|
Name |
Accession |
Description |
Interval |
E-value |
| RBD_KIF20B |
cd21786 |
RAB6 binding domain (RBD) found in kinesin-like protein KIF20B, and similar proteins; KIF20B ... |
26-80 |
4.17e-18 |
|
RAB6 binding domain (RBD) found in kinesin-like protein KIF20B, and similar proteins; KIF20B (also called cancer/testis antigen 90 (CT90), kinesin family member 20B, kinesin-related motor interacting with PIN1, or M-phase phosphoprotein 1 (MPP1)) is a plus-end-directed motor enzyme that is required for completion of cytokinesis. It is required for proper midbody organization and abscission in polarized cortical stem cells. KIF20B plays a role in the regulation of neuronal polarization by mediating the transport of specific cargos. It participates in the mobilization of SHTN1 (shootin 1) and in the accumulation of PIP3 in the growth cone of primary hippocampal neurons in a tubulin and actin-dependent manner. In the developing telencephalon, KIF20B cooperates with SHTN1 to promote both the transition from the multipolar to the bipolar stage and the radial migration of cortical neurons from the ventricular zone toward the superficial layer of the neocortex. KIF20B acts as an oncogene for promoting bladder cancer cell proliferation, apoptosis inhibition, and carcinogenic progression. This model corresponds to a conserved region in KIF20B that shows some sequence similarity to the RAB6 binding domain (RBD) of KIF20A. KIF20A-RBD is a dimer composed of two parallel alpha helices that form a right-handed coiled-coil additionally stabilized by an inter-helical cysteine bridge.
Pssm-ID: 409644 [Multi-domain] Cd Length: 56 Bit Score: 79.06 E-value: 4.17e-18
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 6807925 26 KIREEVTQEFTQYWAQREADFKETLLQEREILEENAERRLAIFKDLVGKCDTREE 80
Cdd:cd21786 1 KIREEVTQEFTELFSEMEKDYSERLEREREILEERAEKRLEIFKNLVNKTAKEEE 55
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
463-737 |
1.27e-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: 72.78 E-value: 1.27e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6807925 463 QIEELEQQIEKLQAEVKGYKDENNRLKEKEHKNQDDLLkEKETLIQQLKEELQEKNVTLDVQIQHVVEGKRALSELTQGV 542
Cdd:TIGR02168 685 KIEELEEKIAELEKALAELRKELEELEEELEQLRKELE-ELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEI 763
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6807925 543 TCYKAKIKELETILETQKVEcshSAKLEQDILEKESIILKLERNLKEFQEHLQDsvkntkdLNVKELKLKEEITQLTNNL 622
Cdd:TIGR02168 764 EELEERLEEAEEELAEAEAE---IEELEAQIEQLKEELKALREALDELRAELTL-------LNEEAANLRERLESLERRI 833
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6807925 623 QDMKHLLQLKEEEEETNRQETEKLKEELSASSARTQNLKADLQRKEEDYADLKEKLTDAKKQIKQVQKEVSVMRDEDKLL 702
Cdd:TIGR02168 834 AATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSEL 913
|
250 260 270
....*....|....*....|....*....|....*
gi 6807925 703 RIKINELEKKKNQCSQELDMKQRTIQQLKEQLNNQ 737
Cdd:TIGR02168 914 RRELEELREKLAQLELRLEGLEVRIDNLQERLSEE 948
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
464-749 |
2.71e-11 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 68.04 E-value: 2.71e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6807925 464 IEELEQQIEKL--QAEV----KGYKDENNRLKEKEHKNQDDLLKEKETLIQQLKEELQEKNVTLDVQIQH----VVEGKR 533
Cdd:COG1196 195 LGELERQLEPLerQAEKaeryRELKEELKELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAEleaeLEELRL 274
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6807925 534 ALSELTQGVTCYKAKIKELETILETQKVECSHSAKLEQDILEKesiILKLERNLKEFQEHLQDSVKNTKDLNVKELKLKE 613
Cdd:COG1196 275 ELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEER---LEELEEELAELEEELEELEEELEELEEELEEAEE 351
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6807925 614 EITQLTNNLQDMKHLLQLKEEEEETNRQETEKLKEELSASSARTQNLKADLQRKEEDYADLKEKLTDAKKQIKQVQKEVS 693
Cdd:COG1196 352 ELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALA 431
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 6807925 694 VMRDEDKLLRIKINELEKKKNQCSQELDMKQRTIQQLKEQLNNQKVEEAIQQYERA 749
Cdd:COG1196 432 ELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELA 487
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
462-745 |
4.63e-11 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 67.27 E-value: 4.63e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6807925 462 HQIEELEQQIEKLQAEVKGYKDENNRLKEKehknqddlLKEKETLIQQLKEELQEKNVTLDVQIQHVVEGKRALSELTQG 541
Cdd:COG1196 232 LKLRELEAELEELEAELEELEAELEELEAE--------LAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQD 303
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6807925 542 VTCYKAKIKELETILETQKVECshsAKLEQDILEKESIILKLERNLKEFQEHLQDSVKNTKDLNVKELKLKEEITQLTNN 621
Cdd:COG1196 304 IARLEERRRELEERLEELEEEL---AELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEE 380
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6807925 622 LQDMKHLLQLKEEEEETNRQETEKLKEELSASSARTQNLKADLQRKEEDYADLKEKLTDAKKQIKQVQKEVSVMRDEDKL 701
Cdd:COG1196 381 LEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEA 460
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 6807925 702 LRIKINELEKKKNQCSQELDMKQRTIQQLKEQLNNQKVEEAIQQ 745
Cdd:COG1196 461 LLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYE 504
|
|
| RBD_KIF20A-like |
cd21744 |
RAB6 binding domain (RBD) found in kinesin-like proteins KIF20A, KIF20B, and similar proteins; ... |
26-80 |
2.29e-10 |
|
RAB6 binding domain (RBD) found in kinesin-like proteins KIF20A, KIF20B, and similar proteins; This family includes kinesin-like proteins KIF20A and KIF20B. KIF20A (also called GG10_2, mitotic kinesin-like protein 2 (MKlp2), Rab6-interacting kinesin-like protein, or rabkinesin-6) is a mitotic kinesin required for chromosome passenger complex (CPC)-mediated cytokinesis. Following phosphorylation by PLK1 (polo-like kinase 1), it is involved in recruitment of PLK1 to the central spindle. KIF20A interacts with guanosine triphosphate (GTP)-bound forms of RAB6A and RAB6B. It may act as a motor required for the retrograde RAB6 regulated transport of Golgi membranes and associated vesicles along microtubules. KIF20A has a microtubule plus-end-directed motility. KIF20B (also called cancer/testis antigen 90 (CT90), kinesin family member 20B, kinesin-related motor interacting with PIN1, or M-phase phosphoprotein 1 (MPP1)) is a plus-end-directed motor enzyme that is required for completion of cytokinesis. It is required for proper midbody organization and abscission in polarized cortical stem cells. KIF20B plays a role in the regulation of neuronal polarization by mediating the transport of specific cargoes. It participates in the mobilization of SHTN1 and in the accumulation of PIP3 in the growth cone of primary hippocampal neurons in a tubulin and actin-dependent manner. In the developing telencephalon, KIF20B cooperates with SHTN1 to promote both the transition from the multipolar to the bipolar stage and the radial migration of cortical neurons from the ventricular zone toward the superficial layer of the neocortex. This model corresponds to a conserved domain in the KIF20A subfamily, that shows RAB6 binding ability and has been called the RAB6 binding domain (RBD). KIF20A-RBD is a dimer composed of two parallel alpha helices that form a right-handed coiled-coil additionally stabilized by an inter-helical cysteine bridge.
Pssm-ID: 409643 [Multi-domain] Cd Length: 56 Bit Score: 57.08 E-value: 2.29e-10
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 6807925 26 KIREEVTQEFTQYWAQREADFKETLLQEREILEENAERRLAIFKDLVGKCDTREE 80
Cdd:cd21744 1 RIREEVSEEFEEQFALMEEDYEERLENEKEILEERYEKRLEIRKELIKKLSAALE 55
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
540-844 |
3.68e-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: 64.69 E-value: 3.68e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6807925 540 QGVTCYKAKIKELETILEtqkvecshsaKLEQDILEKESIILKLERNLKEFQEHLQDSVKNTKDLNVKELKLKEEITQLT 619
Cdd:TIGR02168 670 SSILERRREIEELEEKIE----------ELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLE 739
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6807925 620 NNLQDMKHLLQLKEEEEETNRQETEKLKEELSASSARTQNLKADLQRKEEDYADLKEKLTDAKKQIKQVQKEVSVMRDED 699
Cdd:TIGR02168 740 AEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEA 819
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6807925 700 KLLRIKINELEKKKNQCSQELDMKQRTIQQLKEQLnnQKVEEAIQQYERACKDLNVKEKIIEDMRMTLEEQEQTQVEQDQ 779
Cdd:TIGR02168 820 ANLRERLESLERRIAATERRLEDLEEQIEELSEDI--ESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELE 897
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 6807925 780 VLEAKLEEVERLATELEKWKEKCNDLETKNNQRSNKEHENNTDVLGKLTNL-QDELQESEQKYNAD 844
Cdd:TIGR02168 898 ELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLSEEySLTLEEAEALENKI 963
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
666-969 |
5.57e-10 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 63.80 E-value: 5.57e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6807925 666 RKEEDYADLKEKLTDAKKQIKQVQKEVsvMRDEDKLLRIKINELEKKKNQCSQELDMKQRTIQQLKEQLN--NQKVEEAI 743
Cdd:COG1196 210 EKAERYRELKEELKELEAELLLLKLRE--LEAELEELEAELEELEAELEELEAELAELEAELEELRLELEelELELEEAQ 287
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6807925 744 QQYERACKDLNVKEKIIEDMRMTLEEQEQTQVEQDQVLEAKLEEVERLATELEKWKEKCNDLETKNNQRSNKEHEnntdv 823
Cdd:COG1196 288 AEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAE----- 362
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6807925 824 lgkltnLQDELQESEQKYNADRKKWLEEKMMLITQAKEAENIRNKEmkkyAEDRERFFKQQNEMEILTAQLTEKDSDLQK 903
Cdd:COG1196 363 ------AEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQL----EELEEAEEALLERLERLEEELEELEEALAE 432
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 6807925 904 WREERDQLVAALEIQLKALISSNVQKDNEIEQLKRIISETSKIETQIMDIKPKRISSADPDKLQTE 969
Cdd:COG1196 433 LEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLE 498
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
464-841 |
7.19e-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: 63.54 E-value: 7.19e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6807925 464 IEELEQQIEKLQAEVKG---YKDENNRLKEKEHknqdDLLKekeTLIQQLKEELQEKNVTLDVQIQHVVEGKRALSELTQ 540
Cdd:TIGR02168 195 LNELERQLKSLERQAEKaerYKELKAELRELEL----ALLV---LRLEELREELEELQEELKEAEEELEELTAELQELEE 267
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6807925 541 GVTCYKAKIKELETILEtqkvecshsaKLEQDILEKESIILKLERNLKEFQEHLQDSVKNTKDLNVKELKLKEEITQLTN 620
Cdd:TIGR02168 268 KLEELRLEVSELEEEIE----------ELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAE 337
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6807925 621 NLQDMKHLLQLKEEEEETNRQETEKLKEELSASSARTQNLKADLQRKEEDYADLKEKLTDAKKQIKQvqkevsvmrdedk 700
Cdd:TIGR02168 338 ELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIER------------- 404
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6807925 701 lLRIKINELEKKKNQCSQEldmkqrtIQQLKEQLNNQKVEEAIQQYERACKDLNVKEKIIEDMRMTLEEQEQTQVEQDQV 780
Cdd:TIGR02168 405 -LEARLERLEDRRERLQQE-------IEELLKKLEEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQA 476
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 6807925 781 LEAKLEEVERLATELEKWKEKCNDLEtkNNQRSNKEHENNTDVLGKLTNLQDELQESEQKY 841
Cdd:TIGR02168 477 LDAAERELAQLQARLDSLERLQENLE--GFSEGVKALLKNQSGLSGILGVLSELISVDEGY 535
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
439-797 |
1.12e-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: 63.16 E-value: 1.12e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6807925 439 FHSSIEAIWEECKEIVKASSKKSHQIEELEQQIEKLQAEVKGYKDENNRLKEKEHKNQDDLLKEKETLIQQLKEELQEkn 518
Cdd:TIGR02169 168 FDRKKEKALEELEEVEENIERLDLIIDEKRQQLERLRREREKAERYQALLKEKREYEGYELLKEKEALERQKEAIERQ-- 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6807925 519 vtLDVQIQHVVEGKRALSELTQGVTCYKAKIKELETILETQKVEcsHSAKLEQDILEKESIILKLERNLKEFQEHLQDSV 598
Cdd:TIGR02169 246 --LASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEE--EQLRVKEKIGELEAEIASLERSIAEKERELEDAE 321
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6807925 599 KNTKDLNVKELKLKEEITQLTNNLQDMKhllqlkeeeeetnrQETEKLKEELSASSARTQNLKADLQRKEEDYADLKEKL 678
Cdd:TIGR02169 322 ERLAKLEAEIDKLLAEIEELEREIEEER--------------KRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDEL 387
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6807925 679 TDAKKQIKQVQKEvsvmrdedkllrikINELEKKKNQCSQELDMKQRTIQQLKEQLnnQKVEEAIQQYERACKDLNVKEK 758
Cdd:TIGR02169 388 KDYREKLEKLKRE--------------INELKRELDRLQEELQRLSEELADLNAAI--AGIEAKINELEEEKEDKALEIK 451
|
330 340 350
....*....|....*....|....*....|....*....
