDAEASGLRDppvppATTDpfLLAESDEAKVQRAAAGA 569
Cdd:TIGR02168  822 LRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELES-----ELEA--LLNERASLEEALALLRS 894

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395138  570 G-GSLRAQVERLRQELQREQRRGDEQRDSFEGERLAWQAEKEQVIRYQKQLQHNYIQMYRRNRQLEQELQQLSLELEAR- 647
Cdd:TIGR02168  895 ElEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLSEEYSLTLEEAEALENKIEDDEEEARRRl 974

                          330
                   ....*....|.
gi 1720395138  648 -----ELADLG 653
Cdd:TIGR02168  975 krlenKIKELG 985
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
416-652 2.77e-05

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 47.37  E-value: 2.77e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395138 416 EREQLER---RCATFEREQRELGPRLEETKWEVCQKSGEISLLKQQLKESQAELvqkgSELVALRVALREARATLRVSEG 492
Cdd:PRK03918  177 RIERLEKfikRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEV----KELEELKEEIEELEKELESLEG 252

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395138 493 RARGLQEAARARE---QELEACSQELQRYRQEAERLREKAghldAEASGLRDppvppattdpfLLAESDEAKVQraaaga 569
Cdd:PRK03918  253 SKRKLEEKIRELEeriEELKKEIEELEEKVKELKELKEKA----EEYIKLSE-----------FYEEYLDELRE------ 311

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395138 570 ggsLRAQVERLRQELQREQRRGDEQRDsfEGERLAWQAEKEQVIRYQKQLQHNYIQMYRRNRQLEQELQQLSLELEAREL 649
Cdd:PRK03918  312 ---IEKRLSRLEEEINGIEERIKELEE--KEERLEELKKKLKELEKRLEELEERHELYEEAKAKKEELERLKKRLTGLTP 386


                  ...
gi 1720395138 650 ADL 652
Cdd:PRK03918  387 EKL 389
OmpH smart00935
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH ...
 455-524 3.10e-05

Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH among others. Skp (OmpH) has been characterized as a molecular chaperone that interacts with unfolded proteins as they emerge in the periplasm from the Sec translocation machinery.


Pssm-ID: 214922 [Multi-domain]  Cd Length: 140  Bit Score: 44.11  E-value: 3.10e-05
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395138  455 LKQQLKESQAELVQKGSELVALRVALREARATLRvsegrarglQEAARAREQELEACSQELQRYRQEAER 524
Cdd:smart00935  23 LEKEFKKRQAELEKLEKELQKLKEKLQKDAATLS---------EAAREKKEKELQKKVQEFQRKQQKLQQ 83
GAS pfam13851
Growth-arrest specific micro-tubule binding; This family is the highly conserved central ...
 404-473 6.14e-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 localization 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: 464001 [Multi-domain]  Cd Length: 200  Bit Score: 44.51  E-value: 6.14e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1720395138 404 RQLQDDFAQLLQEREQLERRCATFEREQRELGPRLEETKWEVCQKSG-EISLLKQQLKESQAELVQKGSEL 473
Cdd:pfam13851  95 KVLEKELKDLKWEHEVLEQRFEKVERERDELYDKFEAAIQDVQQKTGlKNLLLEKKLQALGETLEKKEAQL 165
 
Name Accession Description Interval E-value
Fez1 pfam06818
Fez1; This family represents the eukaryotic Fez1 protein. Fez1 contains a leucine-zipper ...
 441-638 1.55e-89

Fez1; This family represents the eukaryotic Fez1 protein. Fez1 contains a leucine-zipper region with similarity to the DNA-binding domain of the cAMP-responsive activating-transcription factor 5. There is evidence that Fez1 inhibits cancer cell growth through regulation of mitosis, and that its alterations result in abnormal cell growth. Note that some family members contain more than one copy of this region.


Pssm-ID: 462015 [Multi-domain]  Cd Length: 198  Bit Score: 277.26  E-value: 1.55e-89
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395138 441 TKWEVCQKSGEISLLKQQLKESQAELVQKGSELVALRVALREARATLRVSEGRARGLQEAARAREQELEACSQELQRYRQ 520
Cdd:pfam06818   1 TKWEVCQKSGEISLLKQQLKDSQAEVTQKLNEIVALRAQLRELRAKLEEKEEQIQELEDSLRSKTLELEVCENELQRKKN 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395138 521 EAERLREKAGHLDAEASGLRDPPVPPATTDPFLLAESDEAKVQRAAAGAGGSLRAQVERLRQELQREQRRGDEQRDSFEG 600
Cdd:pfam06818  81 EAELLREKVGKLEEEVSGLREALSDVSPSGYESVYESDEAKEQRQEEADLGSLRREVERLRAELREERQRRERQASSFEQ 160

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 1720395138 601 ERLAWQAEKEQVIRYQKQLQHNYIQMYRRNRQLEQELQ 638
Cdd:pfam06818 161 ERRTWQEEKEKVIRYQKQLQLNYVQMYRRNQALERELK 198
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 402-656 4.23e-14

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 76.13  E-value: 4.23e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395138 402 EKRQLQDDFAQLLQEREQLERRCATFEREQRELGPRLEETKWEVCQKSGEISLLKQQLKESQAELVQKGSELVALRVALR 481
Cdd:COG1196   233 KLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRR 312

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395138 482 EARATLRVSEGRARGLQEAARAREQELEACSQELQRYRQEAERLREKAGHLDAEASGLRdppvppATTDPFLLAESDEAK 561
Cdd:COG1196   313 ELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAE------AELAEAEEELEELAE 386

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395138 562 VQRAAAGAGGSLRAQVERLRQELQREQRRgdeqRDSFEGERLAWQAEKEQVIRYQKQLQHNYIQMYRRNRQLEQELQQLS 641
Cdd:COG1196   387 ELLEALRAAAELAAQLEELEEAEEALLER----LERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALL 462

                         250
                  ....*....|....*
gi 1720395138 642 LELEARELADLGLAE 656
Cdd:COG1196   463 ELLAELLEEAALLEA 477
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 402-655 9.01e-14

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 74.97  E-value: 9.01e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395138 402 EKRQLQDDFAQLLQEREQLERRCATFEREQRELGPRLEETKWevcqksgEISLLKQQLKESQAELVQKGSELVALRVALR 481
Cdd:COG1196   282 ELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEE-------ELAELEEELEELEEELEELEEELEEAEEELE 354

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395138 482 EARATLRVSEGRARGLQEAARAREQELEACSQELQRYRQEAERLREKAGHLDAEASGLRDppvppattdpfLLAESDEAK 561
Cdd:COG1196   355 EAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLE-----------RLERLEEEL 423

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395138 562 VQRAAAGAggSLRAQVERLRQELQREQRRGDEQRDSFEGERLAWQAEKEQVIRYQKQLQhnyiqmyRRNRQLEQELQQLS 641
Cdd:COG1196   424 EELEEALA--ELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALA-------ELLEELAEAAARLL 494

                         250
                  ....*....|....
gi 1720395138 642 LELEARELADLGLA 655
Cdd:COG1196   495 LLLEAEADYEGFLE 508
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 329-658 1.56e-12

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 71.12  E-value: 1.56e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395138 329 VLEGKLRDREAELQQLRDSMDESEATVcQAFGARQRrwprergedcaaqaqqatqRVQRAQQLLQLQVFQLQQEKRQLQD 408
Cdd:COG1196   257 ELEAELAELEAELEELRLELEELELEL-EEAQAEEY-------------------ELLAELARLEQDIARLEERRRELEE 316

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395138 409 DFAQLLQEREQLERRCATFEREQRELGPRLEETKWEVCQKSGEISLLKQQLKESQAELVQKGSELVALRVALREARATLR 488
Cdd:COG1196   317 RLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAA 396

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395138 489 VSEGRARGLQEAARAREQELEACSQELQRYRQEAERLREKaghldaeasglrdppvppattdpfLLAESDEAKVQRAAAG 568
Cdd:COG1196   397 ELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEE------------------------EEEEEEALEEAAEEEA 452

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395138 569 AGGSLRAQVERLRQELQREQRRGDEQRDSFEGERlawqAEKEQVIRYQKQLQHNYIQMYRRNRQLEQELQQLSLELEARE 648
Cdd:COG1196   453 ELEEEEEALLELLAELLEEAALLEAALAELLEEL----AEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAV 528

                         330
                  ....*....|
gi 1720395138 649 LADLGLAESA 658
Cdd:COG1196   529 LIGVEAAYEA 538
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 330-653 3.09e-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: 70.09  E-value: 3.09e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395138  330 LEGKLRDREAELQQLRDSMDESEATVCQAfgarqrrwpRERGEDCAAQAQQATQRVQRAqqllqlqvfqlqqEKRQlqdd 409
Cdd:TIGR02168  689 LEEKIAELEKALAELRKELEELEEELEQL---------RKELEELSRQISALRKDLARL-------------EAEV---- 742

