|
Name |
Accession |
Description |
Interval |
E-value |
| Angiomotin_C |
pfam12240 |
Angiomotin C terminal; This domain family is found in eukaryotes, and is typically between 197 ... |
540-745 |
7.00e-95 |
|
Angiomotin C terminal; This domain family is found in eukaryotes, and is typically between 197 and 211 amino acids in length. This family is the C terminal region of angiomotin. Angiomotin regulates the action of angiogenesis inhibitor angiostatin. The C terminal region of angiomotin appears to be involved in directing the protein chemotactically.
Pssm-ID: 463503 [Multi-domain] Cd Length: 200 Bit Score: 295.14 E-value: 7.00e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522838240 540 YVEKVERLQQALGQLQAACEKREQLELRLRTRLEQELKALRAQQRQAGAPGGSSGsggspELSALRLSEQLREKEEQILA 619
Cdd:pfam12240 1 YVEKVERLQQALAQLQAACEKREQLELRLRTRLEQELKSLRAQQRQGGSQGSGPS-----EYSAPALMELLREKEERILA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522838240 620 LEADMTKWEQKYLEERAMRQFAMDAAATAAAQRDTTLIRHSPQPSPSSSFNEGLLTGGHRHQEMESRLKVLHAQILEKDA 699
Cdd:pfam12240 76 LEADMTKWEQKYLEESTMRQFAMDAAATAAAQRDTTIINHSPRHSYDSSFNEELLLANRRCQEMENRIKNLHAQILEKDA 155
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 522838240 700 VIKVLQQRSRRDPGKAIQGSLRPAKSVPSVFaAAAAGTQGWQGLSS 745
Cdd:pfam12240 156 MIKVLQQRSRKDPGKTDQQSLRPARSVPSIS-AAATGLHSRQTSLS 200
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
370-639 |
1.31e-13 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 74.97 E-value: 1.31e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522838240 370 AQMEAVLRENARLQRDNERLQRELES-SAEKAGRIEKLESEIQRLSEAHESLTRASSKREALEKtmrnkmdsEMRRLQDF 448
Cdd:COG1196 239 AELEELEAELEELEAELEELEAELAElEAELEELRLELEELELELEEAQAEEYELLAELARLEQ--------DIARLEER 310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522838240 449 NRDLRERLESANRRLASKTQEAQAGSQDMVAKLLAQSYEQQQEQEKLEREMALLRGAIEDQRRRAELLEQALGNAQGRAA 528
Cdd:COG1196 311 RRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLE 390
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522838240 529 RAEEELRKKQAYVEKVERLQQALGQLQAACEKREQLELRLRTRLEQELKALRAQQRQAGAPGGSSGSGGSPELSALRLSE 608
Cdd:COG1196 391 ALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLE 470
|
250 260 270
....*....|....*....|....*....|.
gi 522838240 609 QLREKEEQILALEADMTKWEQKYLEERAMRQ 639
Cdd:COG1196 471 EAALLEAALAELLEELAEAAARLLLLLEAEA 501
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
367-762 |
3.06e-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: 3.06e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522838240 367 AHLAQMEAVLRE-NARLqrdnERLQRElessAEKAGRIEKLESEIQ---------RLSEAHESLTRASSKREALEKTmRN 436
Cdd:COG1196 186 ENLERLEDILGElERQL----EPLERQ----AEKAERYRELKEELKeleaellllKLRELEAELEELEAELEELEAE-LE 256
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522838240 437 KMDSEMRRLQDFNRDLRERLESANRRLASKTQEAQAGSQDmVAKLLAQSYEQQQEQEKLEREMALLRGAIEDQRRRAELL 516
Cdd:COG1196 257 ELEAELAELEAELEELRLELEELELELEEAQAEEYELLAE-LARLEQDIARLEERRRELEERLEELEEELAELEEELEEL 335
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522838240 517 EQALGNAQGRAARAEEELRKKQayvekvERLQQALGQLQAACEKREQLELRLRTRLEQELKALRAQQRQAGAPGGSSGSG 596
Cdd:COG1196 336 EEELEELEEELEEAEEELEEAE------AELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAE 409
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522838240 597 GSPELSALRLSEQLREKEEQILALEADMTKWEQKYLEERAMRQFAMDAAATAAAQRDTTLIRHSPQPSPSSSFNEGLLtg 676
Cdd:COG1196 410 EALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELA-- 487
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522838240 677 ghRHQEMESRLKVLHAQILEKDAVIKVLQQRSRRDPGKAIQGSLRPAKSVPSVFAAAAAGTQGWQGLSSSERQTADAPAR 756
Cdd:COG1196 488 --EAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAALAAALQNIVVEDDEVAAAAIEY 565
|
....*.
gi 522838240 757 LTTDRA 762
Cdd:COG1196 566 LKAAKA 571
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
370-639 |
3.42e-09 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 60.85 E-value: 3.42e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522838240 370 AQMEAVLRENARLQRDNERLQRELESSAEK----AGRIEKLESEIQRLSEAHESLTRASSK-REALEKTMRN-------K 437
Cdd:TIGR02169 716 RKIGEIEKEIEQLEQEEEKLKERLEELEEDlsslEQEIENVKSELKELEARIEELEEDLHKlEEALNDLEARlshsripE 795
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522838240 438 MDSEMRRLQDFNRDLRERLESANRRLASKTQEAQAgSQDMVAKLLAQSYEQQQEQEKLEREMALLRGAIEDQRRRAELLE 517
Cdd:TIGR02169 796 IQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEY-LEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELE 874
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522838240 518 QALGNAQGRAARAEEELRKKQAyveKVERLQQALGQLQAACEKREQLELRLRTRLEqelkALRAQQRQAGAPGGSSGSGG 597
Cdd:TIGR02169 875 AALRDLESRLGDLKKERDELEA---QLRELERKIEELEAQIEKKRKRLSELKAKLE----ALEEELSEIEDPKGEDEEIP 947
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 522838240 598 SPELSALRLSEQLREKEEQILALEADMTKWEQKYlEERAMRQ 639
Cdd:TIGR02169 948 EEELSLEDVQAELQRVEEEIRALEPVNMLAIQEY-EEVLKRL 988
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
380-707 |
6.45e-06 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 50.06 E-value: 6.45e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522838240 380 ARLQRDNERLQRELEssaekagrIEKLESEIQRLSEAHESLTRAsskrealektmRNKMDSEMRRLQDFNRDLRERLESA 459
Cdd:TIGR02168 664 GSAKTNSSILERRRE--------IEELEEKIEELEEKIAELEKA-----------LAELRKELEELEEELEQLRKELEEL 724
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522838240 460 NRRLASKTQEAQAGSQdmvakllaqsyeqqqEQEKLEREMALLRGAIEDQRRRAELLEQALGNAQGRAARAEEELRKKQA 539
Cdd:TIGR02168 725 SRQISALRKDLARLEA---------------EVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEA 789
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522838240 540 yveKVERLQQALGQLqaacekREQLElrlrtRLEQELKALR-AQQRQAGAPGGSSGSGGSPELSALRLSEQLREKEEQIL 618
Cdd:TIGR02168 790 ---QIEQLKEELKAL------REALD-----ELRAELTLLNeEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIE 855
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522838240 619 ALEADMTkwEQKYLEERAMRQFAMDAAATAAAQRDTTLIRHspqpsPSSSFNEGLLTGGHRHQEMESRLKVLHAQILEKD 698
Cdd:TIGR02168 856 SLAAEIE--ELEELIEELESELEALLNERASLEEALALLRS-----ELEELSEELRELESKRSELRRELEELREKLAQLE 928
|
....*....