gi 6807925 759 IIEDMRMTLEEQEQTQVEQDQVLEAKLEEVERLATELEK 797
Cdd:TIGR02169 452 KQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQR 490
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
602-938 |
2.83e-08 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 58.41 E-value: 2.83e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6807925 602 KDLNVKELKLKEEITQLTNNLQDMKHLLQLKEEEEETNRQETEKLKEELSASSARTQNLKADLQRKEEDYADLKEKLTDA 681
Cdd:COG1196 235 RELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRREL 314
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6807925 682 KKQIKQVQKEVSVMRDEDKLLRIKINELEKKKNQCSQELDMKQRTIQQLKEQLNN--QKVEEAIQQYERACKDLNVKEKI 759
Cdd:COG1196 315 EERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEaeAELAEAEEELEELAEELLEALRA 394
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6807925 760 IEDMRMTLEEQEQTQVEQDQVLEAKLEEVERLATELEKWKEKCNDLETKNNQRSNKEHENNTDVLGKLTNLQDELQESEQ 839
Cdd:COG1196 395 AAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAAL 474
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6807925 840 KYNADRKKwleekmmlitQAKEAENIRNKEMKKYAEDRERFFKQQNEMEILTAQLTEKDSDLQKWREERDQLVAALEIQL 919
Cdd:COG1196 475 LEAALAEL----------LEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAAL 544
|
330 340
....*....|....*....|....
gi 6807925 920 KALISSNVQKDNE-----IEQLKR 938
Cdd:COG1196 545 AAALQNIVVEDDEvaaaaIEYLKA 568
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
672-937 |
4.96e-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: 57.76 E-value: 4.96e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6807925 672 ADLKEKLTDAKKQIKQVQKEVSVMRDEDklLRIKINELEKKKNQCSQELDMKQRTIQQLKEQLN-----NQKVEEAIQQY 746
Cdd:TIGR02168 209 AEKAERYKELKAELRELELALLVLRLEE--LREELEELQEELKEAEEELEELTAELQELEEKLEelrleVSELEEEIEEL 286
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6807925 747 ERACKDLNVKEKIIEDMRMTLEEQEQTQVEQDQVLEAKLEEVER----LATELEKWKEKCNDLEtknnqrsnkehENNTD 822
Cdd:TIGR02168 287 QKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESkldeLAEELAELEEKLEELK-----------EELES 355
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6807925 823 VLGKLTNLQDELQESEQKYNADRKKWLEEKmmlitqakeaenirnkemKKYAEDRERFFKQQNEMEILTAQLTEKDSDLQ 902
Cdd:TIGR02168 356 LEAELEELEAELEELESRLEELEEQLETLR------------------SKVAQLELQIASLNNEIERLEARLERLEDRRE 417
|
250 260 270
....*....|....*....|....*....|....*.
gi 6807925 903 KWREERDQLVAAL-EIQLKALISSNVQKDNEIEQLK 937
Cdd:TIGR02168 418 RLQQEIEELLKKLeEAELKELQAELEELEEELEELQ 453
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
295-955 |
1.83e-07 |
|
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: 55.83 E-value: 1.83e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6807925 295 NKQIVHFQQELSLSEKKNLTLSKEVQQIQSNYDIAIAELHVQKSKNQEQEEKIMKLSNEIETATRSITNNVSQIKLMHTK 374
Cdd:TIGR02168 238 REELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQ 317
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6807925 375 IDEL-RTLDSVSQISNIDLLNLRDLSNGSEEDNlpnTQLDLLgndylvSKQVKEYRIQEPNRENSFHSSIEAIWEECKEI 453
Cdd:TIGR02168 318 LEELeAQLEELESKLDELAEELAELEEKLEELK---EELESL------EAELEELEAELEELESRLEELEEQLETLRSKV 388
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6807925 454 VKASSKK---SHQIEELEQQIEKLQAEVKGYKDENNRLKEKEHKNQDDLLK----EKETLIQQLKEELQEKNVTLDVQIQ 526
Cdd:TIGR02168 389 AQLELQIaslNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQaeleELEEELEELQEELERLEEALEELRE 468
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6807925 527 HVVEGKRALSELTQGVTCYKAKIKELETILETQK---------------------------------------------- 560
Cdd:TIGR02168 469 ELEEAEQALDAAERELAQLQARLDSLERLQENLEgfsegvkallknqsglsgilgvlselisvdegyeaaieaalggrlq 548
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6807925 561 ---VECSHSAKLEQDILEKESIIL------------KLERNLKEFQEHLQDSVKNTKDLNVKELKLKEEITQL------T 619
Cdd:TIGR02168 549 avvVENLNAAKKAIAFLKQNELGRvtflpldsikgtEIQGNDREILKNIEGFLGVAKDLVKFDPKLRKALSYLlggvlvV 628
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6807925 620 NNLQDMKHLLQLKEEEEETNRQETEKLKEELSASSAR------TQNLKADLQRKEEDYADLKEKLTDAKKQIKQVQKEVS 693
Cdd:TIGR02168 629 DDLDNALELAKKLRPGYRIVTLDGDLVRPGGVITGGSaktnssILERRREIEELEEKIEELEEKIAELEKALAELRKELE 708
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6807925 694 VMRDEDKLLRIKINELEKKKNQCSQELDMKQRTIQQLKEQLNNQKVE-----EAIQQYERACKDLNVKEKIIEDMRMTLE 768
Cdd:TIGR02168 709 ELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKElteleAEIEELEERLEEAEEELAEAEAEIEELE 788
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6807925 769 EQEQTQVEQDQVLEAKL----EEVERLATELEKWKEKCNDLET------KNNQRSNKEHENNTDVLGKLTNLQDELQESE 838
Cdd:TIGR02168 789 AQIEQLKEELKALREALdelrAELTLLNEEAANLRERLESLERriaateRRLEDLEEQIEELSEDIESLAAEIEELEELI 868
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6807925 839 QKYNADRKKWLEEKMMLITQAKEAENIRNKEMKKYAEDRERFFKQQNEMEILTAQLTEKDSDLQKWREERDQLVAAL--- 915
Cdd:TIGR02168 869 EELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLsee 948
|
730 740 750 760
....*....|....*....|....*....|....*....|.
gi 6807925 916 -EIQLKALISSNVQKDNEIEQLKRiisETSKIETQIMDIKP 955
Cdd:TIGR02168 949 ySLTLEEAEALENKIEDDEEEARR---RLKRLENKIKELGP 986
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
459-888 |
1.90e-07 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 55.46 E-value: 1.90e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6807925 459 KKSHQIEELEQQIEKLQAEVKGYKDENNRLKEKEHKNQDdlLKEKETLIQQLKEELqeKNVTLDVQIQHVVEGKRALSEL 538
Cdd:PRK03918 328 ERIKELEEKEERLEELKKKLKELEKRLEELEERHELYEE--AKAKKEELERLKKRL--TGLTPEKLEKELEELEKAKEEI 403
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6807925 539 TQGVTCYKAKIKELETILETQK--VECSHSAKLEQDILEKESIILKLERNLKEFQEHLQDSVKNTKDLNVKELKLKEEIT 616
Cdd:PRK03918 404 EEEISKITARIGELKKEIKELKkaIEELKKAKGKCPVCGRELTEEHRKELLEEYTAELKRIEKELKEIEEKERKLRKELR 483
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6807925 617 QLTNNLQDMKHLLQLKEEEEETNRqetekLKEELSASSARtqnlkaDLQRKEEDYADLKEKLTDAKKQIKQVQKEVSvmr 696
Cdd:PRK03918 484 ELEKVLKKESELIKLKELAEQLKE-----LEEKLKKYNLE------ELEKKAEEYEKLKEKLIKLKGEIKSLKKELE--- 549
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6807925 697 dedkllriKINELEKKKNQCSQELDMKQRTIQQLKEQLNN------QKVEEAIQQYERACKDLNVKEKIIEDMRMTLEEQ 770
Cdd:PRK03918 550 --------KLEELKKKLAELEKKLDELEEELAELLKELEElgfesvEELEERLKELEPFYNEYLELKDAEKELEREEKEL 621
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6807925 771 EQTQVEqdqvLEAKLEEVERLATELEKWKEKCNDLETKNNQRSNKEHENNTDVLGK----LTNLQDELQESEQKYNADRK 846
Cdd:PRK03918 622 KKLEEE----LDKAFEELAETEKRLEELRKELEELEKKYSEEEYEELREEYLELSRelagLRAELEELEKRREEIKKTLE 697
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 6807925 847 KWLEEKMMLITQAKEAENIrNKEMKKYAEDRERFFKQQNEME 888
Cdd:PRK03918 698 KLKEELEEREKAKKELEKL-EKALERVEELREKVKKYKALLK 738
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
440-754 |
2.69e-07 |
|
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: 55.07 E-value: 2.69e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6807925 440 HSSIEAIWEECKEIVKASSKKSHQIEELEQQIEKLQAEVKGYKDENNRLKEKehknqddlLKEKETLIQQLKEELQEKNV 519
Cdd:TIGR02169 715 SRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEAR--------IEELEEDLHKLEEALNDLEA 786
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6807925 520 TLDVQIQHVVEGKraLSELTQGVTCYKAKIKELETILETQKVEcshSAKLEQDILEKESIILKLERNLKEFQEHLQDSVK 599
Cdd:TIGR02169 787 RLSHSRIPEIQAE--LSKLEEEVSRIEARLREIEQKLNRLTLE---KEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNG 861
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6807925 600 NTKDLNVKELKLKEEITQLTNNLQDMKhllqlkeeeeetnrQETEKLKEELSASSARTQNLKADLQRKEEDYADLKEKLT 679
Cdd:TIGR02169 862 KKEELEEELEELEAALRDLESRLGDLK--------------KERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLE 927
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 6807925 680 DAKKQIKQVQKEVSVMrdedkllrIKINELEKKKNQCSQELDMKQRTIQQLkEQLNNQkveeAIQQYERACKDLN 754
Cdd:TIGR02169 928 ALEEELSEIEDPKGED--------EEIPEEELSLEDVQAELQRVEEEIRAL-EPVNML----AIQEYEEVLKRLD 989
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
126-736 |
2.86e-07 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 55.03 E-value: 2.86e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6807925 126 KRENESDSLIQELETSNKKIITQNQRIKELINIIDQKEDTINEFQNlkshMENTFKCNDKADTSSLIINNKLICNETVEV 205
Cdd:TIGR04523 30 KQDTEEKQLEKKLKTIKNELKNKEKELKNLDKNLNKDEEKINNSNN----KIKILEQQIKDLNDKLKKNKDKINKLNSDL 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6807925 206 PK-DSKSKICSERKRVNENELQQDEPPAKKGSIHVSSAITEDQKKSEEVRPNIAEIEDIRVLQENnegLRAFLLTIENEL 284
Cdd:TIGR04523 106 SKiNSEIKNDKEQKNKLEVELNKLEKQKKENKKNIDKFLTEIKKKEKELEKLNNKYNDLKKQKEE---LENELNLLEKEK 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6807925 285 KNEKEEKAELNKQIVHFQQELSLSEKKN----------LTLSKEVQQIQSNYDIAIAELHVQKSKNQEQEEKIMKLSNEI 354
Cdd:TIGR04523 183 LNIQKNIDKIKNKLLKLELLLSNLKKKIqknkslesqiSELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQ 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6807925 355 ETATRSITNNVSQIKLMHTKIDELRtlDSVSQISNidllNLRDLSNGSEEDNLPNTQLDLLGNDYLVSkQVKEYRIQEPN 434
Cdd:TIGR04523 263 NKIKKQLSEKQKELEQNNKKIKELE--KQLNQLKS----EISDLNNQKEQDWNKELKSELKNQEKKLE-EIQNQISQNNK 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6807925 435 RENSFHSSIEAIWEECKEIVKASSKKSHQIEELEQQIEKLQAEVKGYKDENNRLK------EKEHKNQDDLLKEKETLIQ 508
Cdd:TIGR04523 336 IISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLEsqindlESKIQNQEKLNQQKDEQIK 415
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6807925 509 QLKEELQEKNVTLDVQIQHVVEGKRALSELTQGVTCYKAKIKELETILETQKVECS-----------HSAKLEQDILEKE 577
Cdd:TIGR04523 416 KLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKvlsrsinkikqNLEQKQKELKSKE 495
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6807925 578 SIILKLERNLKEFQEHLQDSVKNTKDLNVKELKLKEEITQLTNNLQDMKHLL---------QLKEEEEETNRQETEKLKE 648
Cdd:TIGR04523 496 KELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDELnkddfelkkENLEKEIDEKNKEIEELKQ 575
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6807925 649 ELSASSARTQNLKADLQRKEEDYADLKEKLTDAKKQIKQVQKEVSVMRDEDKLLRIKINELEKKKNQCSQELDMKQRTIQ 728
Cdd:TIGR04523 576 TQKSLKKKQEEKQELIDQKEKEKKDLIKEIEEKEKKISSLEKELEKAKKENEKLSSIIKNIKSKKNKLKQEVKQIKETIK 655
|
....*...