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395138  410 fAQLLQEREQLERRCATFEREQRELGPRLEETKWEVCQKSGEISLLKQQLKESQAELVQKGSELVALRVALREARATLRV 489
Cdd:TIGR02168  743 -EQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAAN 821

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395138  490 SEGRARGLQEAARAREQELEACSQELQRYRQEAERLREKAGHLDAEASGLRDppvppATTDpfLLAESDEAKVQRAAAGA 569
Cdd:TIGR02168  822 LRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELES-----ELEA--LLNERASLEEALALLRS 894

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395138  570 G-GSLRAQVERLRQELQREQRRGDEQRDSFEGERLAWQAEKEQVIRYQKQLQHNYIQMYRRNRQLEQELQQLSLELEAR- 647
Cdd:TIGR02168  895 ElEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLSEEYSLTLEEAEALENKIEDDEEEARRRl 974

                          330
                   ....*....|.
gi 1720395138  648 -----ELADLG 653
Cdd:TIGR02168  975 krlenKIKELG 985
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 402-648 7.99e-11

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: 65.46  E-value: 7.99e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395138  402 EKRQLQDDFAQLLQEREQLERRCATFEREQRELGPRLEETKWEVCQKSGEISLLKQQLKESQAELVQKGSELVALRVALR 481
Cdd:TIGR02168  233 RLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLA 312

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395138  482 EARATL-RVSEGRARGLQ-------EAARAREQ------ELEACSQELQRYRQEAERLREKAGHLDAEASGLRDppvppa 547
Cdd:TIGR02168  313 NLERQLeELEAQLEELESkldelaeELAELEEKleelkeELESLEAELEELEAELEELESRLEELEEQLETLRS------ 386

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395138  548 ttdpfllaESDEAKVQRAAAGAG-GSLRAQVERLRQELQREQRRGDEQRDSF-EGERLAWQAEKEQVIRYQKQLQHNYIQ 625
Cdd:TIGR02168  387 --------KVAQLELQIASLNNEiERLEARLERLEDRRERLQQEIEELLKKLeEAELKELQAELEELEEELEELQEELER 458

                          250       260
                   ....*....|....*....|...
gi 1720395138  626 MYRRNRQLEQELQQLSLELEARE 648
Cdd:TIGR02168  459 LEEALEELREELEEAEQALDAAE 481
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
457-646 3.82e-10

Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 63.40  E-value: 3.82e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395138  457 QQLKESQAELVQKGSELVALR--VALREARATLRVSEGRARGLQEAARA--REQELEACSQELQRYRQEAERLREKAGHL 532
Cdd:COG4913    235 DDLERAHEALEDAREQIELLEpiRELAERYAAARERLAELEYLRAALRLwfAQRRLELLEAELEELRAELARLEAELERL 314

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395138  533 DAEASGLRdppvppattdpfllAESDEAKVQRAAAGAG--GSLRAQVERLRQELQREQRRGDEQ--------------RD 596
Cdd:COG4913    315 EARLDALR--------------EELDELEAQIRGNGGDrlEQLEREIERLERELEERERRRARLeallaalglplpasAE 380

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|
gi 1720395138  597 SFEGERLAWQAEKEQVIRYQKQLQHNYIQMYRRNRQLEQELQQLSLELEA 646
Cdd:COG4913    381 EFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIAS 430
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 402-641 4.27e-10

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: 63.15  E-value: 4.27e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395138  402 EKRQLQDDFAQLLQEREQLERRCATFEREQRELGPRLEETKWEVCQKSGEISLLKQQLKESQAELVQKGSEL-------V 474
Cdd:TIGR02168  275 EVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLeelkeelE 354

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395138  475 ALRVALREARATLRVSEGRARGLQEAARAR-------EQELEACSQELQRYRQEAERLREKAGHLDAEASGLRDPpvppa 547
Cdd:TIGR02168  355 SLEAELEELEAELEELESRLEELEEQLETLrskvaqlELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKK----- 429

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395138  548 ttdpflLAESDEAKVQRAAAGaggsLRAQVERLRQELQREQRRGDEQRDSFEGERLAWQAEKEQVIRYQ------KQLQH 621
Cdd:TIGR02168  430 ------LEEAELKELQAELEE----LEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQarldslERLQE 499

                          250       260
                   ....*....|....*....|
gi 1720395138  622 NYIQMYRRNRQLEQELQQLS 641
Cdd:TIGR02168  500 NLEGFSEGVKALLKNQSGLS 519
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 402-648 4.33e-10

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: 63.16  E-value: 4.33e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395138  402 EKRQLQDdfaQLLQEREQLER----RCATFEREQRELGPRLEETKWEVCQKSGEISLLKQQLKESQAELVQKGSELVALR 477
Cdd:TIGR02169  195 EKRQQLE---RLRREREKAERyqalLKEKREYEGYELLKEKEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIE 271

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395138  478 VALREARATLR-VSEGRARGLQEAARAREQELEACSQELQRYRQEAERLREKAGHLDAEASGLRdppvppATTDPfLLAE 556
Cdd:TIGR02169  272 QLLEELNKKIKdLGEEEQLRVKEKIGELEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLL------AEIEE-LERE 344

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395138  557 SDEAKVQRAAAGAG-GSLRAQVERLRQELQREQRRGDEQRDsfegERLAWQAEKEQVIRYQKQLQHNYIQMYRRNRQLEQ 635
Cdd:TIGR02169  345 IEEERKRRDKLTEEyAELKEELEDLRAELEEVDKEFAETRD----ELKDYREKLEKLKREINELKRELDRLQEELQRLSE 420

                          250
                   ....*....|...
gi 1720395138  636 ELQQLSLELEARE 648
Cdd:TIGR02169  421 ELADLNAAIAGIE 433
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
402-652 1.70e-09

Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 61.08  E-value: 1.70e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395138  402 EKRQLQDDFAQLLQEREQLERRCATFEREQRELGpRLEETKWE---VCQKSGEISLLKQQLkesqAELVQKGSELVALRV 478
Cdd:COG4913    618 ELAELEEELAEAEERLEALEAELDALQERREALQ-RLAEYSWDeidVASAEREIAELEAEL----ERLDASSDDLAALEE 692

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395138  479 ALREARATLRVSEGRARGLQEAARAREQELEACSQELQRYRQEAERLREKAG-HLDAEASGLRDPpvppattdpfLLAES 557
Cdd:COG4913    693 QLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARlELRALLEERFAA----------ALGDA 762

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395138  558 DEAKVQRAAAGAGGSLRAQVERLRQELQREQRRGDEQrdsFEGERLAWQAEKEQVIRYQKQLQHnyiqmYRRNR--QLEQ 635
Cdd:COG4913    763 VERELRENLEERIDALRARLNRAEEELERAMRAFNRE---WPAETADLDADLESLPEYLALLDR-----LEEDGlpEYEE 834

                          250
                   ....*....|....*..
gi 1720395138  636 ELQQLSLELEARELADL 652
Cdd:COG4913    835 RFKELLNENSIEFVADL 851
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 447-659 2.87e-09

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: 59.39  E-value: 2.87e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395138 447 QKSGEISLLKQQLKESQAELVQKGSELVALRVALREARATLRVSEGRARGLQEAARAREQELEACSQELQRYRQEAERLR 526
Cdd:COG4942    24 EAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQK 103

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395138 527 EKAGHLDAEA--SGLRDPPVPPATTDPFLLAESDE------AKVQRAAAGAGGSLRAQVERLRQELQREQRRGDEQRDSF 598
Cdd:COG4942   104 EELAELLRALyrLGRQPPLALLLSPEDFLDAVRRLqylkylAPARREQAEELRADLAELAALRAELEAERAELEALLAEL 183

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1720395138 599 EGERLAWQAEKEQVIRYQKQLQHNYIQMYRRNRQLEQELQQLSLELEARELADLGLAESAP 659
Cdd:COG4942   184 EEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTP 244
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 333-585 6.79e-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: 59.31  E-value: 6.79e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395138  333 KLRDREAELQQLRDSMDESEATVCQAfGARQRRWPRERGedcaaqaqqatqRVQRAQQLLQLQVFQLQQEKRQLQDDFAQ 412
Cdd:TIGR02169  295 KIGELEAEIASLERSIAEKERELEDA-EERLAKLEAEID------------KLLAEIEELEREIEEERKRRDKLTEEYAE 361

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395138  413 LLQEREQLERRCATFEREQRELGPRLEETKWEVCQKSGEISLLKQQLKESQAELVQKGSELVALRVALREARATLRVSEG 492
Cdd:TIGR02169  362 LKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEE 441

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395138  493 RARGLQEAARAREQELEACSQELQRYRQEAERLREKAGHLDAEASGLRdppvppattdpfllAESDEAKVQRAAAG-AGG 571
Cdd:TIGR02169  442 EKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQ--------------RELAEAEAQARASEeRVR 507

                          250
                   ....*....|....
gi 1720395138  572 SLRAQVERLRQELQ 585
Cdd:TIGR02169  508 GGRAVEEVLKASIQ 521
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
402-657 8.83e-09