gi 522838240 699 AVIKVLQQR 707
Cdd:TIGR02168 929 LRLEGLEVR 937
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
373-638 |
1.22e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 49.37 E-value: 1.22e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522838240 373 EAVLRENARLQRDNERLQRELESSAEKAGRIEKLESEIQRLSEAHESLTRASS---KREALEKTMRNKMDSEMRRLQDfN 449
Cdd:PTZ00121 1455 EAKKAEEAKKKAEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEakkKADEAKKAEEAKKADEAKKAEE-A 1533
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522838240 450 RDLRERLESANRRLASKTQEAQAgsqdmVAKLLAQSYEQQQEQEKLEREMALLRGAIEDQ---RRRAELLEQALGNAQGR 526
Cdd:PTZ00121 1534 KKADEAKKAEEKKKADELKKAEE-----LKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKaeeARIEEVMKLYEEEKKMK 1608
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522838240 527 A--ARAEEELRKKQAYVEKVERLQQALGQLQAACE----KREQL---ELRLRTRLEQELKALRAQQRQAGAPGGSSGSGG 597
Cdd:PTZ00121 1609 AeeAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAeekkKAEELkkaEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEK 1688
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 522838240 598 SPELSALRLSEQLREKEEQILALEADMTKWEQ--KYLEERAMR 638
Cdd:PTZ00121 1689 KAAEALKKEAEEAKKAEELKKKEAEEKKKAEElkKAEEENKIK 1731
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
370-585 |
2.50e-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: 48.30 E-value: 2.50e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522838240 370 AQMEAVLRENARLQRDNERLQR----ELESSAEKAGRIEKLESEIQRLSEAHESLTRASSKREALEKTMRNKMDSEMRR- 444
Cdd:pfam12128 312 AADAAVAKDRSELEALEDQHGAfldaDIETAAADQEQLPSWQSELENLEERLKALTGKHQDVTAKYNRRRSKIKEQNNRd 391
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522838240 445 LQDFNRDLRERLESANRRLASKTQEAQAGSQDMVAKLlaqsyeqqqeqekleremallRGAIEDQRRRAELLEQALGNAQ 524
Cdd:pfam12128 392 IAGIKDKLAKIREARDRQLAVAEDDLQALESELREQL---------------------EAGKLEFNEEEYRLKSRLGELK 450
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 522838240 525 GRAARA---EEELRKKQAYVEKVERLQQALGQLQAACEKREQLELRLRTRLEQELKAL-----RAQQRQ 585
Cdd:pfam12128 451 LRLNQAtatPELLLQLENFDERIERAREEQEAANAEVERLQSELRQARKRRDQASEALrqasrRLEERQ 519
|
|
| OmpH |
smart00935 |
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH ... |
369-470 |
9.59e-04 |
|
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH among others. Skp (OmpH) has been characterized as a molecular chaperone that interacts with unfolded proteins as they emerge in the periplasm from the Sec translocation machinery.
Pssm-ID: 214922 [Multi-domain] Cd Length: 140 Bit Score: 40.26 E-value: 9.59e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522838240 369 LAQMEAVLRENARLQRDNERLQRELESSAEKagrIEKLESEIQRlseahESLTRASSKREALEKTMrNKMDSEMRRL-QD 447
Cdd:smart00935 10 LQESPAGKAAQKQLEKEFKKRQAELEKLEKE---LQKLKEKLQK-----DAATLSEAAREKKEKEL-QKKVQEFQRKqQK 80
|
90 100
....*....|....*....|...
gi 522838240 448 FNRDLRERLESANRRLASKTQEA 470
Cdd:smart00935 81 LQQDLQKRQQEELQKILDKINKA 103
|
|
|
|
Name |
Accession |
Description |
Interval |
E-value |
| Angiomotin_C |
pfam12240 |
Angiomotin C terminal; This domain family is found in eukaryotes, and is typically between 197 ... |
540-745 |
7.00e-95 |
|
Angiomotin C terminal; This domain family is found in eukaryotes, and is typically between 197 and 211 amino acids in length. This family is the C terminal region of angiomotin. Angiomotin regulates the action of angiogenesis inhibitor angiostatin. The C terminal region of angiomotin appears to be involved in directing the protein chemotactically.
Pssm-ID: 463503 [Multi-domain] Cd Length: 200 Bit Score: 295.14 E-value: 7.00e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522838240 540 YVEKVERLQQALGQLQAACEKREQLELRLRTRLEQELKALRAQQRQAGAPGGSSGsggspELSALRLSEQLREKEEQILA 619
Cdd:pfam12240 1 YVEKVERLQQALAQLQAACEKREQLELRLRTRLEQELKSLRAQQRQGGSQGSGPS-----EYSAPALMELLREKEERILA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522838240 620 LEADMTKWEQKYLEERAMRQFAMDAAATAAAQRDTTLIRHSPQPSPSSSFNEGLLTGGHRHQEMESRLKVLHAQILEKDA 699
Cdd:pfam12240 76 LEADMTKWEQKYLEESTMRQFAMDAAATAAAQRDTTIINHSPRHSYDSSFNEELLLANRRCQEMENRIKNLHAQILEKDA 155
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 522838240 700 VIKVLQQRSRRDPGKAIQGSLRPAKSVPSVFaAAAAGTQGWQGLSS 745
Cdd:pfam12240 156 MIKVLQQRSRKDPGKTDQQSLRPARSVPSIS-AAATGLHSRQTSLS 200
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
370-639 |
1.31e-13 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 74.97 E-value: 1.31e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522838240 370 AQMEAVLRENARLQRDNERLQRELES-SAEKAGRIEKLESEIQRLSEAHESLTRASSKREALEKtmrnkmdsEMRRLQDF 448
Cdd:COG1196 239 AELEELEAELEELEAELEELEAELAElEAELEELRLELEELELELEEAQAEEYELLAELARLEQ--------DIARLEER 310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522838240 449 NRDLRERLESANRRLASKTQEAQAGSQDMVAKLLAQSYEQQQEQEKLEREMALLRGAIEDQRRRAELLEQALGNAQGRAA 528
Cdd:COG1196 311 RRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLE 390
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522838240 529 RAEEELRKKQAYVEKVERLQQALGQLQAACEKREQLELRLRTRLEQELKALRAQQRQAGAPGGSSGSGGSPELSALRLSE 608
Cdd:COG1196 391 ALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLE 470
|
250 260 270
....*....|....*....|....*....|.