gi 6807925 729 QLKEQLNN 736
Cdd:TIGR04523 656 EIRNKWPE 663
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
410-954 |
3.68e-07 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 54.68 E-value: 3.68e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6807925 410 TQLDLLGNDYLVSKQVKEYRIQEPNRENSFHSSIEAIWEECKEIVKASSKKSHQIEELEQQIEKLQAEVKGYKDENNRLK 489
Cdd:PRK03918 155 LGLDDYENAYKNLGEVIKEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELE 234
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6807925 490 ----------------EKEHKNQDDLLKEKETLIQQLKEELQ--EKNVTLDVQIQHVVEGKRALSELTQGvtcYKAKIKE 551
Cdd:PRK03918 235 elkeeieelekeleslEGSKRKLEEKIRELEERIEELKKEIEelEEKVKELKELKEKAEEYIKLSEFYEE---YLDELRE 311
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6807925 552 LETILETQKVECSHSAKLEQDILEKESIILKLERNLKEFQ---EHLQDSVKNTKDLNVKELKLKEEITQLTN-NLQDMKH 627
Cdd:PRK03918 312 IEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKELEkrlEELEERHELYEEAKAKKEELERLKKRLTGlTPEKLEK 391
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6807925 628 LLQLKEEEEETNRQETEKLKEELSASSARTQNLKADLQR---------------KEEDYADLKEKLTdakKQIKQVQKEV 692
Cdd:PRK03918 392 ELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEElkkakgkcpvcgrelTEEHRKELLEEYT---AELKRIEKEL 468
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6807925 693 SVMRDEDKLLRIKINELEKKKNQCSQELDMKQrTIQQLKE------QLNNQKVEEAIQQYERACKDLNVKEKIIEDMRMT 766
Cdd:PRK03918 469 KEIEEKERKLRKELRELEKVLKKESELIKLKE-LAEQLKEleeklkKYNLEELEKKAEEYEKLKEKLIKLKGEIKSLKKE 547
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6807925 767 LEEQEQTQVEQDqVLEAKLEEVERLATELEKWKEKCNDLETKNNQRSNKEHENNTDVLGKLTNLQDELQESEQKYNADRK 846
Cdd:PRK03918 548 LEKLEELKKKLA-ELEKKLDELEEELAELLKELEELGFESVEELEERLKELEPFYNEYLELKDAEKELEREEKELKKLEE 626
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6807925 847 KWLEEKMMLITQAKEAENIRNK-EMKKYAEDRERFFKQQNEMEILTAQLTEKDSDLQKWREERDQLVAALEiQLKALISS 925
Cdd:PRK03918 627 ELDKAFEELAETEKRLEELRKElEELEKKYSEEEYEELREEYLELSRELAGLRAELEELEKRREEIKKTLE-KLKEELEE 705
|
570 580
....*....|....*....|....*....
gi 6807925 926 NVQKDNEIEQLKRIISETSKIETQIMDIK 954
Cdd:PRK03918 706 REKAKKELEKLEKALERVEELREKVKKYK 734
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
463-922 |
4.27e-07 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 54.56 E-value: 4.27e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6807925 463 QIEELEQQIEKLQAEVKGYKDENNRLKEKEhKNQDDLLKEKETLIQQLKEELQEKNVTLDVQIQHVVEGKRALSELTQGV 542
Cdd:COG1196 317 RLEELEEELAELEEELEELEEELEELEEEL-EEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAA 395
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6807925 543 TCYKAKIKELETILETQKVEcshSAKLEQDILEKESIILKLERNLKEFQEHLQDSVKNTKDLNVKELKLKEEITQLTNNL 622
Cdd:COG1196 396 AELAAQLEELEEAEEALLER---LERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEA 472
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6807925 623 QDMKHLLQLKEEEEETNRQETEKLKE-----ELSASSARTQNLKADLQRKEEDYADLKEKLTDAKKQIKQV--QKEVSVM 695
Cdd:COG1196 473 ALLEAALAELLEELAEAAARLLLLLEaeadyEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAAlaAALQNIV 552
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6807925 696 RDEDKLLRIKINELEKKKNQCSQELDM-KQRTIQQLKEQLNNQKVEEAIQQYERACKDLNVKEKIIED---MRMTLEEQE 771
Cdd:COG1196 553 VEDDEVAAAAIEYLKAAKAGRATFLPLdKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDtllGRTLVAARL 632
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6807925 772 QTQVEQDQVLEAKLEEVERLATELEKWKEKcndLETKNNQRSNKEHENNTDVLGKLTNLQDELQESEQKYNADRKKWLEE 851
Cdd:COG1196 633 EAALRRAVTLAGRLREVTLEGEGGSAGGSL---TGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEEREL 709
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 6807925 852 KMMLITQAKEAENIRNKEMKKYAEDRERFFKQQNEMEILTAQLTEKDSDLQKWREERDQLvAALEIQLKAL 922
Cdd:COG1196 710 AEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELEREL-ERLEREIEAL 779
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
463-807 |
4.99e-07 |
|
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: 54.30 E-value: 4.99e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6807925 463 QIEELEQQIEKLQAEVKGYKDENNRLkEKEHKNQDDLLKEKETLIQQLKEELQEKNVTLDVQIQHVVEGKRALSELTQGV 542
Cdd:TIGR02169 675 ELQRLRERLEGLKRELSSLQSELRRI-ENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEI 753
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6807925 543 TCYKAKIKELETILEtQKVECSHSAKLEQDILEKE---SIILKLERNLKEFQEHLQDSVKNTKDLNVKELKLKEEITQLT 619
Cdd:TIGR02169 754 ENVKSELKELEARIE-ELEEDLHKLEEALNDLEARlshSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLE 832
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6807925 620 NNLQDmkhllqlKEEEEETNRQETEKLKEELSASSARTQNLKADLQRKEEDYADLKEKLTDAKKQIKQVQKEVSvmrded 699
Cdd:TIGR02169 833 KEIQE-------LQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLR------ 899
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6807925 700 kllrikinELEKKKNQCSQELDMKQRTIQQLKEQLNNQKVEEA-IQQYERACKDLNVKEKIIEDMRMTLEEQEQTQVEQD 778
Cdd:TIGR02169 900 --------ELERKIEELEAQIEKKRKRLSELKAKLEALEEELSeIEDPKGEDEEIPEEELSLEDVQAELQRVEEEIRALE 971
|
330 340
....*....|....*....|....*....
gi 6807925 779 QVLEAKLEEVERLATELEKWKEKCNDLET 807
Cdd:TIGR02169 972 PVNMLAIQEYEEVLKRLDELKEKRAKLEE 1000
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
418-732 |
4.99e-07 |
|
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: 54.30 E-value: 4.99e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6807925 418 DYLVSKQVKEYRIQEPNRENsFHSSIEAIWEECKEIVKASSKKSHQIEELEQQIEKLQAEVKGY-KDENNRLKEKEHKNQ 496
Cdd:TIGR02169 222 EYEGYELLKEKEALERQKEA-IERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLgEEEQLRVKEKIGELE 300
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6807925 497 DDL--LKEKETLIQQLKEELQEKNVTLDVQIQHvvegkralseltqgvtcYKAKIKELETILETQKVEcshSAKLEQDIL 574
Cdd:TIGR02169 301 AEIasLERSIAEKERELEDAEERLAKLEAEIDK-----------------LLAEIEELEREIEEERKR---RDKLTEEYA 360
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6807925 575 EKESIILKLERNLKEFQEHLQDSVKNTKDLNVKELKLKEEITQLTNNLqdmkhllqlkeeeeetnrqetEKLKEELSASS 654
Cdd:TIGR02169 361 ELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKREL---------------------DRLQEELQRLS 419
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6807925 655 ARTQNLKADLQRKEEDYADLKEKLTDAKKQIKQVQKEVSVMRD-----EDKLLRIK--INELEKKKNQCSQELDMKQRTI 727
Cdd:TIGR02169 420 EELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAAdlskyEQELYDLKeeYDRVEKELSKLQRELAEAEAQA 499
|
....*
gi 6807925 728 QQLKE 732
Cdd:TIGR02169 500 RASEE 504
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
43-897 |
1.20e-06 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 53.05 E-value: 1.20e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6807925 43 EADFKETLLQEREILEENAERRLAIFKDLVGKCDTREEAAKDICATKVETEEATACLELKFNQIKAELAKTKGELIKTKE 122
Cdd:pfam02463 164 GSRLKRKKKEALKKLIEETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEYLLYLDYLKLNEERIDLLQ 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6807925 123 ELKKRENESDSLIQELETSNKKIITQNQRIKELINIIDQKEDTINEFQNLKshmentfkCNDKADTSSLIINNKLICNET 202
Cdd:pfam02463 244 ELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKE--------EEELKSELLKLERRKVDDEEK 315
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6807925 203 VEVPKDSKSKICSERKRVNENELQQDEPPAKKGSIHVSSAITEDQKKSEEVRPNIAEIEDIRVLQENNEGLRAFLLTIEN 282
Cdd:pfam02463 316 LKESEKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEE 395
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6807925 283 ELKNEKEEKAELNKQIVHFQQELSLSEKKNLTLSKEVQQIQSnyDIAIAELHVQKSKNQEQEEKIMKLSNEIETATRSIT 362
Cdd:pfam02463 396 ELELKSEEEKEAQLLLELARQLEDLLKEEKKEELEILEEEEE--SIELKQGKLTEEKEELEKQELKLLKDELELKKSEDL 473
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6807925 363 NNVSQIKLMHTKIDELRTLDSVsqisniDLLNLRDLSNGSEEDNLPNTQLDLLGNDyLVSKQVKEYRIQEPNRENSFHSS 442
Cdd:pfam02463 474 LKETQLVKLQEQLELLLSRQKL------EERSQKESKARSGLKVLLALIKDGVGGR-IISAHGRLGDLGVAVENYKVAIS 546
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6807925 443 IEAIWEECKEIVKASSKKSHQIEELEQQIEKLQAEVKGYKDENNRLKEKEHKNQDDLLKEKETLIQQLKEELQEKNVTLD 522
Cdd:pfam02463 547 TAVIVEVSATADEVEERQKLVRALTELPLGARKLRLLIPKLKLPLKSIAVLEIDPILNLAQLDKATLEADEDDKRAKVVE 626
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6807925 523 VQIQHVVEGKRALSELTQGVTCYKAKI-------KELETILETQKVECSHSAKLEQDILEKESIILKLERNLKEFQEHLQ 595
Cdd:pfam02463 627 GILKDTELTKLKESAKAKESGLRKGVSleeglaeKSEVKASLSELTKELLEIQELQEKAESELAKEEILRRQLEIKKKEQ 706
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6807925 596 DSVKNTKDLNVKELKLKEEITQLTNNLQDMKHLLQLKEEEEETNRQETEKLKEELSASSARTQNLKADLQRKEEDYADLK 675
Cdd:pfam02463 707 REKEELKKLKLEAEELLADRVQEAQDKINEELKLLKQKIDEEEEEEEKSRLKKEEKEEEKSELSLKEKELAEEREKTEKL 786
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6807925 676 EKLTDAKKQIKQVQKEVSVMRDEDKLLRIKINELEKKKNQCSQELDMKQRTIQQLKEQLNNQKvEEAIQQYERACKDLNV 755
Cdd:pfam02463 787 KVEEEKEEKLKAQEEELRALEEELKEEAELLEEEQLLIEQEEKIKEEELEELALELKEEQKLE-KLAEEELERLEEEITK 865
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6807925 756 KEKIIEDMRMTLEEQEQTQVEQDQVLEAKLEEVERLATELEKWKEKCNDLETKNNQRSNKEHENNTDVLGKLTNLQDELQ 835
Cdd:pfam02463 866 EELLQELLLKEEELEEQKLKDELESKEEKEKEEKKELEEESQKLNLLEEKENEIEERIKEEAEILLKYEEEPEELLLEEA 945
|
810 820 830 840 850 860
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 6807925 836 ESEQKYNADRKKWLEEKMMLITQAKEAENIRNKEMKKYAEDRERFFKQQNEMEILTAQLTEK 897
Cdd:pfam02463 946 DEKEKEENNKEEEEERNKRLLLAKEELGKVNLMAIEEFEEKEERYNKDELEKERLEEEKKKL 1007
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
463-685 |
3.29e-06 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 51.17 E-value: 3.29e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6807925 463 QIEELEQQIEKLQAEVKGYKDENNRLKEK------EHKNQDDLLKEKETLIQQLKEELQEKNVTLDVQIQHVVEgkrALS 536
Cdd:PHA02562 182 QIQTLDMKIDHIQQQIKTYNKNIEEQRKKngeniaRKQNKYDELVEEAKTIKAEIEELTDELLNLVMDIEDPSA---ALN 258
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6807925 537 ELTQGVTCYKAKIKELETILETQKvECSHSAKLEQDILEKESIILKLERNLKEFQEHLQDSVKNTKDLNVKElklkEEIT 616
Cdd:PHA02562 259 KLNTAAAKIKSKIEQFQKVIKMYE-KGGVCPTCTQQISEGPDRITKIKDKLKELQHSLEKLDTAIDELEEIM----DEFN 333
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 6807925 617 QLTNNLQDMKHLLQLKEEEEETNRQETEKLKEELSASSARTQNLKADLQRKEEDYADLKEKLTDAKKQI 685
Cdd:PHA02562 334 EQSKKLLELKNKISTNKQSLITLVDKAKKVKAAIEELQAEFVDNAEELAKLQDELDKIVKTKSELVKEK 402
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
434-715 |
3.53e-06 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 51.60 E-value: 3.53e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6807925 434 NRENSFHSSIEAIWEECKEIVKASSKKSHQIEELEQQIEKLqaevkgyKDENNRLKEKEHKNQDDLLkEKETLIQQLKEE 513
Cdd:TIGR02168 232 LRLEELREELEELQEELKEAEEELEELTAELQELEEKLEEL-------RLEVSELEEEIEELQKELY-ALANEISRLEQQ 303
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6807925 514 LQEKNVTLDVQIQHVVEGKRALSELTQGVTCYKAKIKELETILETQKVECshsAKLEQDILEKESIILKLERNLKEFQEH 593
Cdd:TIGR02168 304 KQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEEL---ESLEAELEELEAELEELESRLEELEEQ 380