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 58.63  E-value: 8.83e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395138 402 EKRQLQDDFAQLLQEREQLERRCATfEREQRELGPRLEETKWEVCqksgEISLLKQQLKESQAELVQKGSELVALRVALR 481
Cdd:COG4717   113 ELREELEKLEKLLQLLPLYQELEAL-EAELAELPERLEELEERLE----ELRELEEELEELEAELAELQEELEELLEQLS 187

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395138 482 -EARATLRVSEGRARGLQEAARAREQELEACSQELQRYRQEAERLREKAGHLDAEASgLRDPPVPP----------ATTD 550
Cdd:COG4717   188 lATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEER-LKEARLLLliaaallallGLGG 266

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395138 551 PFLLAESDEAKVQRAAAGAGGSLRAQVERLRQELQREQRRGDEQRDSFEGERLAWQAEKEQV----------IRYQKQLQ 620
Cdd:COG4717   267 SLLSLILTIAGVLFLVLGLLALLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALglppdlspeeLLELLDRI 346

                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 1720395138 621 HNYIQMYRRNRQLEQELQQLSLELEARELADLGLAES 657
Cdd:COG4717   347 EELQELLREAEELEEELQLEELEQEIAALLAEAGVED 383
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 387-670 1.48e-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: 58.16  E-value: 1.48e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395138  387 RAQQLLQLQVFQLQQEKRQLQDDFAQLLQEREQLERRCATFEREQRELGPRLEETKWEVCQKSGEISLLKQQLKESQAEL 466
Cdd:TIGR02169  660 RAPRGGILFSRSEPAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERL 739

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395138  467 VQKGSELVALRVALREARATLRVSEGRARGLQEAARAREQELEACSQELQRyrQEAERLREKAGHLDAEASGLRdppvpp 546
Cdd:TIGR02169  740 EELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARLSH--SRIPEIQAELSKLEEEVSRIE------ 811

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395138  547 attdpfLLAESDEAKVQRAAAgaggsLRAQVERLRQELQREQRRGDEQRDSFEGERLAWQAEKE----QVIRYQKQL--- 619
Cdd:TIGR02169  812 ------ARLREIEQKLNRLTL-----EKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEeleeELEELEAALrdl 880

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1720395138  620 --QHNYIQMYRRN-----RQLEQELQQLSLELEARELADLGLAESAPcICLEEITATE 670
Cdd:TIGR02169  881 esRLGDLKKERDEleaqlRELERKIEELEAQIEKKRKRLSELKAKLE-ALEEELSEIE 937
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 415-656 2.47e-08

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: 57.37  E-value: 2.47e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395138  415 QEREQLERRCATFEREQRELGPRLEETKwevcqksGEISLLKQQLKESQAELVQKGSELVALRVALREARATLRVSEGRA 494
Cdd:TIGR02168  677 REIEELEEKIEELEEKIAELEKALAELR-------KELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERI 749

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395138  495 RGLQEAARAREQELEACSQELQRYRQEAERLREKAGHLDAEASGLrdppvppattdpfllaeSDEAKVQRAAAGAggsLR 574
Cdd:TIGR02168  750 AQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQL-----------------KEELKALREALDE---LR 809

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395138  575 AQVERLRQE-------LQREQRRGDEQRDSFEGERLAWQAEKEQVIRYQKQLQHNYIQMYRRNRQLEQELQQLSLELEAR 647
Cdd:TIGR02168  810 AELTLLNEEaanlrerLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEAL 889


                   ....*....
gi 1720395138  648 ELADLGLAE 656
Cdd:TIGR02168  890 ALLRSELEE 898
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
412-654 1.40e-06

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 51.06  E-value: 1.40e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395138 412 QLLQEREQLERRCATFEREQRELGPRLEETKWEVCQKSGEISLLKQQLKESQAELVQKGSELVALRVALREARATLRVSE 491
Cdd:COG4372    14 SLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQ 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395138 492 GRARGLQEAARAREQELEACSQELQRYRQEAERLREKAGHLDAEASglrdppvppattdpfLLAESDEAKVQRAAagagg 571
Cdd:COG4372    94 AELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIA---------------ELQSEIAEREEELK----- 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395138 572 SLRAQVERLRQELQR---EQRRGDEQRDSFEGERLAWQAEKEQVIRYQKQLQHNYIQMYRRNRQLEQELQQLSLELEARE 648
Cdd:COG4372   154 ELEEQLESLQEELAAleqELQALSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGL 233


                  ....*.
gi 1720395138 649 LADLGL 654
Cdd:COG4372   234 ALSALL 239
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
402-540 1.91e-06

Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 51.45  E-value: 1.91e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395138  402 EKRQLQDDFAQLLQEREQLERRCATFEREQRELGPRLEETKwEVCQKSG--EISLLKQQLKESQAELVQKGSELVALRVA 479
Cdd:COG4913    289 RLELLEAELEELRAELARLEAELERLEARLDALREELDELE-AQIRGNGgdRLEQLEREIERLERELEERERRRARLEAL 367

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1720395138  480 LREARATLRVSEGRARGLQEAARAR----EQELEACSQELQRYRQEAERLREKAGHLDAEASGLR 540
Cdd:COG4913    368 LAALGLPLPASAEEFAALRAEAAALlealEEELEALEEALAEAEAALRDLRRELRELEAEIASLE 432
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
402-537 4.16e-06

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 49.52  E-value: 4.16e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395138 402 EKRQLQDDFAQLLQEREQLERRCATFEREQRELGPRLEETKWEVCQKSGEISLLKQQLKESQAELVQKGSELVALRVALR 481
Cdd:COG4372    46 ELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQ 125

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1720395138 482 EARATLRVSEGRARGLQEAARAREQELEACSQELQRYRQEAERLREKAGHLDAEAS 537
Cdd:COG4372   126 DLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEA 181
sbcc TIGR00618
exonuclease SbcC; All proteins in this family for which functions are known are part of an ...
 411-645 6.01e-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: 49.58  E-value: 6.01e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395138  411 AQLLQEREQLE--RRCATFEREQRelgpRLEETKWEVCQKsgEISLLKQQLKESQAELVQKGSELVALRVALREARATLR 488
Cdd:TIGR00618  166 KELLMNLFPLDqyTQLALMEFAKK----KSLHGKAELLTL--RSQLLTLCTPCMPDTYHERKQVLEKELKHLREALQQTQ 239

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395138  489 VSEGRARGLQEAARAREQELEACSQ---ELQRYRQEAERLREKAGHLDAEASGLRDPPVPPATTDPFLLAESDEAKVQRA 565
Cdd:TIGR00618  240 QSHAYLTQKREAQEEQLKKQQLLKQlraRIEELRAQEAVLEETQERINRARKAAPLAAHIKAVTQIEQQAQRIHTELQSK 319

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395138  566 AAGAGGSLRAQVERLRQELQREQRRGDEQRDSFEGERLAWQAEKEQVIRYQKQLQHNYIQMYRRNRQ----LEQELQQLS 641
Cdd:TIGR00618  320 MRSRAKLLMKRAAHVKQQSSIEEQRRLLQTLHSQEIHIRDAHEVATSIREISCQQHTLTQHIHTLQQqkttLTQKLQSLC 399


                   ....
gi 1720395138  642 LELE 645
Cdd:TIGR00618  400 KELD 403
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 402-620 1.27e-05

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: 47.84  E-value: 1.27e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395138 402 EKRQLQDDFAQLLQEREQLERRCATFEREQRELGPRLEETKWEVCQKSGEISLLKQQLKESQAELVQkgsELVALRVALR 481
Cdd:COG4942    42 ELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELAE---LLRALYRLGR 118

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395138 482 EARATLRVSEGRARGLQEAARAREQELEACSQELQRYRQEAERLREKAGHLDAEASGLRdppvppattdpfllaesdeak 561
Cdd:COG4942   119 QPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELE--------------------- 177

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1720395138 562 vqraaagaggSLRAQVERLRQELQREQRRGDEQRDSFEGERLAWQAEKEQVIRYQKQLQ 620
Cdd:COG4942   178 ----------ALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELE 226
Golgin_A5 pfam09787
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining ...
 507-656 1.32e-05

Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining Golgi structure. They stimulate the formation of Golgi stacks and ribbons, and are involved in intra-Golgi retrograde transport. Two main interactions have been characterized: one with RAB1A that has been activated by GTP-binding and another with isoform CASP of CUTL1.


