|
Name |
Accession |
Description |
Interval |
E-value |
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
353-512 |
1.60e-06 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 51.86 E-value: 1.60e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720415013 353 EEQEHLQGTVKSLREELGALQEQLLEKDLEMKQLLQSKIDLEKELETAREGEKGRQEQEQALREEVEALTKKCQELEEAK 432
Cdd:COG1196 260 AELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEEL 339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720415013 433 REEKNSFvavtHEAHPELHApspcSRHSEPDSDNSAGEEgssqppapcsEERREAAIRTLQAQWKAHRRKKREAALDEAA 512
Cdd:COG1196 340 EELEEEL----EEAEEELEE----AEAELAEAEEALLEA----------EAELAEAEEELEELAEELLEALRAAAELAAQ 401
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
149-431 |
6.92e-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: 49.67 E-value: 6.92e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720415013 149 GPDFVRTLAEKKPDTGwvITGLKQRIFRLEQQCKEKDNTINKLQTdmkttNLEEMRIAMETYYEEIHRLQTLLASSEatg 228
Cdd:TIGR02168 656 RPGGVITGGSAKTNSS--ILERRREIEELEEKIEELEEKIAELEK-----ALAELRKELEELEEELEQLRKELEELS--- 725
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720415013 229 KKPMVEKKLGVKRQKKMSSALLNLTRSVQELTEENQSLKEDLDRMLSNSPTISkikgygdwskpRLLRRIAELEKKVS-S 307
Cdd:TIGR02168 726 RQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELA-----------EAEAEIEELEAQIEqL 794
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720415013 308 SESPKQSTSELVNPNPLVRSpSNISVQKQPKGDQSPEDlpKVAPCEEQ--------EHLQGTVKSLREELGALQEQLLEK 379
Cdd:TIGR02168 795 KEELKALREALDELRAELTL-LNEEAANLRERLESLER--RIAATERRledleeqiEELSEDIESLAAEIEELEELIEEL 871
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 1720415013 380 DLEMKQLLQSKIDLEKELETAREGEKGRQEQEQALREEVEALTKKCQELEEA 431
Cdd:TIGR02168 872 ESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREK 923
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
93-693 |
4.00e-05 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 47.04 E-value: 4.00e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720415013 93 SVYREKEDMY-DEIIELKKSLHMQKSDVDLMRTKLRRLEEENSRKDRQIEQLLDPSRGPDFVRTLAEKKPDTGW-VITGL 170
Cdd:pfam15921 331 SELREAKRMYeDKIEELEKQLVLANSELTEARTERDQFSQESGNLDDQLQKLLADLHKREKELSLEKEQNKRLWdRDTGN 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720415013 171 KQRIFRLEQQCKEKDNTINKLQTDMKTT------NLEEMRIAMETYYEEIHRLQTLLASSEATgkKPMVEKKLGVKRQKK 244
Cdd:pfam15921 411 SITIDHLRRELDDRNMEVQRLEALLKAMksecqgQMERQMAAIQGKNESLEKVSSLTAQLEST--KEMLRKVVEELTAKK 488
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720415013 245 MSsaLLNLTRSVQELT----------------------------EENQSLKEDLDRmLSNSPT----------------- 279
Cdd:pfam15921 489 MT--LESSERTVSDLTaslqekeraieatnaeitklrsrvdlklQELQHLKNEGDH-LRNVQTecealklqmaekdkvie 565
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720415013 280 --------ISKIKGYGDWSKPRLLRRIAELEKKVSSSESPKQSTSELVNPN-----PLVRSPSNISVQKQPKGDQSPEDL 346
Cdd:pfam15921 566 ilrqqienMTQLVGQHGRTAGAMQVEKAQLEKEINDRRLELQEFKILKDKKdakirELEARVSDLELEKVKLVNAGSERL 645
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720415013 347 PKVAPC-EEQEHLQGTVKSLREELGALQE--QLLEKDLEMK-------------QLLQSKIDLEKELETAREGEK----- 405
Cdd:pfam15921 646 RAVKDIkQERDQLLNEVKTSRNELNSLSEdyEVLKRNFRNKseemetttnklkmQLKSAQSELEQTRNTLKSMEGsdgha 725
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720415013 406 -----GRQEQEQALREEVEALTKKCQELEEAKREEKNsfvavtheahpelhapspcSRHSEPDSDNSAGEEGSSqppAPC 480