gi 522838240 609 QLREKEEQILALEADMTKWEQKYLEERAMRQ 639
Cdd:COG1196 471 EAALLEAALAELLEELAEAAARLLLLLEAEA 501
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
367-616 |
3.22e-12 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 70.35 E-value: 3.22e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522838240 367 AHLAQMEAVLREN-ARLQRDNERLQRELESSAEKAGRIEKLESEIQRLSEAHESLTRASSKREALEKTMRNKMDSEMRRL 445
Cdd:COG1196 260 AELAELEAELEELrLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEEL 339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522838240 446 QDfnrdLRERLESANRRLASKTQEAQAGSQDMVAKLLAQSYEQQQEQEKLEREMALLRGAIEDQRRRAELlEQALGNAQG 525
Cdd:COG1196 340 EE----LEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEEL-EEAEEALLE 414
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522838240 526 RAARAEEELRKKQAYVEKVERLQQALGQLQAACEKREQLELRLRTRLEQELKALRAQQRQAGAPGGSSGSGGSPELSALR 605
Cdd:COG1196 415 RLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLL 494
|
250
....*....|.
gi 522838240 606 LSEQLREKEEQ 616
Cdd:COG1196 495 LLLEAEADYEG 505
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
367-762 |
3.06e-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: 3.06e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522838240 367 AHLAQMEAVLRE-NARLqrdnERLQRElessAEKAGRIEKLESEIQ---------RLSEAHESLTRASSKREALEKTmRN 436
Cdd:COG1196 186 ENLERLEDILGElERQL----EPLERQ----AEKAERYRELKEELKeleaellllKLRELEAELEELEAELEELEAE-LE 256
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522838240 437 KMDSEMRRLQDFNRDLRERLESANRRLASKTQEAQAGSQDmVAKLLAQSYEQQQEQEKLEREMALLRGAIEDQRRRAELL 516
Cdd:COG1196 257 ELEAELAELEAELEELRLELEELELELEEAQAEEYELLAE-LARLEQDIARLEERRRELEERLEELEEELAELEEELEEL 335
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522838240 517 EQALGNAQGRAARAEEELRKKQayvekvERLQQALGQLQAACEKREQLELRLRTRLEQELKALRAQQRQAGAPGGSSGSG 596
Cdd:COG1196 336 EEELEELEEELEEAEEELEEAE------AELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAE 409
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522838240 597 GSPELSALRLSEQLREKEEQILALEADMTKWEQKYLEERAMRQFAMDAAATAAAQRDTTLIRHSPQPSPSSSFNEGLLtg 676
Cdd:COG1196 410 EALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELA-- 487
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522838240 677 ghRHQEMESRLKVLHAQILEKDAVIKVLQQRSRRDPGKAIQGSLRPAKSVPSVFAAAAAGTQGWQGLSSSERQTADAPAR 756
Cdd:COG1196 488 --EAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAALAAALQNIVVEDDEVAAAAIEY 565
|
....*.
gi 522838240 757 LTTDRA 762
Cdd:COG1196 566 LKAAKA 571
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
370-639 |
3.42e-09 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 60.85 E-value: 3.42e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522838240 370 AQMEAVLRENARLQRDNERLQRELESSAEK----AGRIEKLESEIQRLSEAHESLTRASSK-REALEKTMRN-------K 437
Cdd:TIGR02169 716 RKIGEIEKEIEQLEQEEEKLKERLEELEEDlsslEQEIENVKSELKELEARIEELEEDLHKlEEALNDLEARlshsripE 795
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522838240 438 MDSEMRRLQDFNRDLRERLESANRRLASKTQEAQAgSQDMVAKLLAQSYEQQQEQEKLEREMALLRGAIEDQRRRAELLE 517
Cdd:TIGR02169 796 IQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEY-LEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELE 874
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522838240 518 QALGNAQGRAARAEEELRKKQAyveKVERLQQALGQLQAACEKREQLELRLRTRLEqelkALRAQQRQAGAPGGSSGSGG 597
Cdd:TIGR02169 875 AALRDLESRLGDLKKERDELEA---QLRELERKIEELEAQIEKKRKRLSELKAKLE----ALEEELSEIEDPKGEDEEIP 947
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 522838240 598 SPELSALRLSEQLREKEEQILALEADMTKWEQKYlEERAMRQ 639
Cdd:TIGR02169 948 EEELSLEDVQAELQRVEEEIRALEPVNMLAIQEY-EEVLKRL 988
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
370-630 |
9.20e-09 |
|
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: 59.30 E-value: 9.20e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522838240 370 AQMEAVLRENARLQRDNERLQRELESSAEKAGRIEKLESEIQR-LSEAHESLTRASSKREALEKTMRNkMDSEMRRLQDF 448
Cdd:TIGR02168 684 EKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRqISALRKDLARLEAEVEQLEERIAQ-LSKELTELEAE 762
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522838240 449 NRDLRERLESANRRLASKTQEAQAGSQDmVAKLLAQSYEQQQEQEKLEREMALLRGAIEDQRRRAELLEQALGNAQGRAA 528
Cdd:TIGR02168 763 IEELEERLEEAEEELAEAEAEIEELEAQ-IEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLE 841
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522838240 529 RAEEELRKKQayvEKVERLQQALGQLQAACEK-REQLE--LRLRTRLEQELKALRAQQRQagapggSSGSGGSPELSALR 605
Cdd:TIGR02168 842 DLEEQIEELS---EDIESLAAEIEELEELIEElESELEalLNERASLEEALALLRSELEE------LSEELRELESKRSE 912
|
250 260
....*....|....*....|....*
gi 522838240 606 LSEQLREKEEQILALEADMTKWEQK 630
Cdd:TIGR02168 913 LRRELEELREKLAQLELRLEGLEVR 937
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
402-622 |
3.11e-08 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 57.62 E-value: 3.11e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522838240 402 RIEKLESEIQRLSEAHESLTRASSKREALektmrnkmdsemrrlqdfnrdlrERLESANRRLASKTQEAQAgSQDMVAKL 481
Cdd:COG4913 226 AADALVEHFDDLERAHEALEDAREQIELL-----------------------EPIRELAERYAAARERLAE-LEYLRAAL 281
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522838240 482 laqsyeqqqEQEKLEREMALLRGAIEDQRRRAELLEQALGNAQGRAARAEEELRK-KQAY----VEKVERLQQALGQLQA 556
Cdd:COG4913 282 ---------RLWFAQRRLELLEAELEELRAELARLEAELERLEARLDALREELDElEAQIrgngGDRLEQLEREIERLER 352
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522838240 557 ACEKREQLELRLRTRL----------EQELKALRAQQRQAGAPGGSSGSGGSPELSALR-----LSEQLREKEEQILALE 621
Cdd:COG4913 353 ELEERERRRARLEALLaalglplpasAEEFAALRAEAAALLEALEEELEALEEALAEAEaalrdLRRELRELEAEIASLE 432
|
.