Pssm-ID: 462900 [Multi-domain]  Cd Length: 305  Bit Score: 47.45  E-value: 1.32e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395138 507 ELEACSQELQRYRQEAER-LREKAGHLDA--EASGLRDPPVPPATTdpfllAESDEAKVQRAAAGAG-GSLRAQVERLRQ 582
Cdd:pfam09787   1 NLESAKQELADYKQKAARiLQSKEKLIASlkEGSGVEGLDSSTALT-----LELEELRQERDLLREEiQKLRGQIQQLRT 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395138 583 ELQREQRRGDEQRDS-----------FEGERLAWQAEKEQVIRYQKQLQHNYIQMYR-------RNRQLEQELQQLSLEL 644
Cdd:pfam09787  76 ELQELEAQQQEEAESsreqlqeleeqLATERSARREAEAELERLQEELRYLEEELRRskatlqsRIKDREAEIEKLRNQL 155

                         170
                  ....*....|..
gi 1720395138 645 EARELADLGLAE 656
Cdd:pfam09787 156 TSKSQSSSSQSE 167
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
455-648 1.83e-05

Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 48.09  E-value: 1.83e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395138 455 LKQQLKESQAELVQKGSELVALRvalreARATLRVSEGRARGLQEAARAREQELEACSQELQRYRQEAERLREKAGHLDA 534
Cdd:COG3206   180 LEEQLPELRKELEEAEAALEEFR-----QKNGLVDLSEEAKLLLQQLSELESQLAEARAELAEAEARLAALRAQLGSGPD 254

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395138 535 EASGLRDPPVPPAttdpfLLAESDEAKVQRAAAGAGG--------SLRAQVERLRQELQREQRRGdeqRDSFEGERLAWQ 606
Cdd:COG3206   255 ALPELLQSPVIQQ-----LRAQLAELEAELAELSARYtpnhpdviALRAQIAALRAQLQQEAQRI---LASLEAELEALQ 326

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 1720395138 607 AEKEQVIRYQKQLQhnyiQMYRRNRQLEQELQQLSLELEARE 648
Cdd:COG3206   327 AREASLQAQLAQLE----ARLAELPELEAELRRLEREVEVAR 364
HlpA COG2825
Periplasmic chaperone for outer membrane proteins, Skp family [Cell wall/membrane/envelope ...
 455-524 2.17e-05

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


Pssm-ID: 442073 [Multi-domain]  Cd Length: 171  Bit Score: 45.21  E-value: 2.17e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395138 455 LKQQLKESQAELVQKGSELVALRVALREARATLRvsegrarglQEAARAREQELEACSQELQRYRQEAER 524
Cdd:COG2825    48 LEKEFKKRQAELQKLEKELQALQEKLQKEAATLS---------EEERQKKERELQKKQQELQRKQQEAQQ 108
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
416-652 2.77e-05

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 47.37  E-value: 2.77e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395138 416 EREQLER---RCATFEREQRELGPRLEETKWEVCQKSGEISLLKQQLKESQAELvqkgSELVALRVALREARATLRVSEG 492
Cdd:PRK03918  177 RIERLEKfikRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEV----KELEELKEEIEELEKELESLEG 252

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395138 493 RARGLQEAARARE---QELEACSQELQRYRQEAERLREKAghldAEASGLRDppvppattdpfLLAESDEAKVQraaaga 569
Cdd:PRK03918  253 SKRKLEEKIRELEeriEELKKEIEELEEKVKELKELKEKA----EEYIKLSE-----------FYEEYLDELRE------ 311

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395138 570 ggsLRAQVERLRQELQREQRRGDEQRDsfEGERLAWQAEKEQVIRYQKQLQHNYIQMYRRNRQLEQELQQLSLELEAREL 649
Cdd:PRK03918  312 ---IEKRLSRLEEEINGIEERIKELEE--KEERLEELKKKLKELEKRLEELEERHELYEEAKAKKEELERLKKRLTGLTP 386


                  ...
gi 1720395138 650 ADL 652
Cdd:PRK03918  387 EKL 389
OmpH smart00935
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH ...
 455-524 3.10e-05

Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH among others. Skp (OmpH) has been characterized as a molecular chaperone that interacts with unfolded proteins as they emerge in the periplasm from the Sec translocation machinery.


Pssm-ID: 214922 [Multi-domain]  Cd Length: 140  Bit Score: 44.11  E-value: 3.10e-05
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395138  455 LKQQLKESQAELVQKGSELVALRVALREARATLRvsegrarglQEAARAREQELEACSQELQRYRQEAER 524
Cdd:smart00935  23 LEKEFKKRQAELEKLEKELQKLKEKLQKDAATLS---------EAAREKKEKELQKKVQEFQRKQQKLQQ 83
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
402-589 3.36e-05

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 47.34  E-value: 3.36e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395138 402 EKRQLQDDFAQLLQEREQLERRCATFEREQRELGPRLEETKWEVCQKSGEISLLKQQLKESQAELVQKGSELVALRVA-- 479
Cdd:PRK02224  259 EIEDLRETIAETEREREELAEEVRDLRERLEELEEERDDLLAEAGLDDADAEAVEARREELEDRDEELRDRLEECRVAaq 338

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395138 480 --------LREARATLrvsEGRARGLQEAARAREQELEACSQELQRYRQEAERLREKaghLDAEASGLRDPPVPPATTDP 551
Cdd:PRK02224  339 ahneeaesLREDADDL---EERAEELREEAAELESELEEAREAVEDRREEIEELEEE---IEELRERFGDAPVDLGNAED 412

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 1720395138 552 FL--LAESDEAKVQRAAagaggSLRAQVERLRQELQREQR 589
Cdd:PRK02224  413 FLeeLREERDELREREA-----ELEATLRTARERVEEAEA 447
GAS pfam13851
Growth-arrest specific micro-tubule binding; This family is the highly conserved central ...
 404-473 6.14e-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 localization 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: 464001 [Multi-domain]  Cd Length: 200  Bit Score: 44.51  E-value: 6.14e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1720395138 404 RQLQDDFAQLLQEREQLERRCATFEREQRELGPRLEETKWEVCQKSG-EISLLKQQLKESQAELVQKGSEL 473
Cdd:pfam13851  95 KVLEKELKDLKWEHEVLEQRFEKVERERDELYDKFEAAIQDVQQKTGlKNLLLEKKLQALGETLEKKEAQL 165
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
406-648 6.17e-05

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 46.19  E-value: 6.17e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395138 406 LQDDFAQLLQEREQLERRCATFEREQRELGPRLEETkwEVCQKSGEISLLKQQLKESQ-----AELVQKGSELVALRVAL 480
Cdd:PRK02224  410 AEDFLEELREERDELREREAELEATLRTARERVEEA--EALLEAGKCPECGQPVEGSPhvetiEEDRERVEELEAELEDL 487

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395138 481 REARATLRVSEGRARGLQEAARARE----------QELEACSQELQRYRQEAERLREKAGHLDAEASGLRdppvppattd 550
Cdd:PRK02224  488 EEEVEEVEERLERAEDLVEAEDRIErleerredleELIAERRETIEEKRERAEELRERAAELEAEAEEKR---------- 557

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395138 551 pfllaesDEAKVQRAAAGAGGSLRAQVERLRQELQREQRRGDEQRDSFE-----GERLAWQAEKEQVIRYQKQLQHNYIQ 625
Cdd:PRK02224  558 -------EAAAEAEEEAEEAREEVAELNSKLAELKERIESLERIRTLLAaiadaEDEIERLREKREALAELNDERRERLA 630

                         250       260
                  ....*....|....*....|....
gi 1720395138 626 MYR-RNRQLEQELQQLSLElEARE 648
Cdd:PRK02224  631 EKReRKRELEAEFDEARIE-EARE 653
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
403-650 1.10e-04

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 45.42  E-value: 1.10e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395138 403 KRQLQDDFAQLLQEREQLErrcatfEREQRELGPRLEETKWEVCQKSGEISLLKQQlKESQAELVQKGSELVAlrvALRE 482
Cdd:PRK02224  179 ERVLSDQRGSLDQLKAQIE------EKEEKDLHERLNGLESELAELDEEIERYEEQ-REQARETRDEADEVLE---EHEE 248

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395138 483 ARATLRVSEGRARGLQEAARAREQELEACSQELQRYRQEAERLREKAGHLDAEAsGLRDPpvppattdpfllaeSDEAkv 562
Cdd:PRK02224  249 RREELETLEAEIEDLRETIAETEREREELAEEVRDLRERLEELEEERDDLLAEA-GLDDA--------------DAEA-- 311

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395138 563 qraaagaggslraqVERLRQELQReqrRGDEQRDSFEGERLAWQAEKEQVIRYQKqlqhNYIQMYRRNRQLEQELQQLSL 642
Cdd:PRK02224  312 --------------VEARREELED---RDEELRDRLEECRVAAQAHNEEAESLRE----DADDLEERAEELREEAAELES 370


                  ....*...
gi 1720395138 643 ELEARELA 650
Cdd:PRK02224  371 ELEEAREA 378
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
 404-658 1.13e-04

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: 460256 [Multi-domain]  Cd Length: 1081  Bit Score: 45.55  E-value: 1.13e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395138  404 RQLQDDFAQLLQEREQLERRCATFEREQRELGPRLEETKWEVCQKSGEISLLKQQLKESQaelvqkgSELVALRVALREA 483
Cdd:pfam01576  492 RQLEDERNSLQEQLEEEEEAKRNVERQLSTLQAQLSDMKKKLEEDAGTLEALEEGKKRLQ-------RELEALTQQLEEK 564