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6807925 594 LQDSVKNTKDLNVKELKLKEEITQLTNNLQDMKH-LLQLKEEEEETNRQETEKLKEELSASSARTQNLKADLQrkeEDYA 672
Cdd:TIGR02168 381 LETLRSKVAQLELQIASLNNEIERLEARLERLEDrRERLQQEIEELLKKLEEAELKELQAELEELEEELEELQ---EELE 457
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 6807925 673 DLKEKLTDAKKQIKQVQKEVSVMRDEDKLLRIKINELEKKKNQ 715
Cdd:TIGR02168 458 RLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQEN 500
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
645-847 |
4.55e-06 |
|
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: 50.53 E-value: 4.55e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6807925 645 KLKEELSASSARTQNLKADLQRKEEDYADLKEKLTDAKKQIKQVQKEVSVMRDEDKLLRIKINELEKKKNQCSQELDMKQ 724
Cdd:COG4942 31 QLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELAELL 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6807925 725 RTIQQLKEQ------LNNQKVEEAIQQYERACKDLNVKEKIIEDMRMT---LEEQEQTQVEQDQVLEAKLEEVERLATEL 795
Cdd:COG4942 111 RALYRLGRQpplallLSPEDFLDAVRRLQYLKYLAPARREQAEELRADlaeLAALRAELEAERAELEALLAELEEERAAL 190
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 6807925 796 EKWKEKCNDLETKNNQRSNKEHENNTDVLGKLTNLQDELQESEQKYNADRKK 847
Cdd:COG4942 191 EALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAER 242
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
234-552 |
4.83e-06 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 51.21 E-value: 4.83e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6807925 234 KGSIHVSSAITEDQKKSEEVRPNIAEIE-DIRVLQENNEGLRAFLLTIENELKNEKEEKAELNKQIVHFQQELSLSEKKN 312
Cdd:TIGR02168 663 GGSAKTNSSILERRREIEELEEKIEELEeKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEV 742
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6807925 313 LTLSKEVQQIQSNYDIAIAELHVQKSKNQEQEEKIMKLSNEIETATRSITNNVSQIKLMHTKIDELRtldsvsqiSNIDL 392
Cdd:TIGR02168 743 EQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELR--------AELTL 814
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6807925 393 LNLRDLSNGSEEDNLPNTQLDLLGNDYLVSKQVKEYR--IQEPNRE-NSFHSSIEAIWEECKEIVKASSKKSHQIEELEQ 469
Cdd:TIGR02168 815 LNEEAANLRERLESLERRIAATERRLEDLEEQIEELSedIESLAAEiEELEELIEELESELEALLNERASLEEALALLRS 894
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6807925 470 QIEKLQAEVKGYKDENNRLKEKEHKNQDDLLKEKETL------IQQLKEELQEK-NVTLDVQIQHVVEGKRALSELTQGV 542
Cdd:TIGR02168 895 ELEELSEELRELESKRSELRRELEELREKLAQLELRLeglevrIDNLQERLSEEySLTLEEAEALENKIEDDEEEARRRL 974
|
330
....*....|
gi 6807925 543 TCYKAKIKEL 552
Cdd:TIGR02168 975 KRLENKIKEL 984
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
672-956 |
8.15e-06 |
|
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: 50.45 E-value: 8.15e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6807925 672 ADLKEKLTDAKKQIKQVQKEVSVMRDEDKLLRIKINELEKKKNQCSQELDMKQRtIQQLKEQLNNQKVEEAIQQYERACK 751
Cdd:TIGR02169 166 AEFDRKKEKALEELEEVEENIERLDLIIDEKRQQLERLRREREKAERYQALLKE-KREYEGYELLKEKEALERQKEAIER 244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6807925 752 DLNVKEKIIEDMRMTLEEQEQTQVEQDQVLEAKLEEVERLAT-ELEKWKEKCNDLETKNNQRSNKEHENNTDvlgkltnl 830
Cdd:TIGR02169 245 QLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEeEQLRVKEKIGELEAEIASLERSIAEKERE-------- 316
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6807925 831 QDELQESEQKYNADRKKWLEEKMMLITQAKEAENIRNKEMKKYAEDRErffkqqnEMEILTAQLTEKDSDLQKWREERDQ 910
Cdd:TIGR02169 317 LEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKE-------ELEDLRAELEEVDKEFAETRDELKD 389
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 6807925 911 LVAALEIQLKALISSNVQKDNEIEQLKRIISETSKIETQIMDIKPK 956
Cdd:TIGR02169 390 YREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAK 435
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
427-984 |
1.34e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 49.75 E-value: 1.34e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6807925 427 EYRIQEPNRENSFHSSIEAIWEECKEIVKASSKKSHQIEELEQQIEKLQAEVKGYKDENNRLKEKEHKNQDDllkeKETL 506
Cdd:PTZ00121 1080 DFDAKEDNRADEATEEAFGKAEEAKKTETGKAEEARKAEEAKKKAEDARKAEEARKAEDARKAEEARKAEDA----KRVE 1155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6807925 507 IQQLKEELQEKNVTLDVQIQHVVEGKRALSELTQGVTCYKA----------------------KIKELETILETQKVECS 564
Cdd:PTZ00121 1156 IARKAEDARKAEEARKAEDAKKAEAARKAEEVRKAEELRKAedarkaeaarkaeeerkaeearKAEDAKKAEAVKKAEEA 1235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6807925 565 HSAKLEQDILEKE---SIILKLERNLKEFQEHLQDSVKNTKDLNVKELKLKEEITQL--TNNLQDMKHLLQLKEEEEETN 639
Cdd:PTZ00121 1236 KKDAEEAKKAEEErnnEEIRKFEEARMAHFARRQAAIKAEEARKADELKKAEEKKKAdeAKKAEEKKKADEAKKKAEEAK 1315
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6807925 640 RQETEKLKEELSASSARTQNLKADLQRKEEDYADLKEKltDAKKQIKQVQKEVSVMRDEDKLLRIKINELEKKKNQCSQE 719
Cdd:PTZ00121 1316 KADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAE--AAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKA 1393
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6807925 720 LDMKQRTIQQLKEQLNNQKVEEAIQQYERACKDLNVKEKIIEDMRMTLEEQEQTQVEQDQVLEAKLEEVERLATELEKWK 799
Cdd:PTZ00121 1394 DEAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKAD 1473
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6807925 800 E-KCNDLETKNNQRSNKEHENNTDVLGKLTNLQDELQESEQKYNADRKKWLEEkmmlitqAKEAENIRNKEMKKYAEDRE 878
Cdd:PTZ00121 1474 EaKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADE-------AKKAEEAKKADEAKKAEEKK 1546
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6807925 879 RFFKQQNEMEILTAQLTEKDSDLQKWREERDQLVAALEIQLKALISSNVQKDNEIEQLKRIISETSKIETQiMDIKPKRI 958
Cdd:PTZ00121 1547 KADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEE-AKIKAEEL 1625
|
570 580
....*....|....*....|....*.
gi 6807925 959 SSADPDKLQTEPLSTSFEISRNKIED 984
Cdd:PTZ00121 1626 KKAEEEKKKVEQLKKKEAEEKKKAEE 1651
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
650-879 |
1.40e-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: 48.99 E-value: 1.40e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6807925 650 LSASSARTQNLKADLQRKEEDYADLKEKLTDAKKQIKQVQKEVSVMRDEDKLLRIKINELEKKKNQCSQELDMKQRTIQQ 729
Cdd:COG4942 15 AAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6807925 730 LKEQLNNQKVEEAIQQYERACKDLNVKEKII---------EDMRMTLEEQEQTQVEQDQVLEAKLEEVERLATELEKWKE 800
Cdd:COG4942 95 LRAELEAQKEELAELLRALYRLGRQPPLALLlspedfldaVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERA 174
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 6807925 801 KCNDLETKNNQRSNkehenntdvlgKLTNLQDELQESEQKYNADRKKWLEEKMMLITQAKEAENIRNKEMKKYAEDRER 879
Cdd:COG4942 175 ELEALLAELEEERA-----------ALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAER 242
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
204-897 |
1.73e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 49.37 E-value: 1.73e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6807925 204 EVPKDSKSKICSERKRVNENELQQDEPPAKKGSIHVSSAITEDQKKSEEVRpniaEIEDIRVLQEnneglraflltienE 283
Cdd:PTZ00121 1234 EAKKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKADELK----KAEEKKKADE--------------A 1295
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6807925 284 LKNEKEEKAELNKQIVHFQQELSLSEKKNLTLSKEVQQIQSNYDIAIAELHVQKSKNQEQEEKIMKLSNEIETATRSITN 363
Cdd:PTZ00121 1296 KKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEE 1375
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6807925 364 NVSQIKLMHTKIDELRTLDSVSQISNIDLLNLRDLSNGSEE----DNLPNTQLDLLGNDYLVSKQVKEYRIQEPNRENSF 439
Cdd:PTZ00121 1376 AKKKADAAKKKAEEKKKADEAKKKAEEDKKKADELKKAAAAkkkaDEAKKKAEEKKKADEAKKKAEEAKKADEAKKKAEE 1455
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6807925 440 HSSIEAIWEECKEIVKASSKKSHQIEELEQQIEKLQAEVKGYKDENNRLKEKEHKNQDDLLKEKEtliQQLKEELQEKNV 519
Cdd:PTZ00121 1456 AKKAEEAKKKAEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEE---AKKADEAKKAEE 1532
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6807925 520 TLDVQIQHVVEGKRALSELTqgvtcykaKIKELETILETQKVECSHSAKLEQDILEKESIILKL--ERNLKEFQEHLQDS 597
Cdd:PTZ00121 1533 AKKADEAKKAEEKKKADELK--------KAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKaeEARIEEVMKLYEEE 1604
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6807925 598 VKNTKDLNVKELKLKEEITQLTNNLQDMKHLLQLKEEEEETNRQETEKLKEElSASSARTQNLKADLQRKEEDYADLKEK 677
Cdd:PTZ00121 1605 KKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAE-EENKIKAAEEAKKAEEDKKKAEEAKKA 1683
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6807925 678 LTDAKKQIKQVQKEVSVMRDEDKlLRIKINELEKKKNQCSQELDMKQRTIQQLKeqlnnQKVEEAIQQYERACKDLNVKE 757
Cdd:PTZ00121 1684 EEDEKKAAEALKKEAEEAKKAEE-LKKKEAEEKKKAEELKKAEEENKIKAEEAK-----KEAEEDKKKAEEAKKDEEEKK 1757
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6807925 758 KIIEDMRMTLEEQEQTQVEQDQVLEAKLEEVERLATELEKWKEKCNDLETKNNQRSNKEhenNTDVLgkltNLQDELQES 837
Cdd:PTZ00121 1758 KIAHLKKEEEKKAEEIRKEKEAVIEEELDEEDEKRRMEVDKKIKDIFDNFANIIEGGKE---GNLVI----NDSKEMEDS 1830
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 6807925 838 EQKYNADRKKWLEEKMMLITQAKEAENIRNKEMKKYAED--RERFFKQQNEMEILTAQLTEK 897
Cdd:PTZ00121 1831 AIKEVADSKNMQLEEADAFEKHKFNKNNENGEDGNKEADfnKEKDLKEDDEEEIEEADEIEK 1892
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
313-916 |
2.86e-05 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 48.39 E-value: 2.86e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6807925 313 LTLSKEVQQIQSNYdiAIAELHVQKSKNQEQEEKIMKLSNEIETATRsitnnvsQIKLMHTKIDELRTldsvsqisniDL 392
Cdd:COG1196 216 RELKEELKELEAEL--LLLKLRELEAELEELEAELEELEAELEELEA-------ELAELEAELEELRL----------EL 276
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6807925 393 LNLRDLSNgseednlpntqldllgndylvSKQVKEYRIQepnrensfhSSIEAIWEECKEIVKASSKKSHQIEELEQQIE 472
Cdd:COG1196 277 EELELELE---------------------EAQAEEYELL---------AELARLEQDIARLEERRRELEERLEELEEELA 326
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6807925 473 KLQAEVKGYKDENNRLKEkEHKNQDDLLKEKETLIQQLKEELQEKNVTLDVQIQHVVEGKRALSELTQGVTCYKAKIKEL 552
Cdd:COG1196 327 ELEEELEELEEELEELEE-ELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEEL 405
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6807925 553 ETILETQKVEcshSAKLEQDILEKESIILKLERNLKEFQEHLQDSVKNTKDLNVKELKLKEEITQLTNNLQDMKHLLQLK 632
Cdd:COG1196 406 EEAEEALLER---LERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAEL 482
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6807925 633 EEEEETNRQETEKLKE-----ELSASSARTQNLKADLQRKEEDYADL--KEKLTDAKKQIKQVQKEVSVMRDEDKLLRIK 705
Cdd:COG1196 483 LEELAEAAARLLLLLEaeadyEGFLEGVKAALLLAGLRGLAGAVAVLigVEAAYEAALEAALAAALQNIVVEDDEVAAAA 562
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6807925 706 INELEKKKNQCSQELDM-KQRTIQQLKEQLNNQKVEEAIQQYERACKDLNVKEKIIED---MRMTLEEQEQTQVEQDQVL 781
Cdd:COG1196 563 IEYLKAAKAGRATFLPLdKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDtllGRTLVAARLEAALRRAVTL 642
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6807925 782 EAKLEEVERLATELEKWKEKcndLETKNNQRSNKEHENNTDVLGKLTNLQDELQESEQKYNADRKKWLEEKMMLITQAKE 861
Cdd:COG1196 643 AGRLREVTLEGEGGSAGGSL---TGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEE 719
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*...