gi 522838240 622 A 622
Cdd:COG4913 433 R 433
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
378-633 |
4.35e-08 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 57.00 E-value: 4.35e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522838240 378 ENARLQRDNERLQRELESSAEKAGRIEKLESEI-QRLSEAHESLTRASSKREALEKTmRNKMDSEMRRLQDFNRDLRERL 456
Cdd:TIGR02169 675 ELQRLRERLEGLKRELSSLQSELRRIENRLDELsQELSDASRKIGEIEKEIEQLEQE-EEKLKERLEELEEDLSSLEQEI 753
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522838240 457 ESANRRLASKTQEAQAGSQDMVAKLLAQSYEQQQEQEKLEREMALLRGAIEDQRRRAEL----LEQALGNAQGRAARAEE 532
Cdd:TIGR02169 754 ENVKSELKELEARIEELEEDLHKLEEALNDLEARLSHSRIPEIQAELSKLEEEVSRIEArlreIEQKLNRLTLEKEYLEK 833
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522838240 533 ELRKKQAYVEKVERlqqalgQLQAACEKREQLELRLRtRLEQELKALRAQQRQagapggssgsggspelsalrLSEQLRE 612
Cdd:TIGR02169 834 EIQELQEQRIDLKE------QIKSIEKEIENLNGKKE-ELEEELEELEAALRD--------------------LESRLGD 886
|
250 260
....*....|....*....|.
gi 522838240 613 KEEQILALEADMTKWEQKYLE 633
Cdd:TIGR02169 887 LKKERDELEAQLRELERKIEE 907
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
365-585 |
1.47e-07 |
|
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: 54.38 E-value: 1.47e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522838240 365 GSAHLAQMEAVLRENARLQRDNERLQRELESSAEKAGRIEKLESEIQRLSEAhesLTRASSKREALEKTMrNKMDSEMRR 444
Cdd:COG4942 12 ALAAAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERR---IAALARRIRALEQEL-AALEAELAE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522838240 445 LQDFNRDLRERLESANRRLASKTQEAQAGSQDMVAKLLAqsyeQQQEQEKLEREMALLRGAIEDQRRRAELLEQALGNAQ 524
Cdd:COG4942 88 LEKEIAELRAELEAQKEELAELLRALYRLGRQPPLALLL----SPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELA 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 522838240 525 GRAARAEEELRKKQAYVEKVERLQQALGQLQAaceKREQLELRLRTRLEQELKALRAQQRQ 585
Cdd:COG4942 164 ALRAELEAERAELEALLAELEEERAALEALKA---ERQKLLARLEKELAELAAELAELQQE 221
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
367-631 |
3.00e-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: 51.22 E-value: 3.00e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522838240 367 AHLAQMEAVLRENARLQRDNERLQRELESSAEKAGRIEKLESEI----------------QRLSEAHESLTRASSKREAL 430
Cdd:TIGR02169 234 ALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELnkkikdlgeeeqlrvkEKIGELEAEIASLERSIAEK 313
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522838240 431 EKTMRN------KMDSEMRRLQDFNRDLRERLESANRRLASKT---QEAQAGSQDMVAKL----------LAQSYEQQQE 491
Cdd:TIGR02169 314 ERELEDaeerlaKLEAEIDKLLAEIEELEREIEEERKRRDKLTeeyAELKEELEDLRAELeevdkefaetRDELKDYREK 393
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522838240 492 QEKLEREMALLRGAIEDQRRRAELLEQALGNAQGRAARAEEELRKKQAYVE----KVERLQQALGQLQAACEKREQLELR 567
Cdd:TIGR02169 394 LEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEdkalEIKKQEWKLEQLAADLSKYEQELYD 473
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 522838240 568 LRTRLEQELKALRAQQRQAGAPGGSSGSGGSPELSALRLSEQLREKEEQILALEADMTKWEQKY 631
Cdd:TIGR02169 474 LKEEYDRVEKELSKLQRELAEAEAQARASEERVRGGRAVEEVLKASIQGVHGTVAQLGSVGERY 537
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
402-585 |
6.38e-06 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 49.91 E-value: 6.38e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522838240 402 RIEKLESEIQRLSEAHESLTRASSKREALEKTMRNKmDSEMRRLQDFNRDLRErLESANRRLASKTQEAQA--GSQDMVA 479
Cdd:COG4913 611 KLAALEAELAELEEELAEAEERLEALEAELDALQER-REALQRLAEYSWDEID-VASAEREIAELEAELERldASSDDLA 688
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522838240 480 KLlaqsyeqqqeqeklEREMALLRGAIEDQRRRAELLEQALGNAQGRAARAEEELRKKQAYVEKVERLQQAlgQLQAACE 559
Cdd:COG4913 689 AL--------------EEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARL--ELRALLE 752
|
170 180 190
....*....|....*....|....*....|..