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395138  484 RATLRVSEGRARGLQeaarareQELEACSQELQRYRQEAERLREKAGHLDAeasglrdppvppattdpfLLAESDEAKVQ 563
Cdd:pfam01576  565 AAAYDKLEKTKNRLQ-------QELDDLLVDLDHQRQLVSNLEKKQKKFDQ------------------MLAEEKAISAR 619

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395138  564 RAAAGAggslRAQVERLRQE-----LQREQRRGDEQRDSFEGERLAWQAEKEQVIRYQKQLQHNYIQMYRRNRQLEQELQ 638
Cdd:pfam01576  620 YAEERD----RAEAEAREKEtralsLARALEEALEAKEELERTNKQLRAEMEDLVSSKDDVGKNVHELERSKRALEQQVE 695

                          250       260
                   ....*....|....*....|.
gi 1720395138  639 QLSLELEarELAD-LGLAESA 658
Cdd:pfam01576  696 EMKTQLE--ELEDeLQATEDA 714
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 444-659 1.30e-04

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 44.82  E-value: 1.30e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395138 444 EVCQKSGEISLLKQQLKESQAELVQKGSELVALRVALREARATLRVSEGRARGLQEAARAREQELEACSQELqryrqeAE 523
Cdd:COG3883    17 QIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREEL------GE 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395138 524 RLRekaghlDAEASGLRDPPVppattDPFLLAESDEAKVQRAAA-----GAGGSLRAQVERLRQELQREQRRGDEQRDSF 598
Cdd:COG3883    91 RAR------ALYRSGGSVSYL-----DVLLGSESFSDFLDRLSAlskiaDADADLLEELKADKAELEAKKAELEAKLAEL 159

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1720395138 599 EGERLAWQAEKEQVIRYQKQLQHNYIQMYRRNRQLEQELQQLSLELEARELADLGLAESAP 659
Cdd:COG3883   160 EALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAA 220
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 402-605 1.55e-04

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


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 44.37  E-value: 1.55e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395138 402 EKRQLQDDFAQLLQEREQLERRCATFEREQRELGPRLEETKWEVCQKSGEISLLKQQLKESQAELVQKGSELVALRVALR 481
Cdd:COG4942    21 AAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELE 100

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395138 482 EARATLRV-------------------------SEGRARGLQEAARAREQELEACSQELQRYRQEAERLREKAGHLDAEA 536
Cdd:COG4942   101 AQKEELAEllralyrlgrqpplalllspedfldAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALL 180

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395138 537 SGL-------------RDPPVPPATTDPFLLAESDEAKVQRAAagaggSLRAQVERLRQELQREQRRGDEQRDSFEGERL 603
Cdd:COG4942   181 AELeeeraalealkaeRQKLLARLEKELAELAAELAELQQEAE-----ELEALIARLEAEAAAAAERTPAAGFAALKGKL 255


                  ..
gi 1720395138 604 AW 605
Cdd:COG4942   256 PW 257
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
413-632 1.81e-04

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 44.76  E-value: 1.81e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395138 413 LLQEREQLERRCATFEREQRELGPRLEETKWevCQKSGEISLLKQQLKESQAELVQKGSELVALRVALREARATLRVSE- 491
Cdd:COG4717   291 LLLAREKASLGKEAEELQALPALEELEEEEL--EELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLEEl 368

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395138 492 --GRARGLQEAARAREQELEACSQELQRYRQEAERLREKAGHLDAEASGLRDppVPPATTDPFLLAESDEAKVQRAAAGA 569
Cdd:COG4717   369 eqEIAALLAEAGVEDEEELRAALEQAEEYQELKEELEELEEQLEELLGELEE--LLEALDEEELEEELEELEEELEELEE 446

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1720395138 570 G-GSLRAQVERLRQELQR--EQRRGDEQRDSFEG--ERLAWQAEKEQVIRYQKQLQHNYIQMYRRNRQ 632
Cdd:COG4717   447 ElEELREELAELEAELEQleEDGELAELLQELEElkAELRELAEEWAALKLALELLEEAREEYREERL 514
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 402-582 1.95e-04

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: 43.37  E-value: 1.95e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395138 402 EKRQLQDDFAQLLQEREQLERRCATFEREQRELGPRLEETKWEVCQKSGEISLLKQQLKESQAEL--VQKGSELVALRVA 479
Cdd:COG1579    18 ELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLgnVRNNKEYEALQKE 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395138 480 LREARATLRVSEGRARGLQEAARAREQELEACSQELQryrQEAERLREKAGHLDAEASGLRdppvppattdpfllAESDE 559
Cdd:COG1579    98 IESLKRRISDLEDEILELMERIEELEEELAELEAELA---ELEAELEEKKAELDEELAELE--------------AELEE 160

                         170       180
                  ....*....|....*....|....*
gi 1720395138 560 AKVQRAAAGAG--GSLRAQVERLRQ 582
Cdd:COG1579   161 LEAEREELAAKipPELLALYERIRK 185
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 330-613 2.17e-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: 44.67  E-value: 2.17e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395138  330 LEGKLRDREAELQQLRDSMDESEATVcqafgaRQRRWPRERGE-----DCAAQAQQATQRVQRAQQLLQLQVFQLQQEKR 404
Cdd:TIGR02169  763 LEARIEELEEDLHKLEEALNDLEARL------SHSRIPEIQAElskleEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQ 836

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395138  405 QLQddfaqllQEREQLERRCATFEREQRELGPRLEEtkwevcqksgeislLKQQLKESQAELVQKGSELVALRVALREAR 484
Cdd:TIGR02169  837 ELQ-------EQRIDLKEQIKSIEKEIENLNGKKEE--------------LEEELEELEAALRDLESRLGDLKKERDELE 895

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395138  485 ATLRvsegrarglqeAARAREQELEAcsqELQRYRQEAERLREKAGHLDAEASGLRDP-----PVPPATTDPFLLAESDE 559
Cdd:TIGR02169  896 AQLR-----------ELERKIEELEA---QIEKKRKRLSELKAKLEALEEELSEIEDPkgedeEIPEEELSLEDVQAELQ 961

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1720395138  560 AKVQRAAAGAGGSLRAQverlrQELQREQRRgdeqRDSFEGERLAWQAEKEQVI 613
Cdd:TIGR02169  962 RVEEEIRALEPVNMLAI-----QEYEEVLKR----LDELKEKRAKLEEERKAIL 1006
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 331-653 2.90e-04

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 44.16  E-value: 2.90e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395138 331 EGKLRDREAELQQLRDSMDESEATVcqafGARQRRWPRERGEDCAAQAQQATQRVQRAQQLLQLQVFQLQQEKRQLQDDF 410
Cdd:COG1196   486 LAEAAARLLLLLEAEADYEGFLEGV----KAALLLAGLRGLAGAVAVLIGVEAAYEAALEAALAAALQNIVVEDDEVAAA 561

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395138 411 AQLLQEREQLERrcATFEREQRELGPRLEETKWEVCQKSGEISLLKQQLKESQAELVQKGSELVALRVALREARATLRVS 490
Cdd:COG1196   562 AIEYLKAAKAGR--ATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRA 639

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395138 491 EGRARGLQEAARAREQELEACSQELQRYRQEAERLREKaghldaeasglrdppvppattdpfllAESDEAKVQRAAAGAG 570
Cdd:COG1196   640 VTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEA--------------------------EAELEELAERLAEEEL 693

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395138 571 GSLRAQVERLRQELQREQRRGDEQRDSFEGERLAWQAEKEQVIRYQKQLQHNYIQMYRRNR---------QLEQELQQLs 641
Cdd:COG1196   694 ELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEelpeppdleELERELERL- 772

                         330
                  ....*....|..
gi 1720395138 642 leleARELADLG 653
Cdd:COG1196   773 ----EREIEALG 780
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 303-665 3.56e-04

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 43.90  E-value: 3.56e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395138  303 GSSSGGDRSPPPPPPPPPSDEALLHcvlegKLRDREAELQQLRDSMDEseatvcqafgaRQRRWPRERGEdcaaqaqqat 382
Cdd:TIGR02169  653 GAMTGGSRAPRGGILFSRSEPAELQ-----RLRERLEGLKRELSSLQS-----------ELRRIENRLDE---------- 706

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395138  383 qrVQRAQQLLQLQVFQLQQEKRQLQDDFAQLLQEREQLERRCATFEReqrelgprleetkwevcqksgEISLLKQQLKES 462
Cdd:TIGR02169  707 --LSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQ---------------------EIENVKSELKEL 763

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395138  463 QAELVQKGSELVALRVAL-----REARATLRVSEGRARGLQEAARAREQELEACSQELQRYRQEAERLREKAGHldaeas 537
Cdd:TIGR02169  764 EARIEELEEDLHKLEEALndleaRLSHSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQE------ 837

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395138  538 glrdppvppattdpfLLAESDEAKVQRAAAGAG-GSLRAQVERLRQELQREQ---RRGDEQRDSFEGERLAWQAEKEQVI 613
Cdd:TIGR02169  838 ---------------LQEQRIDLKEQIKSIEKEiENLNGKKEELEEELEELEaalRDLESRLGDLKKERDELEAQLRELE 902

                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1720395138  614 RYQKQLQHNYIQMYRRNRQLEQELQQLSLELEARELADLGLAESAPCICLEE 665
Cdd:TIGR02169  903 RKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDEEIPEEELSLE 954
Crescentin pfam19220
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament ...
 402-647 3.82e-04

Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament proteins, named crescentin, whose cytoskeletal function is required for the vibrioid and helical shapes of Caulobacter crescentus. Without crescentin, the cells adopt a straight-rod morphology. Crescentin has characteriztic features of IF proteins including the ability to assemble into filaments in vitro without energy or cofactor requirements. In vivo, crescentin forms a helical structure that colocalizes with the inner cell curvatures beneath the cytoplasmic membrane.