gi 6807925 862 AENIRNKEMKKYAEDRERFFKQQNEMEILTAQLTEKDS---DLQKWREERDQLVAALE 916
Cdd:COG1196 720 ELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPeppDLEELERELERLEREIE 777
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
49-758 |
3.04e-05 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 48.68 E-value: 3.04e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6807925 49 TLLQEREILEENAERRLAIFKDLVGKCDTREEAAKDICAT-KVETEEATACLElkfNQIKAELAKTKGELIKTKEELKKR 127
Cdd:pfam12128 244 TKLQQEFNTLESAELRLSHLHFGYKSDETLIASRQEERQEtSAELNQLLRTLD---DQWKEKRDELNGELSAADAAVAKD 320
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6807925 128 ENESDSLiqeletSNKKIITQNQRIKELINIIDQKEDTINEFQNL-KSHMENTFKCND-KADTSSLIINNKLICNETVEV 205
Cdd:pfam12128 321 RSELEAL------EDQHGAFLDADIETAAADQEQLPSWQSELENLeERLKALTGKHQDvTAKYNRRRSKIKEQNNRDIAG 394
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6807925 206 PKDSKSKICSERKR---VNENELQQDEPPAKkgsihvssaitedqkksEEVRPNIAEIEDIRVLQENNEGLRAFLLTIEN 282
Cdd:pfam12128 395 IKDKLAKIREARDRqlaVAEDDLQALESELR-----------------EQLEAGKLEFNEEEYRLKSRLGELKLRLNQAT 457
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6807925 283 ELKNEKEEKAELNKQIVHFQQELSLSEKKNLTLSKEVQQIQSNYDIA-----IAELHVQKSKNQEQEEKIMkLSNEIETA 357
Cdd:pfam12128 458 ATPELLLQLENFDERIERAREEQEAANAEVERLQSELRQARKRRDQAsealrQASRRLEERQSALDELELQ-LFPQAGTL 536
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6807925 358 TRSITNNVSQIKlmhtkiDELRTLDSVSQISNIDLLNLRDLSNGSEEDNLPNTQLDLLG---NDYLVSKQVKEYRIqepn 434
Cdd:pfam12128 537 LHFLRKEAPDWE------QSIGKVISPELLHRTDLDPEVWDGSVGGELNLYGVKLDLKRidvPEWAASEEELRERL---- 606
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6807925 435 reNSFHSSIEAIWEECKEIVKASSKKSHQIEELEQQIEKLQAEVKGYKDENNRLKEKEHKNQDDLLKEKETLIQQLKEEL 514
Cdd:pfam12128 607 --DKAEEALQSAREKQAAAEEQLVQANGELEKASREETFARTALKNARLDLRRLFDEKQSEKDKKNKALAERKDSANERL 684
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6807925 515 QeknvTLDVQIQHVVEGKRALSELTQGvtcyKAKIKELETILETQKVECSHSAKLEQDILEKESIILKLERNLKEFQEHL 594
Cdd:pfam12128 685 N----SLEAQLKQLDKKHQAWLEEQKE----QKREARTEKQAYWQVVEGALDAQLALLKAAIAARRSGAKAELKALETWY 756
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6807925 595 QDSVKNTKDLNVKELKLKEEITQLTNNL----QDMKHLLQLKEEEEETNRQETEKLKEELSASSARTQNLKADLQRKEEd 670
Cdd:pfam12128 757 KRDLASLGVDPDVIAKLKREIRTLERKIeriaVRRQEVLRYFDWYQETWLQRRPRLATQLSNIERAISELQQQLARLIA- 835
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6807925 671 yadlkekltDAKKQIKQVQKEvsvmRDEDKLLRIKINELEKKknqcsqeLDMKQRTIQQLKEQLNNQKVEEAIQQYERAC 750
Cdd:pfam12128 836 ---------DTKLRRAKLEME----RKASEKQQVRLSENLRG-------LRCEMSKLATLKEDANSEQAQGSIGERLAQL 895
|
....*...
gi 6807925 751 KDLNVKEK 758
Cdd:pfam12128 896 EDLKLKRD 903
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
660-964 |
3.67e-05 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 48.14 E-value: 3.67e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6807925 660 LKADLQRKEEDYADLKEKLTDAKKQIKQVQKEVSVMRDEDKLLRIKINELEKKKNQCSQELDMKQRTIQQLKEQLnnQKV 739
Cdd:TIGR02169 672 EPAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDL--SSL 749
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6807925 740 EEAIQQYERACKDLnvkEKIIEDMRMTLEEqeqtqveqdqvLEAKLEEVERLATElEKWKEKCNDLETKNNQRSNKEhen 819
Cdd:TIGR02169 750 EQEIENVKSELKEL---EARIEELEEDLHK-----------LEEALNDLEARLSH-SRIPEIQAELSKLEEEVSRIE--- 811
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6807925 820 ntdvlGKLTNLQDELQESEQK--YNADRKKWLEEKMMLITQAKEAENIRNKEMKKYAEDRERFFKqqnEMEILTAQLTEK 897
Cdd:TIGR02169 812 -----ARLREIEQKLNRLTLEkeYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELE---ELEAALRDLESR 883
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 6807925 898 DSDLQKWREERDQLVAALEIQLKALISSNVQKDNEIEQLKRIISETSKIETQIMDIKPKRISSADPD 964
Cdd:TIGR02169 884 LGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDEEIPEEE 950
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
464-872 |
7.66e-05 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 46.94 E-value: 7.66e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6807925 464 IEELEQQIEKLQAEVKGYKDENNRLKEKEHKNQDDL------LKEKETLIQQLKEELQEKNVTLDVQIQHVVEGKRALSE 537
Cdd:TIGR04523 206 LKKKIQKNKSLESQISELKKQNNQLKDNIEKKQQEInektteISNTQTQLNQLKDEQNKIKKQLSEKQKELEQNNKKIKE 285
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6807925 538 LTQGVTCYKAKI------------KELETILETQKVECSHS-----------AKLEQDILEKESIILKLERNLKEFQEHL 594
Cdd:TIGR04523 286 LEKQLNQLKSEIsdlnnqkeqdwnKELKSELKNQEKKLEEIqnqisqnnkiiSQLNEQISQLKKELTNSESENSEKQREL 365
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6807925 595 QDSVKNTKDLNVKELKLKEEITQLTNNLQDMKHLLQLKEEEEETNRQETEKLKEELSASSARTQNLKADLQRKEEDYADL 674
Cdd:TIGR04523 366 EEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDL 445
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6807925 675 KEKLTDAKKQIKQVQKEVSVMRDEDKLLRIKINELEKKKNQCSQELDMKQRTIQQLKEQlnNQKVEEAIQQYERACKDLN 754
Cdd:TIGR04523 446 TNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEE--KKELEEKVKDLTKKISSLK 523
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6807925 755 VKEKIIEdmrmtleeqeqtQVEQDQVLEAKLEEVERLATELEKWKEKCNDLETKNNQRSNKEHENNTDVLGKLTNLQDEL 834
Cdd:TIGR04523 524 EKIEKLE------------SEKKEKESKISDLEDELNKDDFELKKENLEKEIDEKNKEIEELKQTQKSLKKKQEEKQELI 591
|
410 420 430
....*....|....*....|....*....|....*...
gi 6807925 835 QESEQKYNADRKKwLEEKMMLITQAKEAENIRNKEMKK 872
Cdd:TIGR04523 592 DQKEKEKKDLIKE-IEEKEKKISSLEKELEKAKKENEK 628
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
309-748 |
9.88e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 46.68 E-value: 9.88e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6807925 309 EKKNLTLSKEVQQIQSNYDIAIAELHVQKSKNQEQEEKIMKLSNEIETATRSITNNVSQIKLMHTKIDELRTLDSVSQIs 388
Cdd:COG4717 52 EKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPL- 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6807925 389 nidllnLRDLSNGSEEDNLPNTQLDLLGNDYlvsKQVKEYRIQEPNRENSFHSSIEAIWEECKEIvkaSSKKSHQIEELE 468
Cdd:COG4717 131 ------YQELEALEAELAELPERLEELEERL---EELRELEEELEELEAELAELQEELEELLEQL---SLATEEELQDLA 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6807925 469 QQIEKLQAEVKGYKDENNRLK-EKEHKNQDDLLKEKETLIQQLKEELQEKNVTL------------DVQIQHVVEGKRAL 535
Cdd:COG4717 199 EELEELQQRLAELEEELEEAQeELEELEEELEQLENELEAAALEERLKEARLLLliaaallallglGGSLLSLILTIAGV 278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6807925 536 SELTQGVTCYKAKIKELETILETQKVECSHSAKLEQDILEKESIILKLERNLKEFQE-----HLQDSVKNTKDLNVKELK 610
Cdd:COG4717 279 LFLVLGLLALLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSpeellELLDRIEELQELLREAEE 358
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6807925 611 LKEEItQLTNNLQDMKHLLQLKEEEEETNRQETEKLKEELSASSARTQNLKADLQRKEE---------DYADLKEKLTDA 681
Cdd:COG4717 359 LEEEL-QLEELEQEIAALLAEAGVEDEEELRAALEQAEEYQELKEELEELEEQLEELLGeleellealDEEELEEELEEL 437
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 6807925 682 KKQIKQVQKEVSVMRDEDKLLRIKINELEKkknqcSQELDMKQRTIQQLKEQLNN------------QKVEEAIQQYER 748
Cdd:COG4717 438 EEELEELEEELEELREELAELEAELEQLEE-----DGELAELLQELEELKAELRElaeewaalklalELLEEAREEYRE 511
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
613-797 |
1.23e-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: 45.91 E-value: 1.23e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6807925 613 EEITQLTNNLQDMKHLLQLKEEEEETNRQETEKLKEELSASSARTQNLKADLQRKEEDYADLKEKLTDAKKQIKQVQKEV 692
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAEL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6807925 693 SVMRDEdklLRIKINELEKKKNQCSQELDMKQRTIQQLKEQLN-----NQKVEEAIQQYERACKDLNVKEKIIEDMRMTL 767
Cdd:COG4942 100 EAQKEE---LAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQylkylAPARREQAEELRADLAELAALRAELEAERAEL 176
|
170 180 190
....*....|....*....|....*....|
gi 6807925 768 EEQEQTQVEQDQVLEAKLEEVERLATELEK 797
Cdd:COG4942 177 EALLAELEEERAALEALKAERQKLLARLEK 206
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
530-874 |
1.50e-04 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 46.20 E-value: 1.50e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6807925 530 EGKRALSELTQGVTCYKAKIKELETILEtqkvecshsaKLEQDILEKESIILKLERNLKefqeHLQDSVKNTKDLNVKEL 609
Cdd:TIGR02168 155 EERRAIFEEAAGISKYKERRKETERKLE----------RTRENLDRLEDILNELERQLK----SLERQAEKAERYKELKA 220
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6807925 610 KLKE-EITQLTNNLQDMKHLLQLKEEEEETNRQETEKLKEELSASSARTQNLKADLQRKEEDYADLKEKLTDAKKQIKQV 688
Cdd:TIGR02168 221 ELRElELALLVLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRL 300
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6807925 689 QKEVSVMRDEDKLLRIKINELEKKKNQCSQELDMKQRTIQQLKEQLN--NQKVEEAIQQYERACKDLNVKEKIIEDMRMT 766
Cdd:TIGR02168 301 EQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEelKEELESLEAELEELEAELEELESRLEELEEQ 380
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6807925 767 LEEQEQTQVEQDQVLEAKLEEVERLATELEKWKEKCNDLETKNNQRSNKEHENNTDVLGKLTNLQDELQESEQKYNADRK 846
Cdd:TIGR02168 381 LETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQAELEELEEELEELQEELERLE 460
|
330 340
....*....|....*....|....*...