gi 522838240 560 KR------EQLELRLRTRLEQELKALRAQQRQ 585
Cdd:COG4913 753 ERfaaalgDAVERELRENLEERIDALRARLNR 784
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
380-707 |
6.45e-06 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 50.06 E-value: 6.45e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522838240 380 ARLQRDNERLQRELEssaekagrIEKLESEIQRLSEAHESLTRAsskrealektmRNKMDSEMRRLQDFNRDLRERLESA 459
Cdd:TIGR02168 664 GSAKTNSSILERRRE--------IEELEEKIEELEEKIAELEKA-----------LAELRKELEELEEELEQLRKELEEL 724
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522838240 460 NRRLASKTQEAQAGSQdmvakllaqsyeqqqEQEKLEREMALLRGAIEDQRRRAELLEQALGNAQGRAARAEEELRKKQA 539
Cdd:TIGR02168 725 SRQISALRKDLARLEA---------------EVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEA 789
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522838240 540 yveKVERLQQALGQLqaacekREQLElrlrtRLEQELKALR-AQQRQAGAPGGSSGSGGSPELSALRLSEQLREKEEQIL 618
Cdd:TIGR02168 790 ---QIEQLKEELKAL------REALD-----ELRAELTLLNeEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIE 855
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522838240 619 ALEADMTkwEQKYLEERAMRQFAMDAAATAAAQRDTTLIRHspqpsPSSSFNEGLLTGGHRHQEMESRLKVLHAQILEKD 698
Cdd:TIGR02168 856 SLAAEIE--ELEELIEELESELEALLNERASLEEALALLRS-----ELEELSEELRELESKRSELRRELEELREKLAQLE 928
|
....*....
gi 522838240 699 AVIKVLQQR 707
Cdd:TIGR02168 929 LRLEGLEVR 937
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
373-638 |
1.22e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 49.37 E-value: 1.22e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522838240 373 EAVLRENARLQRDNERLQRELESSAEKAGRIEKLESEIQRLSEAHESLTRASS---KREALEKTMRNKMDSEMRRLQDfN 449
Cdd:PTZ00121 1455 EAKKAEEAKKKAEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEakkKADEAKKAEEAKKADEAKKAEE-A 1533
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522838240 450 RDLRERLESANRRLASKTQEAQAgsqdmVAKLLAQSYEQQQEQEKLEREMALLRGAIEDQ---RRRAELLEQALGNAQGR 526
Cdd:PTZ00121 1534 KKADEAKKAEEKKKADELKKAEE-----LKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKaeeARIEEVMKLYEEEKKMK 1608
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522838240 527 A--ARAEEELRKKQAYVEKVERLQQALGQLQAACE----KREQL---ELRLRTRLEQELKALRAQQRQAGAPGGSSGSGG 597
Cdd:PTZ00121 1609 AeeAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAeekkKAEELkkaEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEK 1688
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 522838240 598 SPELSALRLSEQLREKEEQILALEADMTKWEQ--KYLEERAMR 638
Cdd:PTZ00121 1689 KAAEALKKEAEEAKKAEELKKKEAEEKKKAEElkKAEEENKIK 1731
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
367-710 |
1.67e-05 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 48.51 E-value: 1.67e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522838240 367 AHLAQMEAVLREnarLQRDNERLQRELESsAEKAGRIEKLESEIQ------RLSEAHESLTRASSKREALEkTMRNKMDS 440
Cdd:TIGR02168 186 ENLDRLEDILNE---LERQLKSLERQAEK-AERYKELKAELRELElallvlRLEELREELEELQEELKEAE-EELEELTA 260
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522838240 441 EMRRLQDfnrDLrERLESANRRLASKTQEAQAGSQDMVAKLlaqsyeqqqeqekleremALLRGAIEDQRRRAELLEQal 520
Cdd:TIGR02168 261 ELQELEE---KL-EELRLEVSELEEEIEELQKELYALANEI------------------SRLEQQKQILRERLANLER-- 316
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522838240 521 gNAQGRAARAEEELRKKQAYVEKVERLQQALGQLQAACEkREQLELRLRTRLEQELKALRAQQRQAGAPGGSSGSGGSPE 600
Cdd:TIGR02168 317 -QLEELEAQLEELESKLDELAEELAELEEKLEELKEELE-SLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQ 394
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522838240 601 LSALRlsEQLREKEEQILALEADMTKWEQKYLEERamRQFAMDAAATAAAQRDTTLIRHSPQPSPSSSFNEGLLTGGHRH 680
Cdd:TIGR02168 395 IASLN--NEIERLEARLERLEDRRERLQQEIEELL--KKLEEAELKELQAELEELEEELEELQEELERLEEALEELREEL 470
|
330 340 350
....*....|....*....|....*....|
gi 522838240 681 QEMESRLKVLHAQILEKDAVIKVLQQRSRR 710
Cdd:TIGR02168 471 EEAEQALDAAERELAQLQARLDSLERLQEN 500
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
370-585 |
2.50e-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: 48.30 E-value: 2.50e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522838240 370 AQMEAVLRENARLQRDNERLQR----ELESSAEKAGRIEKLESEIQRLSEAHESLTRASSKREALEKTMRNKMDSEMRR- 444
Cdd:pfam12128 312 AADAAVAKDRSELEALEDQHGAfldaDIETAAADQEQLPSWQSELENLEERLKALTGKHQDVTAKYNRRRSKIKEQNNRd 391
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522838240 445 LQDFNRDLRERLESANRRLASKTQEAQAGSQDMVAKLlaqsyeqqqeqekleremallRGAIEDQRRRAELLEQALGNAQ 524
Cdd:pfam12128 392 IAGIKDKLAKIREARDRQLAVAEDDLQALESELREQL---------------------EAGKLEFNEEEYRLKSRLGELK 450
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 522838240 525 GRAARA---EEELRKKQAYVEKVERLQQALGQLQAACEKREQLELRLRTRLEQELKAL-----RAQQRQ 585
Cdd:pfam12128 451 LRLNQAtatPELLLQLENFDERIERAREEQEAANAEVERLQSELRQARKRRDQASEALrqasrRLEERQ 519
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
367-634 |
9.15e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 46.29 E-value: 9.15e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522838240 367 AHLAQMEAVLRENARLQRDNERLQRELESSAEKAGRIEKL-ESEIQRLSEahesltrASSKREALEKTMRNKMDSEMRRL 445
Cdd:PTZ00121 1064 AHVGQDEGLKPSYKDFDFDAKEDNRADEATEEAFGKAEEAkKTETGKAEE-------ARKAEEAKKKAEDARKAEEARKA 1136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522838240 446 QDFNRDLRERLESANRRLASKTQEAQAGSQDMVAKLLAQSYEQQQEQEKLEREMALLRGAieDQRRRAELLEQALGNAQG 525
Cdd:PTZ00121 1137 EDARKAEEARKAEDAKRVEIARKAEDARKAEEARKAEDAKKAEAARKAEEVRKAEELRKA--EDARKAEAARKAEEERKA 1214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522838240 526 RAARAEEELRKKQAyVEKVERLQQALGQLQAACEKREQLELRlrtRLEQELKALRAQQRQAGAPGGSSGSGGSPELSALR 605
Cdd:PTZ00121 1215 EEARKAEDAKKAEA-VKKAEEAKKDAEEAKKAEEERNNEEIR---KFEEARMAHFARRQAAIKAEEARKADELKKAEEKK 1290
|
250 260
....*....|....*....|....*....