Cdd:pfam15921 726 mkvamGMQKQITAKRGQIDALQSKIQFLEEAMTNANK-------------------EKHFLKEEKNKLSQELST---VAT 783
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720415013 481 SEERREAAIRTLQAQWKAHRRK--KREAALDEAAtvLQAA------FRGHLARSKLVRSKVPDSRSPSLPGLLSplnQSS 552
Cdd:pfam15921 784 EKNKMAGELEVLRSQERRLKEKvaNMEVALDKAS--LQFAecqdiiQRQEQESVRLKLQHTLDVKELQGPGYTS---NSS 858
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720415013 553 PAPRVLSPISPAEENPTqeeaviviqsilrgylaqarfiasccreiaASSQRETVSLTPSGSASPPSLRASPGVIRKELC 632
Cdd:pfam15921 859 MKPRLLQPASFTRTHSN------------------------------VPSSQSTASFLSHHSRKTNALKEDPTRDLKQLL 908
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1720415013 633 asEELRETSASEPAPSVPYSAQGGHG-------DCPSSSSLEAvpSMKDAMCEERSSSPRSAGPSLAE 693
Cdd:pfam15921 909 --QELRSVINEEPTVQLSKAEDKGRApslgaldDRVRDCIIES--SLRSDICHSSSNSLQTEGSKSSE 972
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
96-421 |
2.36e-04 |
|
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: 44.43 E-value: 2.36e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720415013 96 REKEDMYDEIIELKKSLHMQKSDVDlmrTKLRRLEEENSRKDRQIEQLLDPSRGPDfvRTLAEKKPDTGWVITGLKQRIF 175
Cdd:pfam10174 411 RDKDKQLAGLKERVKSLQTDSSNTD---TALTTLEEALSEKERIIERLKEQRERED--RERLEELESLKKENKDLKEKVS 485
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720415013 176 RLEQQCKEKDNTINKLQTDM---------KTTNLEEMRIAMETYYEEIHRLQTLLASSEatgkkpmvEKKLGVKRQKKMS 246
Cdd:pfam10174 486 ALQPELTEKESSLIDLKEHAsslassglkKDSKLKSLEIAVEQKKEECSKLENQLKKAH--------NAEEAVRTNPEIN 557
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720415013 247 SALLNLTRSVQELTEENQSLKEDLDRMLSNSPTISKIKGYGDwskprllRRIAELEKKVSSSESPKQSTSELVNPNPLVR 326
Cdd:pfam10174 558 DRIRLLEQEVARYKEESGKAQAEVERLLGILREVENEKNDKD-------KKIAELESLTLRQMKEQNKKVANIKHGQQEM 630
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720415013 327 SPSNISVQKQPKgdqSPEDLPKVAPCEEQ-EHLQGTVKSLREELGAL-------QEQLLEKD-----------------L 381
Cdd:pfam10174 631 KKKGAQLLEEAR---RREDNLADNSQQLQlEELMGALEKTRQELDATkarlsstQQSLAEKDghltnlraerrkqleeiL 707
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 1720415013 382 EMKQ-LLQSKIDlEKE-----LETAREGEKGRQEQEQALREEVEAL 421
Cdd:pfam10174 708 EMKQeALLAAIS-EKDanialLELSSSKKKKTQEEVMALKREKDRL 752
|
|
| IQCD |
cd23767 |
IQ (isoleucine-glutamine) motif containing D (IQCD); IQCD, also called dynein regulatory ... |
501-532 |
3.49e-04 |
|
IQ (isoleucine-glutamine) motif containing D (IQCD); IQCD, also called dynein regulatory complex protein 10 (DRC10), belongs to the IQ motif-containing protein family which contains a C-terminal conserved IQ motif domain and two coiled-coil domains. The IQ motif ([ILV]QxxxRxxxx[RK]), where x stands for any amino-acid residue, interacts with calmodulin (CaM) in a calcium-independent manner and is present in proteins with a wide diversity of biological functions. The IQCD protein was found to primarily accumulate in the acrosome area of round and elongating spermatids of the testis during late stage of spermiogenesis and was then localized to the acrosome and tail regions of mature spermatozoa. The expression of IQCD follows the trajectory of acrosome development during spermatogenesis. IQCD is associated with neuroblastoma and neurodegenerative diseases, and is reported to interact with the nuclear retinoid X receptor in the presence of 9-cis-retinoic acid, thereby activating the transcriptional activity of the receptor.