gi 6807925 847 KWLEEKMMLITQAKEAENIRNKEMKKYA 874
Cdd:TIGR02168 461 EALEELREELEEAEQALDAAERELAQLQ 488
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
463-937 |
1.64e-04 |
|
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: 46.12 E-value: 1.64e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6807925 463 QIEELEQQIEKLQAEVKGYKDENNRLKEKEHKNQDDllKEKETLIQQLKEELQEKNVTLDVQIQHVvEGKRALSELTQGV 542
Cdd:TIGR00618 450 TAQCEKLEKIHLQESAQSLKEREQQLQTKEQIHLQE--TRKKAVVLARLLELQEEPCPLCGSCIHP-NPARQDIDNPGPL 526
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6807925 543 TCykakikELETILETQKvecshsaKLEQDILEKESIILKLERNLKEFQEHLQDSVKNTKDLNVKELKLKEEITQLTNNL 622
Cdd:TIGR00618 527 TR------RMQRGEQTYA-------QLETSEEDVYHQLTSERKQRASLKEQMQEIQQSFSILTQCDNRSKEDIPNLQNIT 593
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6807925 623 QDMKHLLQLKEEEEETNRQETEKLKEELsassartqNLKADLQRKEEDYADLKEKLTDAKKQIKQVQKEVSVMRDEDKLL 702
Cdd:TIGR00618 594 VRLQDLTEKLSEAEDMLACEQHALLRKL--------QPEQDLQDVRLHLQQCSQELALKLTALHALQLTLTQERVREHAL 665
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6807925 703 RIKINELEKkknqcSQELDMKQRTIQQLKEQLNNQKveEAIQQYERACKDLNVKEKIIEDMRMTLEEQEQTQVEQDQVLE 782
Cdd:TIGR00618 666 SIRVLPKEL-----LASRQLALQKMQSEKEQLTYWK--EMLAQCQTLLRELETHIEEYDREFNEIENASSSLGSDLAARE 738
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6807925 783 AKLEEVERLATELEKWKEKCNDLEtknNQRSNKEHENNTDVLGKLTNLQDELQESEQKYNADRKKWLEEKMMLITQAKEA 862
Cdd:TIGR00618 739 DALNQSLKELMHQARTVLKARTEA---HFNNNEEVTAALQTGAELSHLAAEIQFFNRLREEDTHLLKTLEAEIGQEIPSD 815
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 6807925 863 ENIRNKEMKKYAEDRERFfkqQNEMEILTAQLTEKDSDLQKWREERDQLVAALEIQLKalISSNVQKDNEIEQLK 937
Cdd:TIGR00618 816 EDILNLQCETLVQEEEQF---LSRLEEKSATLGEITHQLLKYEECSKQLAQLTQEQAK--IIQLSDKLNGINQIK 885
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
461-733 |
1.79e-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: 45.14 E-value: 1.79e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6807925 461 SHQIEELEQQIEKLQAEVKGYKDENNRLKEKEHKNQDDLlKEKETLIQQLKEELQEKNvtldvqiqhvvegkRALSELTQ 540
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQL-AALERRIAALARRIRALE--------------QELAALEA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6807925 541 GVTCYKAKIKELETILETQKvecshsakleqdilekesiilklernlKEFQEHLQDSVKNTKDLNVKELKLKEEITQLTN 620
Cdd:COG4942 84 ELAELEKEIAELRAELEAQK---------------------------EELAELLRALYRLGRQPPLALLLSPEDFLDAVR 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6807925 621 NLQDMKHLLQlkeeeeeTNRQETEKLKEELSASSARTQNLKADLQRKEEDYADLKEKLTDAKKQIKQVQKEVSVMRDEDK 700
Cdd:COG4942 137 RLQYLKYLAP-------ARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELA 209
|
250 260 270
....*....|....*....|....*....|...
gi 6807925 701 LLRIKINELEKKKNQCSQELDMKQRTIQQLKEQ 733
Cdd:COG4942 210 ELAAELAELQQEAEELEALIARLEAEAAAAAER 242
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
645-896 |
1.80e-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: 45.83 E-value: 1.80e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6807925 645 KLKEELSASSARTQNLKADL------QRKEEDYAD-LKEKLTDAKKQIKQVQKEVSVMRDEDKLLRIKINELEKKKNQCS 717
Cdd:TIGR02169 671 SEPAELQRLRERLEGLKRELsslqseLRRIENRLDeLSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLE 750
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6807925 718 QELDMKQRTIQQLKEQLnnQKVEEAIQQYERACKDLNVKE-----KIIEDMRMTLEEQEQTQVEQDQVLEAKLEEV---- 788
Cdd:TIGR02169 751 QEIENVKSELKELEARI--EELEEDLHKLEEALNDLEARLshsriPEIQAELSKLEEEVSRIEARLREIEQKLNRLtlek 828
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6807925 789 ERLATELEKWKEKCNDLETKNNQRSNKEHENNTDvLGKLTNLQDELQESEQKYNADRKKWLEEKMMLITQAKEAENIRNK 868
Cdd:TIGR02169 829 EYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGK-KEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEE 907
|
250 260
....*....|....*....|....*...
gi 6807925 869 EMKKYAEDRERFFKQQNEMEILTAQLTE 896
Cdd:TIGR02169 908 LEAQIEKKRKRLSELKAKLEALEEELSE 935
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
448-916 |
3.62e-04 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 45.03 E-value: 3.62e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6807925 448 EECKEIVKASSKKSHQIEELEQQIEKLQAEVKGYKDENNRLKE--KEHKNQ--------DDLLKEKE------TLIQQLK 511
Cdd:PRK02224 237 DEADEVLEEHEERREELETLEAEIEDLRETIAETEREREELAEevRDLRERleeleeerDDLLAEAGlddadaEAVEARR 316
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6807925 512 EELQEKnvtlDVQIQHVVEGKR-ALSELTQGVTCYKAKIKELETILETQKVEcshSAKLEQDILEKESIILKLERNLKEF 590
Cdd:PRK02224 317 EELEDR----DEELRDRLEECRvAAQAHNEEAESLREDADDLEERAEELREE---AAELESELEEAREAVEDRREEIEEL 389
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6807925 591 QEHLQDSVKNTKDLNVKELKLKEEITQLTNNLQDMKHLLQLKEEEEETNRQETEKLKEELSASSART--QNLK-----AD 663
Cdd:PRK02224 390 EEEIEELRERFGDAPVDLGNAEDFLEELREERDELREREAELEATLRTARERVEEAEALLEAGKCPEcgQPVEgsphvET 469
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6807925 664 LQRKEEDYADLKEKLTDAKKQIKQVQKEVSVMRDEDKLLRiKINELEKKKNQCSQELDMKQRTIQQLKEQ---LNNQKVE 740
Cdd:PRK02224 470 IEEDRERVEELEAELEDLEEEVEEVEERLERAEDLVEAED-RIERLEERREDLEELIAERRETIEEKRERaeeLRERAAE 548
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6807925 741 ---EAIQQYERACKdlnvKEKIIEDMRMTLEEQEQTQVEqdqvLEAKLEEVERLATELEKWKEKCNDLETKNNQRSNKEh 817
Cdd:PRK02224 549 leaEAEEKREAAAE----AEEEAEEAREEVAELNSKLAE----LKERIESLERIRTLLAAIADAEDEIERLREKREALA- 619
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6807925 818 ENNTDVLGKLTNLQDELQESEQKYNADRkkwleekmmlITQAKeaenirnkemkkyaEDRERFFKQQNEMEILTAQLTEK 897
Cdd:PRK02224 620 ELNDERRERLAEKRERKRELEAEFDEAR----------IEEAR--------------EDKERAEEYLEQVEEKLDELREE 675
|
490 500 510
....*....|....*....|....*....|...