gi 522838240 606 LSEQLREKEEQILALEADMTKWEQKYLEE 634
Cdd:PTZ00121 1291 KADEAKKAEEKKKADEAKKKAEEAKKADE 1319
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
499-630 |
9.25e-05 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 46.08 E-value: 9.25e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522838240 499 MALLRGAIEDQRRRAELLEQALGNAQG---RAARAEEELRKKQAYVEKVERLQQALGQLQAACEKREQLELRLRTRLEQE 575
Cdd:COG1196 634 AALRRAVTLAGRLREVTLEGEGGSAGGsltGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAE 713
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 522838240 576 LKALRAQQRQAGAPGGSSGSGGSPELSALRLSEQLREKEEQILALEADMTKWEQK 630
Cdd:COG1196 714 EERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELERE 768
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
369-541 |
1.02e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 45.91 E-value: 1.02e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522838240 369 LAQMEAVLRENARLQRDNERLQRELESSAEKAGRIEKLESEIQRLSEAHESLTRASSKREALE--KTMRNKMDSEMRRLQ 446
Cdd:COG4717 70 LKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQelEALEAELAELPERLE 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522838240 447 DFN------RDLRERLESANRRLASKTQEAQAGSQDMVAKLLAQSYEQQQEQEKLEREMALLRGAIEDQRRRAELLEQAL 520
Cdd:COG4717 150 ELEerleelRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEEL 229
|
170 180
....*....|....*....|.
gi 522838240 521 GNAQGRAARAEEELRKKQAYV 541
Cdd:COG4717 230 EQLENELEAAALEERLKEARL 250
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
367-557 |
1.20e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 45.53 E-value: 1.20e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522838240 367 AHLAQMEAVLRENARLQRDNERLQRELESSAEkagRIEKLESEIQRLSEAHESLTRASSKREALE--KTMRNKMDSEMRR 444
Cdd:COG4717 71 KELKELEEELKEAEEKEEEYAELQEELEELEE---ELEELEAELEELREELEKLEKLLQLLPLYQelEALEAELAELPER 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522838240 445 LQDFNRDLRErLESANRRLASKTQEAQAGSQDMVAKLLAQSYEQQQEQEKLEREMALLRGAIEDQRRRAELLEQALGNAQ 524
Cdd:COG4717 148 LEELEERLEE-LRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELE 226
|
170 180 190
....*....|....*....|....*....|...
gi 522838240 525 GRAARAEEELRKKQAYvekvERLQQALGQLQAA 557
Cdd:COG4717 227 EELEQLENELEAAALE----ERLKEARLLLLIA 255
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
369-539 |
1.86e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 45.29 E-value: 1.86e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522838240 369 LAQMEAVLRENARLQRDNERLQRELESSAEKAGRIEK----------LESEIQRLSEAHESLTRASSKREALEKTmRNKM 438
Cdd:COG4913 619 LAELEEELAEAEERLEALEAELDALQERREALQRLAEyswdeidvasAEREIAELEAELERLDASSDDLAALEEQ-LEEL 697
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522838240 439 DSEMRRLQDFNRDLRERLESANRRLASKTQEAQAgsqdmvAKLLAQSYEQQQEQEKLEREMALLRGAIEDQRRR--AELL 516
Cdd:COG4913 698 EAELEELEEELDELKGEIGRLEKELEQAEEELDE------LQDRLEAAEDLARLELRALLEERFAAALGDAVERelRENL 771
|
170 180
....*....|....*....|...
gi 522838240 517 EQALGNAQGRAARAEEELRKKQA 539
Cdd:COG4913 772 EERIDALRARLNRAEEELERAMR 794
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
508-635 |
2.82e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 44.52 E-value: 2.82e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522838240 508 DQRRRAELLEQALGNAQGRAARAEEELRKKQAYVEKVERLQQALGQLQ----------AACEKREQLELRLR-------- 569
Cdd:COG4913 607 DNRAKLAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAeyswdeidvaSAEREIAELEAELErldassdd 686
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 522838240 570 -TRLEQELKALRAQQRQAGAPGGSSGSGGSPELSAL-RLSEQLREKEEQILALEADMTKWEQKYLEER 635
Cdd:COG4913 687 lAALEEQLEELEAELEELEEELDELKGEIGRLEKELeQAEEELDELQDRLEAAEDLARLELRALLEER 754
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
502-710 |
7.76e-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: 43.12 E-value: 7.76e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522838240 502 LRGAIEDQRRRAELLEQALGNAQGRAARAEEELRKKQAYVEKVERLQQALGQLQAACEKREQLELRLRTRLEQELKALrA 581
Cdd:TIGR02168 682 LEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTEL-E 760
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522838240 582 QQRQAGAPGGSSGSGGSPELSALR--LSEQLREKEEQILALEADMTKWEQKYLEERAMRQFAMDAAATAAAQRDTTLIRH 659
Cdd:TIGR02168 761 AEIEELEERLEEAEEELAEAEAEIeeLEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRL 840
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 522838240 660 SPQPSPSSSFNEGLLTGGHRHQEMESRLKVLHAQILEKDAVIKVLQQRSRR 710
Cdd:TIGR02168 841 EDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALAL 891
|
|
| HlpA |
COG2825 |
Periplasmic chaperone for outer membrane proteins, Skp family [Cell wall/membrane/envelope ... |
369-470 |
8.92e-04 |
|
Periplasmic chaperone for outer membrane proteins, Skp family [Cell wall/membrane/envelope biogenesis, Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 442073 [Multi-domain] Cd Length: 171 Bit Score: 40.97 E-value: 8.92e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522838240 369 LAQMEAVLRENARLQRDNERLQRELESsaeKAGRIEKLESEIQRlseahESLTRASSKREALEKTMRNKMDSEMRRLQDF 448
Cdd:COG2825 35 LQESPEGKAAQKKLEKEFKKRQAELQK---LEKELQALQEKLQK-----EAATLSEEERQKKERELQKKQQELQRKQQEA 106
|
90 100
....*....|....*....|..