Pssm-ID: 437057 [Multi-domain]  Cd Length: 401  Bit Score: 43.52  E-value: 3.82e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395138 402 EKRQLQDDFAQLLQEREQLERRCATFEREQRELGPRLEETKWEVCQKS--------------GEISLLKQQLKESQAELV 467
Cdd:pfam19220  70 ELAGLTRRLSAAEGELEELVARLAKLEAALREAEAAKEELRIELRDKTaqaealerqlaaetEQNRALEEENKALREEAQ 149

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395138 468 QKGSELVAL---RVALREARATLRVSEGRARGLQEAARAREQELEACSQEL-QRYRQEAERLREKAGHLDAEASGLRDpp 543
Cdd:pfam19220 150 AAEKALQRAegeLATARERLALLEQENRRLQALSEEQAAELAELTRRLAELeTQLDATRARLRALEGQLAAEQAERER-- 227

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395138 544 vppattdpfLLAESDEAKVQRAAAGAGGSLR--------AQVERLRQELQREQRRGDEQRDSFEGERLAWQAEKEQVIRY 615
Cdd:pfam19220 228 ---------AEAQLEEAVEAHRAERASLRMKlealtaraAATEQLLAEARNQLRDRDEAIRAAERRLKEASIERDTLERR 298

                         250       260       270
                  ....*....|....*....|....*....|..
gi 1720395138 616 QKQLQHnyiQMYRRNRQLeQELQQLSLELEAR 647
Cdd:pfam19220 299 LAGLEA---DLERRTQQF-QEMQRARAELEER 326
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 333-540 3.83e-04

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


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 43.21  E-value: 3.83e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395138 333 KLRDREAELQQLRDSMDESEATVCQAFGARQRrwprergedcaaqAQQATQRVQRAQQLLQLQVFQLQQEKRQLQDDFAQ 412
Cdd:COG4942    21 AAAEAEAELEQLQQEIAELEKELAALKKEEKA-------------LLKQLAALERRIAALARRIRALEQELAALEAELAE 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395138 413 LLQEREQLERRcatFEREQRELGPRLEETkwevcQKSGEISLLK-----------------------------QQLKESQ 463
Cdd:COG4942    88 LEKEIAELRAE---LEAQKEELAELLRAL-----YRLGRQPPLAlllspedfldavrrlqylkylaparreqaEELRADL 159

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1720395138 464 AELVQKGSELVALRVALREARATLrvsEGRARGLQEAARAREQELEACSQELQRYRQEAERLREKAGHLDAEASGLR 540
Cdd:COG4942   160 AELAALRAELEAERAELEALLAEL---EEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLE 233
mukB PRK04863
chromosome partition protein MukB;
405-648 5.09e-04

chromosome partition protein MukB;


Pssm-ID: 235316 [Multi-domain]  Cd Length: 1486  Bit Score: 43.41  E-value: 5.09e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395138  405 QLQDDFAQLLQE----REQLERRCATFEreqrELGPRLEETKWEVCQKSGEISLLKQQLKESQAELVQKGSELV----AL 476
Cdd:PRK04863   331 QAASDHLNLVQTalrqQEKIERYQADLE----ELEERLEEQNEVVEEADEQQEENEARAEAAEEEVDELKSQLAdyqqAL 406

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395138  477 RV-------------ALREARATLRVSE---GRARGLQEAARAREQEL-EACSQELQRYR--QEAERLREKAGHLDAEAS 537
Cdd:PRK04863   407 DVqqtraiqyqqavqALERAKQLCGLPDltaDNAEDWLEEFQAKEQEAtEELLSLEQKLSvaQAAHSQFEQAYQLVRKIA 486

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395138  538 GlrdpPVPPATTDPFLLAESDEAKVQRAAAGAGGSLRAQ-------------VERLRQELQREQRRGDEQRDSFEGERLA 604
Cdd:PRK04863   487 G----EVSRSEAWDVARELLRRLREQRHLAEQLQQLRMRlseleqrlrqqqrAERLLAEFCKRLGKNLDDEDELEQLQEE 562

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....
gi 1720395138  605 WQAEKEQVIRYQKQLQHNYIQMyrrnRQLEQELQQLSLELEARE 648
Cdd:PRK04863   563 LEARLESLSESVSEARERRMAL----RQQLEQLQARIQRLAARA 602
OmpH pfam03938
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH ...
 455-524 8.14e-04

Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH among others. Skp (OmpH) has been characterized as a molecular chaperone that interacts with unfolded proteins as they emerge in the periplasm from the Sec translocation machinery.


Pssm-ID: 461098 [Multi-domain]  Cd Length: 140  Bit Score: 40.25  E-value: 8.14e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395138 455 LKQQLKESQAELVQKGSELVALRVALREARATLrvsegrarglQEAARAREQELEACSQELQRYRQEAER 524
Cdd:pfam03938  24 LEKKFKKRQAELEAKQKELQKLYEELQKDGALL----------EEEREEKEQELQKKEQELQQLQQKAQQ 83
HOOK pfam05622
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ...
 405-564 8.49e-04

HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from different eukaryotic organizms. 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 this 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. This entry includes the central coiled-coiled domain and the divergent C-terminal domain.


Pssm-ID: 461694 [Multi-domain]  Cd Length: 528  Bit Score: 42.37  E-value: 8.49e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395138 405 QLQDDFAQLLQEREQLERRCATFEREQR-------ELGPRLEE---TKWEVCQKSGEISLLKQQLKESQAELVQKGSELV 474
Cdd:pfam05622 301 SYRERLTELQQLLEDANRRKNELETQNRlanqrilELQQQVEElqkALQEQGSKAEDSSLLKQKLEEHLEKLHEAQSELQ 380

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395138 475 ALRVALREARATLRVSEGR-ARGLQEAARAREQELEACSqelQRYRQEAERLREKAGHLD--------AEASGLRDPPVP 545
Cdd:pfam05622 381 KKKEQIEELEPKQDSNLAQkIDELQEALRKKDEDMKAME---ERYKKYVEKAKSVIKTLDpkqnpaspPEIQALKNQLLE 457

                         170
                  ....*....|....*....
gi 1720395138 546 PATTDPFLLAESDEAKVQR 564
Cdd:pfam05622 458 KDKKIEHLERDFEKSKLQR 476
DUF3584 pfam12128
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ...
 407-646 8.84e-04

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: 432349 [Multi-domain]  Cd Length: 1191  Bit Score: 42.52  E-value: 8.84e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395138  407 QDDFAQLLQE-REQLERRCATFEREQRELGPRLEETKWEVCQKSGEISLLKQQ-------------LKESQAELVQKGSE 472
Cdd:pfam12128  414 EDDLQALESElREQLEAGKLEFNEEEYRLKSRLGELKLRLNQATATPELLLQLenfderierareeQEAANAEVERLQSE 493

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395138  473 LVALRVALREARATLRVSEGRARGLQEAARAREQELEACSQELQRY-RQEAERLREKAGHLDAEASGLR---DPPVPPAT 548
Cdd:pfam12128  494 LRQARKRRDQASEALRQASRRLEERQSALDELELQLFPQAGTLLHFlRKEAPDWEQSIGKVISPELLHRtdlDPEVWDGS 573

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395138  549 TD-----------------PFLLAESDEAKVQRAAA----GAGGSLRAQVER----LRQELQREQRRGDEQRDSFEGERL 603
Cdd:pfam12128  574 VGgelnlygvkldlkridvPEWAASEEELRERLDKAeealQSAREKQAAAEEqlvqANGELEKASREETFARTALKNARL 653

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*..
gi 1720395138  604 A---WQAEKEQV-IRYQKQLQHNYIQMYRRNRQLEQELQQLSLELEA 646
Cdd:pfam12128  654 DlrrLFDEKQSEkDKKNKALAERKDSANERLNSLEAQLKQLDKKHQA 700
PRK12704 PRK12704
phosphodiesterase; Provisional
 403-524 9.50e-04

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 42.07  E-value: 9.50e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395138 403 KRQLQDDFAQLLQEREQLERRCATFEREQRElgprLEETKWEVCQKSGEISLLKQQLKESQAELVQKGSELVALRVAlrE 482
Cdd:PRK12704   81 RNELQKLEKRLLQKEENLDRKLELLEKREEE----LEKKEKELEQKQQELEKKEEELEELIEEQLQELERISGLTAE--E 154