gi 6807925 898 DSDLQK--------------WREERDQLVAALE 916
Cdd:PRK02224 676 RDDLQAeigaveneleeleeLRERREALENRVE 708
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
781-954 |
5.06e-04 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 44.24 E-value: 5.06e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6807925 781 LEAKLEEVERlatELEKWKEKCNDLETknNQRSNKEHENNTDVLGKLTNLQDELQESEQKYNADRKKwLEEKMMLITQAK 860
Cdd:COG3206 187 LRKELEEAEA---ALEEFRQKNGLVDL--SEEAKLLLQQLSELESQLAEARAELAEAEARLAALRAQ-LGSGPDALPELL 260
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6807925 861 EAENIRNKemkkyaedRERFFKQQNEMEILTAQLTEKDSDLQKWREERDQL-----------VAALEIQLKALISSNVQK 929
Cdd:COG3206 261 QSPVIQQL--------RAQLAELEAELAELSARYTPNHPDVIALRAQIAALraqlqqeaqriLASLEAELEALQAREASL 332
|
170 180
....*....|....*....|....*
gi 6807925 930 DNEIEQLKRIISETSKIETQIMDIK 954
Cdd:COG3206 333 QAQLAQLEARLAELPELEAELRRLE 357
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
781-969 |
5.42e-04 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 44.28 E-value: 5.42e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6807925 781 LEAKLEEVERLATELEKWKEKCNDLETKNNQRSnkehenntdvlGKLTNLQDELQESEQKYNADRKKWLE------EKMM 854
Cdd:TIGR02168 234 LEELREELEELQEELKEAEEELEELTAELQELE-----------EKLEELRLEVSELEEEIEELQKELYAlaneisRLEQ 302
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6807925 855 LITQAKEAENIRNKEMKKYAEDRERFFKQQNEMEILTAQLTEKDSDLQKWREERDQLVAALEIQLKALISSNVQKDNEIE 934
Cdd:TIGR02168 303 QKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLE 382
|
170 180 190
....*....|....*....|....*....|....*
gi 6807925 935 QLKRIISETSKIETQIMdikpKRISSADPDKLQTE 969
Cdd:TIGR02168 383 TLRSKVAQLELQIASLN----NEIERLEARLERLE 413
|
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
611-746 |
6.97e-04 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 43.42 E-value: 6.97e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6807925 611 LKEEIT-------QLTNNLQDMKHLLQLKEEEEETNRQETEKLKEELSASSA---RTQNLKADLQRK----EEDYADLKE 676
Cdd:PRK09039 44 LSREISgkdsaldRLNSQIAELADLLSLERQGNQDLQDSVANLRASLSAAEAersRLQALLAELAGAgaaaEGRAGELAQ 123
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 6807925 677 KLTDAKKQIKQVQKEVSVMRDEDKLLRIKINELEKKKNQCSQELDMKQRTIQQLKEQLN---NQKVEEaIQQY 746
Cdd:PRK09039 124 ELDSEKQVSARALAQVELLNQQIAALRRQLAALEAALDASEKRDRESQAKIADLGRRLNvalAQRVQE-LNRY 195
|
|
| PTZ00108 |
PTZ00108 |
DNA topoisomerase 2-like protein; Provisional |
887-1173 |
7.72e-04 |
|
DNA topoisomerase 2-like protein; Provisional
Pssm-ID: 240271 [Multi-domain] Cd Length: 1388 Bit Score: 43.88 E-value: 7.72e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6807925 887 MEILTAQLTEKDSDLQK---------WREERDQLVAALEiqlkaliSSNVQKDNEIEQLKRIISETSKIETQIMDIKPKR 957
Cdd:PTZ00108 1104 VEKLNAELEKKEKELEKlknttpkdmWLEDLDKFEEALE-------EQEEVEEKEIAKEQRLKSKTKGKASKLRKPKLKK 1176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6807925 958 ISSADPDKLQTEPLSTSFEISRNKIEDGSVVLDSCEVSTENDQSTRFPKPELEIQFTplqpnKMAVKHPGCTTPVTVKIP 1037
Cdd:PTZ00108 1177 KEKKKKKSSADKSKKASVVGNSKRVDSDEKRKLDDKPDNKKSNSSGSDQEDDEEQKT-----KPKKSSVKRLKSKKNNSS 1251
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6807925 1038 KARKRKSNEMEEDLVKCENKKNATPRTNLKFPISDDRNSSVKKEQKVAIRPSS--KKTYSLRSQASIIGVNLATKKKEGT 1115
Cdd:PTZ00108 1252 KSSEDNDEFSSDDLSKEGKPKNAPKRVSAVQYSPPPPSKRPDGESNGGSKPSSptKKKVKKRLEGSLAALKKKKKSEKKT 1331
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 6807925 1116 LQKfgdflqhspsilqskakkiietmSSSKLSNVEASKENVSQPKRAKRKLYTSEISS 1173
Cdd:PTZ00108 1332 ARK-----------------------KKSKTRVKQASASQSSRLLRRPRKKKSDSSSE 1366
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
341-737 |
8.99e-04 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 43.75 E-value: 8.99e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6807925 341 QEQEEKIMKLSNEIETATRSITNNVSQIklmhtkiDELRTLDSVSQISNIDLLNLRDLSNGSEE--DNLPNTQLDLLG-N 417
Cdd:PRK11281 76 DRQKEETEQLKQQLAQAPAKLRQAQAEL-------EALKDDNDEETRETLSTLSLRQLESRLAQtlDQLQNAQNDLAEyN 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6807925 418 DYLVSKQVKEYRIQEPNRENSFHS-SIEAI---WEECKEIVKASSKKSHQIEE--LEQQIEKLQAEVKGykdeNNRLKEK 491
Cdd:PRK11281 149 SQLVSLQTQPERAQAALYANSQRLqQIRNLlkgGKVGGKALRPSQRVLLQAEQalLNAQNDLQRKSLEG----NTQLQDL 224
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6807925 492 EHKnQDDLLKEKetlIQQLKEELQEknvtldvqIQHVVEGKR-ALSELTqgvtcykakIKELETILETQKV--------E 562
Cdd:PRK11281 225 LQK-QRDYLTAR---IQRLEHQLQL--------LQEAINSKRlTLSEKT---------VQEAQSQDEAARIqanplvaqE 283
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6807925 563 CSHSAKLEQDILEKEsiilklERNLKEFQEHLQdsVKNTKD-LNVKELKLKEEITQLTNNLQDMKHLLQLKeeeeetnrq 641
Cdd:PRK11281 284 LEINLQLSQRLLKAT------EKLNTLTQQNLR--VKNWLDrLTQSERNIKEQISVLKGSLLLSRILYQQQ--------- 346
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6807925 642 eteklkeelsassartQNLKADlqrkeedyaDLKEKLTDAKKQIKQVQKEVSVMRDE--------DKLLRIKINELEKK- 712
Cdd:PRK11281 347 ----------------QALPSA---------DLIEGLADRIADLRLEQFEINQQRDAlfqpdayiDKLEAGHKSEVTDEv 401
|
410 420
....*....|....*....|....*
gi 6807925 713 KNQCSQELDMKQRTIQQLKEQLNNQ 737
Cdd:PRK11281 402 RDALLQLLDERRELLDQLNKQLNNQ 426
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
423-937 |
9.52e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 43.59 E-value: 9.52e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6807925 423 KQVKEYRIQEPNRENSFHSSIEAIWEECKEIVKASSKKShQIEELEQQIEKLQ--AEVKGYKDENNRLKEKEHKNQDDLL 500
Cdd:PTZ00121 1284 KKAEEKKKADEAKKAEEKKKADEAKKKAEEAKKADEAKK-KAEEAKKKADAAKkkAEEAKKAAEAAKAEAEAAADEAEAA 1362
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6807925 501 KEKETLIQQLKEELQEKNVTLDVQiqhvVEGKRALSELTQGVTCYKAKIKELETILETQKVECSHSAKLEQ----DILEK 576
Cdd:PTZ00121 1363 EEKAEAAEKKKEEAKKKADAAKKK----AEEKKKADEAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEkkkaDEAKK 1438
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6807925 577 ESIILKLERNLKEFQEHLQDSVKNTKDLNVK----ELKLKEEITQLTNNLQDMKHLLQLKEEEEETNRQETEKLKEELSA 652
Cdd:PTZ00121 1439 KAEEAKKADEAKKKAEEAKKAEEAKKKAEEAkkadEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKA 1518
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6807925 653 SSARtqnlKADLQRKEEDYADLKE-KLTDAKKQIKQVQKEVSVMRDEDKLLRIKINELEKKKNQCSQELDMKQRTIQQLK 731
Cdd:PTZ00121 1519 EEAK----KADEAKKAEEAKKADEaKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARI 1594
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6807925 732 EQLNNQKVEEAIQQYERACKDLNVKEKIIEdmrmtlEEQEQTQVEQDQVLEAKLEEVERLATELEKWKEkcnDLETKNNQ 811
Cdd:PTZ00121 1595 EEVMKLYEEEKKMKAEEAKKAEEAKIKAEE------LKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEE---ENKIKAAE 1665
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6807925 812 RSNKEHENNTdvlgKLTNLQDELQESEQKYNADRKKWLEEKMMLITQAKEAENIRNKEMKKYAEDRERF----FKQQNEM 887
Cdd:PTZ00121 1666 EAKKAEEDKK----KAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIkaeeAKKEAEE 1741
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....
gi 6807925 888 EILTAQLTEKDSD----LQKWREERDQLVAALEIQLKALISSNVQKDNEIEQLK 937
Cdd:PTZ00121 1742 DKKKAEEAKKDEEekkkIAHLKKEEEKKAEEIRKEKEAVIEEELDEEDEKRRME 1795
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
442-795 |
1.01e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 43.51 E-value: 1.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6807925 442 SIEAIWEECKEIVKASSKKSHQIEELEQQIEKLQAEVKGYKDENNRLKEKEHK-----------NQDDLLKEKETLIQQL 510
Cdd:PRK03918 385 TPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKAKGKcpvcgrelteeHRKELLEEYTAELKRI 464
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6807925 511 KEELQEKNVTLDVQIQHVVEGKRALSELTQGVTCYKA--KIKELETILETQKVECSHSAKLEQDILEKESIILKLErnlk 588
Cdd:PRK03918 465 EKELKEIEEKERKLRKELRELEKVLKKESELIKLKELaeQLKELEEKLKKYNLEELEKKAEEYEKLKEKLIKLKGE---- 540
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6807925 589 efQEHLQDSVKNTKDLNVKELKLKEEITQLTNNLQDMKHLLQLKEEEEETNRQETEKLKEELSASSARTQNLKADLQRKE 668
Cdd:PRK03918 541 --IKSLKKELEKLEELKKKLAELEKKLDELEEELAELLKELEELGFESVEELEERLKELEPFYNEYLELKDAEKELEREE 618
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6807925 669 EDYADLKEKLTDAKKQIKQVQKEVSVMRDEDKLLRIKINE-----LEKKKNQCSQELDMKQRTIQQLKEQL-----NNQK 738
Cdd:PRK03918 619 KELKKLEEELDKAFEELAETEKRLEELRKELEELEKKYSEeeyeeLREEYLELSRELAGLRAELEELEKRReeikkTLEK 698
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 6807925 739 VEEAIQQYERACKDLNVKEKIIEDMRmtlEEQEQTQVEQDQVLEAKLEEVERLATEL 795
Cdd:PRK03918 699 LKEELEEREKAKKELEKLEKALERVE---ELREKVKKYKALLKERALSKVGEIASEI 752
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
645-767 |
1.18e-03 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 41.83 E-value: 1.18e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6807925 645 KLKEELSASSARTQNLKADLQRKEEDYADLKEKLTDAKKQIKQV--QKEVSVMRDEDKLLRIKINELEKKKNQCSQELDM 722
Cdd:COG1579 42 ALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVrnNKEYEALQKEIESLKRRISDLEDEILELMERIEE 121
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 6807925 723 KQRTIQQLKEQLNNQK--VEEAIQQYERACKDLNVKEKIIEDMRMTL 767
Cdd:COG1579 122 LEEELAELEAELAELEaeLEEKKAELDEELAELEAELEELEAEREEL 168
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
463-694 |
1.29e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 42.51 E-value: 1.29e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6807925 463 QIEELEQQIEKLQAEVKGYKDENNRLKEKEHKNQDDLlKEKETLIQQLKEELQEKNVTLDVQIQHVveGKRALSELTQGV 542
Cdd:COG3883 24 ELSELQAELEAAQAELDALQAELEELNEEYNELQAEL-EALQAEIDKLQAEIAEAEAEIEERREEL--GERARALYRSGG 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6807925 543 TcykakIKELETILETQKVecshsakleQDILEKESIILKL-ERNLKEFQEHLQDsvknTKDLNVKELKLKEEITQLTNN 621
Cdd:COG3883 101 S-----VSYLDVLLGSESF---------SDFLDRLSALSKIaDADADLLEELKAD----KAELEAKKAELEAKLAELEAL 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 6807925 622 LQDMKhllqlkeeeeetnrqeteKLKEELSASSARTQNLKADLQRKEEDYADLKEKLTDAKKQIKQVQKEVSV 694
Cdd:COG3883 163 KAELE------------------AAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAA 217
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
463-682 |
1.68e-03 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 42.70 E-value: 1.68e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6807925 463 QIEELEQQIEKLQAEVKGYKDENNRLK-EKEHKNQDDLLKEKETLIQQLKEELQEKNVTLDVQIQHVVEGKRALSELTQ- 540
Cdd:COG3206 183 QLPELRKELEEAEAALEEFRQKNGLVDlSEEAKLLLQQLSELESQLAEARAELAEAEARLAALRAQLGSGPDALPELLQs 262
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6807925 541 -GVTCYKAKIKELETILetqkvecshsAKLEQDILEKESIILKLERNLKEFQEHLQDSVKNTKDLNVKELK-LKEEITQL 618
Cdd:COG3206 263 pVIQQLRAQLAELEAEL----------AELSARYTPNHPDVIALRAQIAALRAQLQQEAQRILASLEAELEaLQAREASL 332
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 6807925 619 TNNLQDMKHLLQlkeeeeetnrqeteklkeELSASSARTQNLKADLQRKEEDYADLKEKLTDAK 682
Cdd:COG3206 333 QAQLAQLEARLA------------------ELPELEAELRRLEREVEVARELYESLLQRLEEAR 378
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
645-797 |
2.21e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 41.74 E-value: 2.21e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6807925 645 KLKEELSASSARTQNLKADLQRKEEDYADLKEKLTDAKKQIKQVQKEVSVMRDEDKLLRIKINEL---EKKKNQCSQELD 721
Cdd:COG3883 27 ELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERaraLYRSGGSVSYLD 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6807925 722 M------------KQRTIQQLKEQLNnqkveEAIQQYERACKDLNVKEKIIEDMRMTLEEQEQTQVEQDQVLEAKLEEVE 789
Cdd:COG3883 107 VllgsesfsdfldRLSALSKIADADA-----DLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQE 181
|
....*...
gi 6807925 790 RLATELEK 797
Cdd:COG3883 182 ALLAQLSA 189
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
664-815 |
2.40e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 42.06 E-value: 2.40e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6807925 664 LQRKEEDYADLKEKLTDAKKQIKQVQKEVSVMRDEDKLLRIKIN--ELEKKKNQCSQELDMKQRTIQQLKEQLNN----- 736
Cdd:COG4717 83 AEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQllPLYQELEALEAELAELPERLEELEERLEElrele 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6807925 737 ---QKVEEAIQQYERACKDL-----NVKEKIIEDMRMTLEEQEQTQVEQDQVLEAKLEEVERLATELEKWKEKCNDLETK 808
Cdd:COG4717 163 eelEELEAELAELQEELEELleqlsLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALE 242
|
....*..