gi 522838240 449 NRDLRERLESANRRLASKTQEA 470
Cdd:COG2825 107 QQDLQKRQQELLQPILEKIQKA 128
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
376-571 |
9.42e-04 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 42.80 E-value: 9.42e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522838240 376 LRENARL----QRDNERLQRELESsaekAGRIEKLESEIQRlseaheSLTRASSKREALEKTMRNKMDSEMRRLQDFN-R 450
Cdd:pfam17380 377 MRELERLqmerQQKNERVRQELEA----ARKVKILEEERQR------KIQQQKVEMEQIRAEQEEARQREVRRLEEERaR 446
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522838240 451 DL-RERLESANR-----RLASKTQEAQAGSQDMVAKLLAQSYEQQQEQEKLEREMALLRGAIEDQRRRAELLEQALGNAQ 524
Cdd:pfam17380 447 EMeRVRLEEQERqqqveRLRQQEEERKRKKLELEKEKRDRKRAEEQRRKILEKELEERKQAMIEEERKRKLLEKEMEERQ 526
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 522838240 525 GRAA-----RAEEELRKKQAYVEKVERLQQalgQLQAACEKREQLELRLRTR 571
Cdd:pfam17380 527 KAIYeeerrREAEEERRKQQEMEERRRIQE---QMRKATEERSRLEAMERER 575
|
|
| OmpH |
smart00935 |
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH ... |
369-470 |
9.59e-04 |
|
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH among others. Skp (OmpH) has been characterized as a molecular chaperone that interacts with unfolded proteins as they emerge in the periplasm from the Sec translocation machinery.
Pssm-ID: 214922 [Multi-domain] Cd Length: 140 Bit Score: 40.26 E-value: 9.59e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522838240 369 LAQMEAVLRENARLQRDNERLQRELESSAEKagrIEKLESEIQRlseahESLTRASSKREALEKTMrNKMDSEMRRL-QD 447
Cdd:smart00935 10 LQESPAGKAAQKQLEKEFKKRQAELEKLEKE---LQKLKEKLQK-----DAATLSEAAREKKEKEL-QKKVQEFQRKqQK 80
|
90 100
....*....|....*....|...
gi 522838240 448 FNRDLRERLESANRRLASKTQEA 470
Cdd:smart00935 81 LQQDLQKRQQEELQKILDKINKA 103
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
378-615 |
1.46e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 42.44 E-value: 1.46e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522838240 378 ENARLQRDNERLqrELESSAEKAGRIE--KLESEIQRLSEAH--ESLTRASSKREALE--KTMRNKMDSEMRRLQDFNRD 451
Cdd:PTZ00121 1143 EEARKAEDAKRV--EIARKAEDARKAEeaRKAEDAKKAEAARkaEEVRKAEELRKAEDarKAEAARKAEEERKAEEARKA 1220
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522838240 452 LRERLESANRRLASKTQEAQAGSQdmvAKLLAQSYEQQQEQEKLEREMALLRGAIE-DQRRRAELLEQALGNAQGRAARA 530
Cdd:PTZ00121 1221 EDAKKAEAVKKAEEAKKDAEEAKK---AEEERNNEEIRKFEEARMAHFARRQAAIKaEEARKADELKKAEEKKKADEAKK 1297
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522838240 531 EEELRKKQAYVEKVERLQQALGQLQAACEKREQLELRLRTRLEQELKALRAQQRQAGAPGGSSGSGGSPELSALRLSEQL 610
Cdd:PTZ00121 1298 AEEKKKADEAKKKAEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAK 1377
|
....*
gi 522838240 611 REKEE 615
Cdd:PTZ00121 1378 KKADA 1382
|
|
| HOOK |
pfam05622 |
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ... |
370-626 |
1.65e-03 |
|
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from different eukaryotic organizms. The different members of the human gene family are HOOK1, HOOK2 and HOOK3. Different domains have been identified in the three human HOOK proteins, and it was demonstrated that the highly conserved NH2-domain mediates attachment to microtubules, whereas this central coiled-coil motif mediates homodimerization and the more divergent C-terminal domains are involved in binding to specific organelles (organelle-binding domains). It has been demonstrated that endogenous HOOK3 binds to Golgi membranes, whereas both HOOK1 and HOOK2 are localized to discrete but unidentified cellular structures. In mice the Hook1 gene is predominantly expressed in the testis. Hook1 function is necessary for the correct positioning of microtubular structures within the haploid germ cell. Disruption of Hook1 function in mice causes abnormal sperm head shape and fragile attachment of the flagellum to the sperm head. This entry includes the central coiled-coiled domain and the divergent C-terminal domain.
Pssm-ID: 461694 [Multi-domain] Cd Length: 528 Bit Score: 41.98 E-value: 1.65e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522838240 370 AQMEAVLRENARL--QRDNER-LQRELESSAEKAGRIEKLESEIQRLSEAHESLTRASSKREALEKTMRnkmdsemrrLQ 446
Cdd:pfam05622 218 EKLEALQKEKERLiiERDTLReTNEELRCAQLQQAELSQADALLSPSSDPGDNLAAEIMPAEIREKLIR---------LQ 288
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522838240 447 DFNRDLRERLESANRRLASKTQEAQAGSQDMVAKLLAQSYEQQQEQEKLEREMALLRGAIEDQRRRAE---LLEQALGNA 523
Cdd:pfam05622 289 HENKMLRLGQEGSYRERLTELQQLLEDANRRKNELETQNRLANQRILELQQQVEELQKALQEQGSKAEdssLLKQKLEEH 368
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522838240 524 QGRAARAEEELRKKQAYVEKVE-----RLQQALGQLQAACEKREQ----LELRLRTRLEQE---LKALRAQQRQagapgg 591
Cdd:pfam05622 369 LEKLHEAQSELQKKKEQIEELEpkqdsNLAQKIDELQEALRKKDEdmkaMEERYKKYVEKAksvIKTLDPKQNP------ 442
|
250 260 270
....*....|....*....|....*....|....*
gi 522838240 592 ssgsGGSPELSALRlsEQLREKEEQILALEADMTK 626
Cdd:pfam05622 443 ----ASPPEIQALK--NQLLEKDKKIEHLERDFEK 471
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
357-579 |
1.86e-03 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 41.97 E-value: 1.86e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522838240 357 AQASSATSGSAHLAQMEAVLRENARLQRDNERLQRELESSAEKAGRIEKLESEIQRLSEAHESLTRAsskREALEkTMRN 436
Cdd:TIGR02168 794 LKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAE---IEELE-ELIE 869
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522838240 437 KMDSEMRRLQDFNRDLRERLESANRRLASKTQEAQAGSQDMVAkllaqsyeqqqeqekleremalLRGAIEDQRRRAELL 516