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1720395138 483 ARATL--RVsEGRARgLQEAARAREQELEAcsqelqryRQEAER 524
Cdd:PRK12704  155 AKEILleKV-EEEAR-HEAAVLIKEIEEEA--------KEEADK 188
MukB COG3096
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ...
 404-665 1.26e-03

Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 442330 [Multi-domain]  Cd Length: 1470  Bit Score: 42.25  E-value: 1.26e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395138  404 RQLQddFAQLLQEREQLERRCATFEREQRELGPRLEETKWEVCQKSGEISLLKQQLKESQA---------ELVQKGSELV 474
Cdd:COG3096    411 RAIQ--YQQAVQALEKARALCGLPDLTPENAEDYLAAFRAKEQQATEEVLELEQKLSVADAarrqfekayELVCKIAGEV 488

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395138  475 ALRVALREARATLRvsegRARGLQEAArAREQELEACSQELQRYRQEAERLREKAGHLDAEASGLRDPPvppatTDPFLL 554
Cdd:COG3096    489 ERSQAWQTARELLR----RYRSQQALA-QRLQQLRAQLAELEQRLRQQQNAERLLEEFCQRIGQQLDAA-----EELEEL 558

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395138  555 AESDEAKVQRAAAgaggSLRAQVERlRQELQREQRRGDEQRDSFEGERLAWQAEKEQVIRYQKQ----------LQHNYI 624
Cdd:COG3096    559 LAELEAQLEELEE----QAAEAVEQ-RSELRQQLEQLRARIKELAARAPAWLAAQDALERLREQsgealadsqeVTAAMQ 633

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*.
gi 1720395138  625 QMYRRNRQLEQELQQL-----SLELEARELADLGLAESAPCICLEE 665
Cdd:COG3096    634 QLLEREREATVERDELaarkqALESQIERLSQPGGAEDPRLLALAE 679
PTZ00121 PTZ00121
MAEBL; Provisional
 385-651 1.49e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 42.05  E-value: 1.49e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395138  385 VQRAQQLLQLQVFQLQQEKRQLQDDFAQLLQ--EREQLERRCATFEREQRELGPRL-----EETKWEVCQKSGEISLLKQ 457
Cdd:PTZ00121  1557 LKKAEEKKKAEEAKKAEEDKNMALRKAEEAKkaEEARIEEVMKLYEEEKKMKAEEAkkaeeAKIKAEELKKAEEEKKKVE 1636

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395138  458 QLKESQAELVQKGSELvalrvalREARatlrvSEGRARGLQEAARAREQELEAcsQELqryRQEAERLREKAGHLDAEAS 537
Cdd:PTZ00121  1637 QLKKKEAEEKKKAEEL-------KKAE-----EENKIKAAEEAKKAEEDKKKA--EEA---KKAEEDEKKAAEALKKEAE 1699

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395138  538 GLRdppvppaTTDPFLLAESDEAKVQRAAAGAGGSLRAQVERLRQELQREQRRGDEQRDSfEGERLAWQAEKEQVIRYQK 617
Cdd:PTZ00121  1700 EAK-------KAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKD-EEEKKKIAHLKKEEEKKAE 1771

                          250       260       270
                   ....*....|....*....|....*....|....
gi 1720395138  618 QLQHNYIQMYRRNRQLEQELQQLSLELEARELAD 651
Cdd:PTZ00121  1772 EIRKEKEAVIEEELDEEDEKRRMEVDKKIKDIFD 1805
MukB COG3096
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ...
 414-658 2.75e-03

Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 442330 [Multi-domain]  Cd Length: 1470  Bit Score: 41.09  E-value: 2.75e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395138  414 LQEREQLERRCATFEreqrELGPRLEETKWEVCQKSGEISLLKQQLKESQAELVQKGSELV----ALRV----------- 478
Cdd:COG3096    343 LRQQEKIERYQEDLE----ELTERLEEQEEVVEEAAEQLAEAEARLEAAEEEVDSLKSQLAdyqqALDVqqtraiqyqqa 418

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395138  479 --ALREARATLRVSE---GRARGLQEAARAREQELEACSQELQ-----------RYRQEAERLREKAGHLDAEASGLRdp 542
Cdd:COG3096    419 vqALEKARALCGLPDltpENAEDYLAAFRAKEQQATEEVLELEqklsvadaarrQFEKAYELVCKIAGEVERSQAWQT-- 496

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395138  543 pvppATTdpfLLAESDEakvQRAAAGAGGSLRAQ-------------VERLRQELQREQRRGDEQRDSFEGERLAWQAEK 609
Cdd:COG3096    497 ----ARE---LLRRYRS---QQALAQRLQQLRAQlaeleqrlrqqqnAERLLEEFCQRIGQQLDAAEELEELLAELEAQL 566

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*....
gi 1720395138  610 EQVIRYQKQLQHNYIQMyrrnRQLEQELQQLSLELEARELADLGLAESA 658
Cdd:COG3096    567 EELEEQAAEAVEQRSEL----RQQLEQLRARIKELAARAPAWLAAQDAL 611
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
 403-639 3.53e-03

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: 40.49  E-value: 3.53e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395138 403 KRQLQDDFAQLLQEREQLERRCATFEREQRELGPRLEETKWEVCQKSGEISLLKQQLKESQAELVQKGSELVALRVALRE 482
Cdd:pfam17380 286 ERQQQEKFEKMEQERLRQEKEEKAREVERRRKLEEAEKARQAEMDRQAAIYAEQERMAMERERELERIRQEERKRELERI 365

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395138 483 ARATLRVSEGRARGLQEAARAREQELEACSQELQRYR----QEAERLReKAGHLDAEASGLRDPPVPPATTDPFLLAESD 558
Cdd:pfam17380 366 RQEEIAMEISRMRELERLQMERQQKNERVRQELEAARkvkiLEEERQR-KIQQQKVEMEQIRAEQEEARQREVRRLEEER 444

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395138 559 EAKVQRAAAGAGgSLRAQVERLRQElQREQRRGDEQRDSFEGERLAWQAEKEQVIRYQ-KQLQHNYIQMYRRNRQLEQEL 637
Cdd:pfam17380 445 AREMERVRLEEQ-ERQQQVERLRQQ-EEERKRKKLELEKEKRDRKRAEEQRRKILEKElEERKQAMIEEERKRKLLEKEM 522


                  ..
gi 1720395138 638 QQ 639
Cdd:pfam17380 523 EE 524
rad50 TIGR00606
rad50; All proteins in this family for which functions are known are involvedin recombination, ...
 405-656 5.73e-03

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: 40.03  E-value: 5.73e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395138  405 QLQDDFAQLLQEREQLERrcatFEREQRELGPRL---EETKWEVCQKSGEISLLKQQLKESQAELVQKGSELVALRVALR 481
Cdd:TIGR00606  225 QITSKEAQLESSREIVKS----YENELDPLKNRLkeiEHNLSKIMKLDNEIKALKSRKKQMEKDNSELELKMEKVFQGTD 300

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395138  482 EARATLRVSEGRArglqeaARAREQELEACSQELQRYRQEAERLREKAGHLDAEASGL-------------RDPPVPPAT 548
Cdd:TIGR00606  301 EQLNDLYHNHQRT------VREKERELVDCQRELEKLNKERRLLNQEKTELLVEQGRLqlqadrhqehiraRDSLIQSLA 374

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395138  549 T---------DPFLLAESDEAK--VQRAAAGAGGSLRAQVERLRQELQREQRRGDEQRDSFEGERLAWQAEKEQVIRYQK 617
Cdd:TIGR00606  375 TrleldgferGPFSERQIKNFHtlVIERQEDEAKTAAQLCADLQSKERLKQEQADEIRDEKKGLGRTIELKKEILEKKQE 454

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|..
gi 1720395138  618 QLQHNYIQMyrrnRQLEQELQQLsLELEA---RELADLGLAE 656
Cdd:TIGR00606  455 ELKFVIKEL----QQLEGSSDRI-LELDQelrKAERELSKAE 491
COG1340 COG1340
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
438-645 5.82e-03

Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];


Pssm-ID: 440951 [Multi-domain]  Cd Length: 297  Bit Score: 39.12  E-value: 5.82e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395138 438 LEETKWEVCQKSGEISLLKQQLKESQAELVQKGSELVALRVALREaratlrvsegRARGLQEAARAREQELEACSQELQR 517
Cdd:COG1340     6 LSSSLEELEEKIEELREEIEELKEKRDELNEELKELAEKRDELNA----------QVKELREEAQELREKRDELNEKVKE 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395138 518 YRQEAERLREKAGHLDAEASGLRdppvppattdpfllAESDEAKVQRaaaGAGGSLRAQVERLRQELQREQRRGDEQRDS 597
Cdd:COG1340    76 LKEERDELNEKLNELREELDELR--------------KELAELNKAG---GSIDKLRKEIERLEWRQQTEVLSPEEEKEL 138