gi 6807925 809 NNQRSNK 815
Cdd:COG4717 243 ERLKEAR 249
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
550-754 |
2.55e-03 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 41.67 E-value: 2.55e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6807925 550 KELETILETQKVECSHSAKLEQDILEKESIILKLERNLKEFQEHLQDSVKNTKDLNVKELKLKEEITQLTNNLQDMKHLL 629
Cdd:COG4942 27 AELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEEL 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6807925 630 QlKEEEEETNRQETEKLKEELSASSA-RTQNLKADLQRKEEDYADLKEKLTDAKKQIKQVQKEVSVMRDEdklLRIKINE 708
Cdd:COG4942 107 A-ELLRALYRLGRQPPLALLLSPEDFlDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAE---LEALLAE 182
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 6807925 709 LEKKKNQCSQELDMKQRTIQQLKEQLNNQkvEEAIQQYERACKDLN 754
Cdd:COG4942 183 LEEERAALEALKAERQKLLARLEKELAEL--AAELAELQQEAEELE 226
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
591-842 |
2.84e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 41.43 E-value: 2.84e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6807925 591 QEHLQDSVKNTKDLNVKELKLKEEITQLTNNLQDMKHLLQLKEEEEETNRQETEKLKEELSASSARTQNLKADLQRKEED 670
Cdd:COG4372 30 SEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEE 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6807925 671 YADLKEKLTDAKKQIKQVQKEVSVMRDEDKLLRIKINELEKKKNQCSQELDMKQRTIQQLKEQLNNQKVEEAIQQYERAC 750
Cdd:COG4372 110 AEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQALDELL 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6807925 751 KDLNVKEKIIEDMRMTLEEQEQ-TQVEQDQVLEAKLEEVERLATELEKWKEKCNDLETKNNQRSNKEHENNTDVLGKLTN 829
Cdd:COG4372 190 KEANRNAEKEEELAEAEKLIESlPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAILV 269
|
250
....*....|...
gi 6807925 830 LQDELQESEQKYN 842
Cdd:COG4372 270 EKDTEEEELEIAA 282
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
458-947 |
3.49e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 41.56 E-value: 3.49e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6807925 458 SKKSHQIEELEQQIEklqaevkgykdennrlkEKEHKNQDDLLKEKETLIQQLKEELQEKNVTLDvqiqhvvEGKRALSE 537
Cdd:PRK02224 183 SDQRGSLDQLKAQIE-----------------EKEEKDLHERLNGLESELAELDEEIERYEEQRE-------QARETRDE 238
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6807925 538 LTQGVTCYKAKIKELETiletqkvecshsakLEQDILEKESIILKLERNLKEFQEHLQDsvkntkdlnvkelkLKEEITQ 617
Cdd:PRK02224 239 ADEVLEEHEERREELET--------------LEAEIEDLRETIAETEREREELAEEVRD--------------LRERLEE 290
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6807925 618 LTNNLQDMKHLLQLKEEeeetnrqeteklkeELSASSARTQNLKADLQRKEEDYADLKEKLTDAKKQIKQVQKEVSVMRD 697
Cdd:PRK02224 291 LEEERDDLLAEAGLDDA--------------DAEAVEARREELEDRDEELRDRLEECRVAAQAHNEEAESLREDADDLEE 356
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6807925 698 EDKLLRIKINELEKKKNQCSQELDMKQRTIQQLKEQLnnqkvEEAIQQYERACKDLNVKEKIIEDMRMTLEEQEQTQVEq 777
Cdd:PRK02224 357 RAEELREEAAELESELEEAREAVEDRREEIEELEEEI-----EELRERFGDAPVDLGNAEDFLEELREERDELREREAE- 430
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6807925 778 dqvLEAKLEEVERLATELEKWKEKCNDLETKNNQRSNKEHENNTDVLGKLTNLQDELQESEQKyNADRKKWLEEKMMLIT 857
Cdd:PRK02224 431 ---LEATLRTARERVEEAEALLEAGKCPECGQPVEGSPHVETIEEDRERVEELEAELEDLEEE-VEEVEERLERAEDLVE 506
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6807925 858 QAKEAENIRNKE---MKKYAEDRERFFKQQNEMEILTAQLTEKDSDLQKWREE----RDQLVAALEiQLKALISSNVQKD 930
Cdd:PRK02224 507 AEDRIERLEERRedlEELIAERRETIEEKRERAEELRERAAELEAEAEEKREAaaeaEEEAEEARE-EVAELNSKLAELK 585
|
490
....*....|....*..
gi 6807925 931 NEIEQLKRIISETSKIE 947
Cdd:PRK02224 586 ERIESLERIRTLLAAIA 602
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
464-954 |
4.67e-03 |
|
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.
Pssm-ID: 431111 [Multi-domain] Cd Length: 766 Bit Score: 41.35 E-value: 4.67e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6807925 464 IEELEQQIEKLQAE-VKGYKDENNRLKEKE-HKNQDDLLKEKetlIQQLKEELQEKNVTLdvqiqhvVEGKRALSELTQG 541
Cdd:pfam10174 249 IRDLEDEVQMLKTNgLLHTEDREEEIKQMEvYKSHSKFMKNK---IDQLKQELSKKESEL-------LALQTKLETLTNQ 318
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6807925 542 VTCYKAKIKELETILETQKVECShsakleqdILEKESIILKLerNLKEFQEHLQDSVKNTKDLNvkelklkEEITQLTNN 621
Cdd:pfam10174 319 NSDCKQHIEVLKESLTAKEQRAA--------ILQTEVDALRL--RLEEKESFLNKKTKQLQDLT-------EEKSTLAGE 381
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6807925 622 LQDMKHLLQLKEEEEETNRQETEKLKEELSASSARTQNLKADLQRKEED-------YADLKEKLTDAKKQIKQVQKEVS- 693
Cdd:pfam10174 382 IRDLKDMLDVKERKINVLQKKIENLQEQLRDKDKQLAGLKERVKSLQTDssntdtaLTTLEEALSEKERIIERLKEQREr 461
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6807925 694 ---VMRDEDKLLRIKINELEKKKNQCSQELDMKQRTIQQLKEQLNNQ------------KVEEAIQQYERACKDLNVKEK 758
Cdd:pfam10174 462 edrERLEELESLKKENKDLKEKVSALQPELTEKESSLIDLKEHASSLassglkkdsklkSLEIAVEQKKEECSKLENQLK 541
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6807925 759 IIEDMRMTlEEQEQTQVEQDQVLEA----KLEEVERLATELEKWKEKCNDLETKNNQRSNKEHENNTDVLGKLTNLQDEL 834
Cdd:pfam10174 542 KAHNAEEA-VRTNPEINDRIRLLEQevarYKEESGKAQAEVERLLGILREVENEKNDKDKKIAELESLTLRQMKEQNKKV 620
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6807925 835 QESEQKYNADRKKWLEEkmMLITQAKEAENIRNKEMKKYAEDRERFFKQQNEMEILTAQLT-------EKDSDLQKWR-E 906
Cdd:pfam10174 621 ANIKHGQQEMKKKGAQL--LEEARRREDNLADNSQQLQLEELMGALEKTRQELDATKARLSstqqslaEKDGHLTNLRaE 698
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 6807925 907 ERDQLVAALEIQLKALISSNVQKDNEIEQLKRIISETSKIETQIMDIK 954
Cdd:pfam10174 699 RRKQLEEILEMKQEALLAAISEKDANIALLELSSSKKKKTQEEVMALK 746
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
567-907 |
5.60e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 41.05 E-value: 5.60e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6807925 567 AKLEqdILEKEsiILKLERNLKEFQEHLQDsVKNTKDLNVKELKLKEEITQLTNNLQDM----KHLLQLKEEeeetnrqe 642
Cdd:COG4913 610 AKLA--ALEAE--LAELEEELAEAEERLEA-LEAELDALQERREALQRLAEYSWDEIDVasaeREIAELEAE-------- 676
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6807925 643 teklKEELSASSARTQNLKADLQRKEEDYADLKEKLTDAKKQIKQVQKEVSVMRDEDKLLRIKINELEKKKNQcSQELDM 722
Cdd:COG4913 677 ----LERLDASSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARL-ELRALL 751
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6807925 723 KQRTIQQLKEQLNNQKVEEAIQQYERACKDLNVKEKIIEDMRMTLEEQEQTQVEQDQVLEAKLEEVERLATEL------- 795
Cdd:COG4913 752 EERFAAALGDAVERELRENLEERIDALRARLNRAEEELERAMRAFNREWPAETADLDADLESLPEYLALLDRLeedglpe 831
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6807925 796 --EKWKEKCNDLETKN----NQRSNKEHENNTDVLGKLtNlqDELQESEqkYNADRKKWLEEKMMLITQAKE----AENI 865
Cdd:COG4913 832 yeERFKELLNENSIEFvadlLSKLRRAIREIKERIDPL-N--DSLKRIP--FGPGRYLRLEARPRPDPEVREfrqeLRAV 906
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 6807925 866 RNKEMKKYAEDRERFFKQQNE-MEILTAQLTEKDsdlQKWREE 907
Cdd:COG4913 907 TSGASLFDEELSEARFAALKRlIERLRSEEEESD---RRWRAR 946
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
567-763 |
6.96e-03 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 40.13 E-value: 6.96e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6807925 567 AKLEQDILEKESIILKLERNLKEFQEHLQDSVKNTKDLNVKELKLKEEITQLTNNLQDMKHLLQlkeEEEETNRQETEKL 646
Cdd:COG4942 30 EQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIA---ELRAELEAQKEEL 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6807925 647 KEELSASSARTQNLKADLQRKEEDYADLKEKLTDAKKQIKQVQKEVSVMRDEDKLLRIKINELEKKKNQCSQELDMKQRT 726
Cdd:COG4942 107 AELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEE 186
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 6807925 727 IQQLKEQLNNQ-----KVEEAIQQYERACKDLNVKEKIIEDM 763
Cdd:COG4942 187 RAALEALKAERqkllaRLEKELAELAAELAELQQEAEELEAL 228
|
|
| CCDC73 |
pfam15818 |
Coiled-coil domain-containing protein 73 family; CCDC73 is a family of eukaryotic coiled-coil ... |
489-749 |
8.14e-03 |
|
Coiled-coil domain-containing protein 73 family; CCDC73 is a family of eukaryotic coiled-coil containing proteins. The function is not known. The alternative name is sarcoma antigen NY-SAR-79.
Pssm-ID: 464893 [Multi-domain] Cd Length: 1048 Bit Score: 40.70 E-value: 8.14e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6807925 489 KEKEHKNQDDLLKEKETLIQQLKEeLQEKNVTLDVQIQHVVEGKRALSELTQG----VTCYKAKIKELETILETQKVECS 564
Cdd:pfam15818 129 KEDHHKQLNEIEKYYATITGQFGL-VKENHGKLEQNVQEAIQLNKRLSALNKKqeseICSLKKELKKVTSDLIKSKVTCQ 207
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6807925 565 HSakleqdiLEKESIILKL-ERNLKEFQEHLQDSVKNTKDLNVKELKLKEEITQLTNNLQDMKHLLQlkeeeeeTNRQET 643
Cdd:pfam15818 208 YK-------MGEENINLTIkEQKFQELQERLNMELELNKKINEEITHIQEEKQDIIISFQHMQQLLQ-------QQTQAN 273
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6807925 644 EKLKEELSASSARTQNLKAD--LQRK-----EEDYADLKEKLTDA----KKQIKQVQKEVSVMRDEDKLLRIKINELEKK 712
Cdd:pfam15818 274 TEMEAELKALKENNQTLERDneLQREkvkenEEKFLNLQNEHEKAlgtwKKHVEELNGEINEIKNELSSLKETHIKLQEH 353
|
250 260 270
....*....|....*....|....*....|....*...
gi 6807925 713 KN-QCSQELDMKQRTIQQLKEqLNNQKVEEAIQQYERA 749
Cdd:pfam15818 354 YNkLCNQKKFEEDKKFQNVPE-VNNENSEMSTEKSENL 390
|
|
| GAS |
pfam13851 |
Growth-arrest specific micro-tubule binding; This family is the highly conserved central ... |
610-748 |
8.90e-03 |
|
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: 38.73 E-value: 8.90e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6807925 610 KLKEEITQLTNNLQDMKHLLQlkeeeeeTNRQETEKLKEELsassARTQNLKADLQRKEEDYADLKEKLTDAKKQIKQVQ 689
Cdd:pfam13851 30 SLKEEIAELKKKEERNEKLMS-------EIQQENKRLTEPL----QKAQEEVEELRKQLENYEKDKQSLKNLKARLKVLE 98
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 6807925 690 KEVSVMRDEDKLLRIKINELEKKKNQCSQELDMKQRTIQQ---LKEQLNNQKVEEAIQQYER 748
Cdd:pfam13851 99 KELKDLKWEHEVLEQRFEKVERERDELYDKFEAAIQDVQQktgLKNLLLEKKLQALGETLEK 160
|
|
| |