Cdd:TIGR02168 870 ELESELEALLNERASLEEALALLRSELEELSEELRELESKRSE----------------------LRRELEELREKLAQL 927
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 522838240 517 EQALGNAQGRAARAEEELRkkqayvEKVERLQQALGQLQAACE-KREQLELRLRtRLEQELKAL 579
Cdd:TIGR02168 928 ELRLEGLEVRIDNLQERLS------EEYSLTLEEAEALENKIEdDEEEARRRLK-RLENKIKEL 984
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
369-585 |
2.95e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 41.18 E-value: 2.95e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522838240 369 LAQMEAVLRENARLQRDNERLQRE---------------LESSAEKAGRIEKLESEIQRLSEAHESLTRASSKREALEKT 433
Cdd:PRK02224 428 EAELEATLRTARERVEEAEALLEAgkcpecgqpvegsphVETIEEDRERVEELEAELEDLEEEVEEVEERLERAEDLVEA 507
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522838240 434 MRNKMDSEMRR--LQDFNRDLRERLESANRRLASKTQEAQAGSQDMVAKllaqsyeqqqeqeklEREMALLRGAIEDQRR 511
Cdd:PRK02224 508 EDRIERLEERRedLEELIAERRETIEEKRERAEELRERAAELEAEAEEK---------------REAAAEAEEEAEEARE 572
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 522838240 512 RAELLEQALGNAQGRAaraeEELRKKQAYVEKVERLQQALGQLQaacEKREQLELRLRTRLEQeLKALRAQQRQ 585
Cdd:PRK02224 573 EVAELNSKLAELKERI----ESLERIRTLLAAIADAEDEIERLR---EKREALAELNDERRER-LAEKRERKRE 638
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
388-585 |
3.06e-03 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 40.29 E-value: 3.06e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522838240 388 RLQRELESSAEKAGRIEKLESEIQRLSEAHESL-TRASSKREALEKtmrnkMDSEMRRLQDFNRDLRERLESANRRL--A 464
Cdd:COG1579 11 DLQELDSELDRLEHRLKELPAELAELEDELAALeARLEAAKTELED-----LEKEIKRLELEIEEVEARIKKYEEQLgnV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522838240 465 SKTQEAQAgsqdmvakllaqsyeqqqeqekleremalLRGAIEDQRRRAELLEQALGNAQGRAARAEEELRKKQayvEKV 544
Cdd:COG1579 86 RNNKEYEA-----------------------------LQKEIESLKRRISDLEDEILELMERIEELEEELAELE---AEL 133
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 522838240 545 ERLQQALGQLQAACEKREQlelrlrtRLEQELKALRAQQRQ 585
Cdd:COG1579 134 AELEAELEEKKAELDEELA-------ELEAELEELEAEREE 167
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
357-614 |
4.40e-03 |
|
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: 40.98 E-value: 4.40e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522838240 357 AQASSATSGSAHLAQMEAVLRE--NARLQRDNERLQRELESSAEKAGRI----------EKLESEIQRLSEAHESLTRAS 424
Cdd:pfam12128 405 ARDRQLAVAEDDLQALESELREqlEAGKLEFNEEEYRLKSRLGELKLRLnqatatpellLQLENFDERIERAREEQEAAN 484
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522838240 425 SKREAL---EKTMRNKMDSEMRRLQDFNRDLRERlesANRRLASKTQ-EAQAGS------------QDMVAKLLAQSYEQ 488
Cdd:pfam12128 485 AEVERLqseLRQARKRRDQASEALRQASRRLEER---QSALDELELQlFPQAGTllhflrkeapdwEQSIGKVISPELLH 561
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522838240 489 Q-----QEQEKLEREMALLRG--------------AIEDQ-RRRAELLEQALGNAQGRAARAEEEL-------------- 534
Cdd:pfam12128 562 RtdldpEVWDGSVGGELNLYGvkldlkridvpewaASEEElRERLDKAEEALQSAREKQAAAEEQLvqangelekasree 641
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522838240 535 -RKKQAYVEKVERLQQALGQLQAACEKREQLELRLRTRLEQELKALRAQQRQAGAPGGSSGSGGSPELSALRLSEQLREK 613
Cdd:pfam12128 642 tFARTALKNARLDLRRLFDEKQSEKDKKNKALAERKDSANERLNSLEAQLKQLDKKHQAWLEEQKEQKREARTEKQAYWQ 721
|
.
gi 522838240 614 E 614
Cdd:pfam12128 722 V 722
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
367-635 |
5.90e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 40.14 E-value: 5.90e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522838240 367 AHLAQMEAVLRENARLQRDNERLQRELESSAEKAGRIEKLESEIQRLSEAHESLTRASSKREALEKTMRNKMDS------ 440
Cdd:COG4717 112 EELREELEKLEKLLQLLPLYQELEALEAELAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQlslate 191
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522838240 441 -EMRRLQDFNRDLRERLESANRRLASKTQEAQAGSQDMVAKLLAQSYEQQQEQEKLEREMALLRGAI------------- 506
Cdd:COG4717 192 eELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERLKEARLLLLIAAALlallglggsllsl 271
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522838240 507 -------------------EDQRRRAELLEQALGNAQGRAARAEEELRKKQAYVEK-----------VERLQQALGQLQA 556
Cdd:COG4717 272 iltiagvlflvlgllallfLLLAREKASLGKEAEELQALPALEELEEEELEELLAAlglppdlspeeLLELLDRIEELQE 351
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522838240 557 ACEKREQLELRLRT-RLEQELKALRAQQRQAGAPGGSSGSGGSPELSALRlsEQLREKEEQILALEADMTKWEQKYLEER 635
Cdd:COG4717 352 LLREAEELEEELQLeELEQEIAALLAEAGVEDEEELRAALEQAEEYQELK--EELEELEEQLEELLGELEELLEALDEEE 429
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
370-580 |
9.70e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 39.66 E-value: 9.70e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522838240 370 AQMEAVLRENARLQRDNERLQRELEssaekagrieKLESEIQRLSEAHESLTRASSKREALEKTMRnKMDSEMRRLQDFN 449
Cdd:PRK03918 200 KELEEVLREINEISSELPELREELE----------KLEKEVKELEELKEEIEELEKELESLEGSKR-KLEEKIRELEERI 268
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522838240 450 RDLRER---LESANRRLASKTQEAQAGSQdmVAKLLAQSYEQQQEQEKLEREMALLRGAIEDQRRRAELLEQALGNAQGR 526
Cdd:PRK03918 269 EELKKEieeLEEKVKELKELKEKAEEYIK--LSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEELKKK 346
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 522838240 527 AARAEEELRKKQAYVEKVERLQQALGQLQAACEKREQLELRlrtRLEQELKALR 580
Cdd:PRK03918 347 LKELEKRLEELEERHELYEEAKAKKEELERLKKRLTGLTPE---KLEKELEELE 397
|
|
|