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 1720395138 598 FEG-ERLAWQAEK-EQVIRYQKQLqhnyiqmyrrnRQLEQELQQLSLELE 645
Cdd:COG1340   139 VEKiKELEKELEKaKKALEKNEKL-----------KELRAELKELRKEAE 177
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
333-649 6.21e-03

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 39.75  E-value: 6.21e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395138 333 KLRDREAELQQLRDSMDESEATVcqafgarqrrwpRERGEDCAAQAQQATQRVQRAQQLLQLQVFQLQQEKRQLQDDFAQ 412
Cdd:COG4717   150 ELEERLEELRELEEELEELEAEL------------AELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEE 217

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395138 413 LLQEREQLERRCATFEREQRELGP--RLEETKWEVCQKSGEISLLKQQLKESQAELVQKGSELVALRVALREARATLRVS 490
Cdd:COG4717   218 AQEELEELEEELEQLENELEAAALeeRLKEARLLLLIAAALLALLGLGGSLLSLILTIAGVLFLVLGLLALLFLLLAREK 297

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395138 491 EGRARGLQEAARAREQElEACSQELQRYR---------------------QEAERLREKAGHLDAEASGLRdppvppatt 549
Cdd:COG4717   298 ASLGKEAEELQALPALE-ELEEEELEELLaalglppdlspeellelldriEELQELLREAEELEEELQLEE--------- 367

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395138 550 dpflLAESDEAKVQRAAAGAGGSLRAQVERLR--QELQREQRRGDEQRDSFEGERLA---------WQAEKEQVIRYQKQ 618
Cdd:COG4717   368 ----LEQEIAALLAEAGVEDEEELRAALEQAEeyQELKEELEELEEQLEELLGELEEllealdeeeLEEELEELEEELEE 443

                         330       340       350
                  ....*....|....*....|....*....|.
gi 1720395138 619 LQHNYIQMYRRNRQLEQELQQLSLELEAREL 649
Cdd:COG4717   444 LEEELEELREELAELEAELEQLEEDGELAEL 474
YqiK COG2268
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
402-540 6.26e-03

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


Pssm-ID: 441869 [Multi-domain]  Cd Length: 439  Bit Score: 39.47  E-value: 6.26e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395138 402 EKRQLQDDfAQLLQEREQLERRCAtfeREQRELGPRLEETKWEvcQKSGEIsLLKQQLKESQAEL---VQKGSELVAL-- 476
Cdd:COG2268   218 QANREAEE-AELEQEREIETARIA---EAEAELAKKKAEERRE--AETARA-EAEAAYEIAEANAereVQRQLEIAERer 290

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1720395138 477 RVALREARATLRVSEGRA-RGLQEAARAREQELEAcsqelqryRQEAERLREKAghlDAEASGLR 540
Cdd:COG2268   291 EIELQEKEAEREEAELEAdVRKPAEAEKQAAEAEA--------EAEAEAIRAKG---LAEAEGKR 344
OmpH pfam03938
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH ...
 553-639 6.96e-03

Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH among others. Skp (OmpH) has been characterized as a molecular chaperone that interacts with unfolded proteins as they emerge in the periplasm from the Sec translocation machinery.


Pssm-ID: 461098 [Multi-domain]  Cd Length: 140  Bit Score: 37.56  E-value: 6.96e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395138 553 LLAESDEAK-VQRAAAGAGGSLRAQVERLRQELQREQRRGDEQRDSFEGERLAWQAE-KEQVIRYQKQLQHNYIQMYRRN 630
Cdd:pfam03938  10 ILEESPEGKaAQAQLEKKFKKRQAELEAKQKELQKLYEELQKDGALLEEEREEKEQElQKKEQELQQLQQKAQQELQKKQ 89


                  ....*....
gi 1720395138 631 RQLEQELQQ 639
Cdd:pfam03938  90 QELLQPIQD 98
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
 402-653 7.62e-03

Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.


Pssm-ID: 464943 [Multi-domain]  Cd Length: 1112  Bit Score: 39.72  E-value: 7.62e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395138  402 EKRQLQDDFAQLLQE-REQLERRCATFEREQRELGPRLEETK--W---------------EVCQKSGEI----SLLKQQL 459
Cdd:pfam15921  360 EARTERDQFSQESGNlDDQLQKLLADLHKREKELSLEKEQNKrlWdrdtgnsitidhlrrELDDRNMEVqrleALLKAMK 439

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395138  460 KESQAEL-------------VQKGSELVA--------LRVALREARA---TLRVSEGRARGLQEAARAREQELEACSQEL 515
Cdd:pfam15921  440 SECQGQMerqmaaiqgknesLEKVSSLTAqlestkemLRKVVEELTAkkmTLESSERTVSDLTASLQEKERAIEATNAEI 519

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395138  516 QRYRQEAERLREKAGHLDAEASGLRDppvppattdpfLLAESDEAKVQRAAAGaggslrAQVERLRQELQR-EQRRGDEQ 594
Cdd:pfam15921  520 TKLRSRVDLKLQELQHLKNEGDHLRN-----------VQTECEALKLQMAEKD------KVIEILRQQIENmTQLVGQHG 582

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1720395138  595 RDSfeGERLAWQAEKEQVIRYQK-QLQHNYIQMYRRNRQL-EQELQQLSLELEARELADLG 653
Cdd:pfam15921  583 RTA--GAMQVEKAQLEKEINDRRlELQEFKILKDKKDAKIrELEARVSDLELEKVKLVNAG 641
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
330-651 7.93e-03

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 39.12  E-value: 7.93e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395138 330 LEGKLRDREAELQQLRDSMDESEatvcqafgarqrrwprERGEDCAAQAQQATQRVQRAqqllqlqvfqlQQEKRQLQDD 409
Cdd:COG4372    64 LEEELEQARSELEQLEEELEELN----------------EQLQAAQAELAQAQEELESL-----------QEEAEELQEE 116

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395138 410 FAQLLQEREQLERRCATFEREQRELgprleetKWEVCQKSGEISLLKQQLKESQAELVQKGSELVALRVALREARATLRV 489
Cdd:COG4372   117 LEELQKERQDLEQQRKQLEAQIAEL-------QSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQALDELL 189

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395138 490 SEGRARGLQEAARAREQELEACSQELQRYRQEAERLREKAGHLDAEASGLRDPPVPPATTDPFLLAESDEAKVQRAAAGA 569
Cdd:COG4372   190 KEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAILV 269

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395138 570 GGSLRAQVERLRQELQREQRR-GDEQRDSFEGERLAWQAEKEQVIRYQKQLQHNYIQMYRRNRQLEQELQQLSLELEARE 648
Cdd:COG4372   270 EKDTEEEELEIAALELEALEEaALELKLLALLLNLAALSLIGALEDALLAALLELAKKLELALAILLAELADLLQLLLVG 349


                  ...
gi 1720395138 649 LAD 651
Cdd:COG4372   350 LLD 352
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
 405-611 8.06e-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: 39.13  E-value: 8.06e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395138 405 QLQDDFAQLLQEREQLE-RRCATFEREQRElgpRLEETKWEVCQKSGEISLLKQQLKESQAELVQKGSELVALRVAL--- 480
Cdd:pfam13868 137 EEQAEWKELEKEEEREEdERILEYLKEKAE---REEEREAEREEIEEEKEREIARLRAQQEKAQDEKAERDELRAKLyqe 213

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395138 481 ----REARATLRVSEGRARGLQEAARAREQELEACSQELQRYRQEAERLREKAghLDAEASGLRdppvppattdpfLLAE 556
Cdd:pfam13868 214 eqerKERQKEREEAEKKARQRQELQQAREEQIELKERRLAEEAEREEEEFERM--LRKQAEDEE------------IEQE 279

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1720395138 557 SDEAKVQRAAAgaggsLRAQVERLRQElQREQRRGDEQRDSFEGERLAWQAEKEQ 611
Cdd:pfam13868 280 EAEKRRMKRLE-----HRRELEKQIEE-REEQRAAEREEELEEGERLREEEAERR 328
CALCOCO1 pfam07888
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ...
 412-590 9.69e-03

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: 462303 [Multi-domain]  Cd Length: 488  Bit Score: 39.11  E-value: 9.69e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395138 412 QLLQEREQLERRCATFEREQRELGPRLEETKWEVCQKSGEISLLKQQLKESQAelvqKGSELVALRVALREARATlrvSE 491
Cdd:pfam07888  56 QREKEKERYKRDREQWERQRRELESRVAELKEELRQSREKHEELEEKYKELSA----SSEELSEEKDALLAQRAA---HE 128

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720395138 492 GRARGLQEAARAREQELEACSQELQRYRQEAERLREKAGHLDAEASGLRDPPVPPATTDPFLLAESDEAKVQRAAAGAGG 571
Cdd:pfam07888 129 ARIRELEEDIKTLTQRVLERETELERMKERAKKAGAQRKEEEAERKQLQAKLQQTEEELRSLSKEFQELRNSLAQRDTQV 208

                         170       180
                  ....*....|....*....|
gi 1720395138 572 -SLRAQVERLRQELQREQRR 590
Cdd:pfam07888 209 lQLQDTITTLTQKLTTAHRK 228
 
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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