Pssm-ID: 467745 [Multi-domain] Cd Length: 37 Bit Score: 38.29 E-value: 3.49e-04
10 20 30
....*....|....*....|....*....|..
gi 1720415013 501 RKKREAALDEAATVLQAAFRGHLARSKLVRSK 532
Cdd:cd23767 1 EEEELQRMNRAATLIQALWRGYKVRKELKKKK 32
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
96-434 |
1.20e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 42.33 E-value: 1.20e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720415013 96 REKEDMYDEIIELKKSLHMQKSDVDLMRTKLRRLEEENSRKDRQIEQLLDpsRGPDFVRTLAEKKPDTGWV---ITGLKQ 172
Cdd:PRK02224 272 REREELAEEVRDLRERLEELEEERDDLLAEAGLDDADAEAVEARREELED--RDEELRDRLEECRVAAQAHneeAESLRE 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720415013 173 RIFRLEQQCKEKDNTINKLQTDmkttnLEEMRIAMETYYEEIHRLQTLLASSEAtgkkpmvekklgvkrqkkmssALLNL 252
Cdd:PRK02224 350 DADDLEERAEELREEAAELESE-----LEEAREAVEDRREEIEELEEEIEELRE---------------------RFGDA 403
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720415013 253 TRSVQELTEENQSLKEDLDRmlsnsptiskikgygdwskprLLRRIAELEKKVSSSESPKQSTSELVNPNplvrspsnis 332
Cdd:PRK02224 404 PVDLGNAEDFLEELREERDE---------------------LREREAELEATLRTARERVEEAEALLEAG---------- 452
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720415013 333 vqKQPKGDQSPEDLPKVAPCEEQEhlqGTVKSLREELGALQEQL--LEKDLE-----------MKQLLQSKIDLEKELET 399
Cdd:PRK02224 453 --KCPECGQPVEGSPHVETIEEDR---ERVEELEAELEDLEEEVeeVEERLEraedlveaedrIERLEERREDLEELIAE 527
|
330 340 350
....*....|....*....|....*....|....*
gi 1720415013 400 AREGEKGRQEQEQALREEVEALTKKCQELEEAKRE 434
Cdd:PRK02224 528 RRETIEEKRERAEELRERAAELEAEAEEKREAAAE 562
|
|
| PHA03307 |
PHA03307 |
transcriptional regulator ICP4; Provisional |
433-706 |
1.25e-03 |
|
transcriptional regulator ICP4; Provisional
Pssm-ID: 223039 [Multi-domain] Cd Length: 1352 Bit Score: 42.47 E-value: 1.25e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720415013 433 REEKNSFVAVTHEAHPELHAPSPCSRHSEPDSDNSAGEEGSSQP--PAPCSEERREAAIRTLQAQWKAHRRKKREAALDE 510
Cdd:PHA03307 80 PANESRSTPTWSLSTLAPASPAREGSPTPPGPSSPDPPPPTPPPasPPPSPAPDLSEMLRPVGSPGPPPAASPPAAGASP 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720415013 511 AATVLQAAFRGHLAR-SKLVRSKV--PDSRSPSLPGLLSPLNQSSPAPRVLSPISPAEENPTQEEAVIVIQSILRGYLAQ 587
Cdd:PHA03307 160 AAVASDAASSRQAALpLSSPEETAraPSSPPAEPPPSTPPAAASPRPPRRSSPISASASSPAPAPGRSAADDAGASSSDS 239
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720415013 588 ArfiASCCREIAASSQRETVSLTPSGSASPPSLRASPGVIRKELCASEELRETSASEPAPSV-PYSAQGGHGDCPSSSSL 666
Cdd:PHA03307 240 S---SSESSGCGWGPENECPLPRPAPITLPTRIWEASGWNGPSSRPGPASSSSSPRERSPSPsPSSPGSGPAPSSPRASS 316
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 1720415013 667 EAVPSMKDAMCEERSSSPRSAGPSLAEPSPPELQPLSPPP 706
Cdd:PHA03307 317 SSSSSRESSSSSTSSSSESSRGAAVSPGPSPSRSPSPSRP 356
|
|
| IQ |
smart00015 |
Calmodulin-binding motif; Short calmodulin-binding motif containing conserved Ile and Gln ... |
508-528 |
2.69e-03 |
|
Calmodulin-binding motif; Short calmodulin-binding motif containing conserved Ile and Gln residues.
Pssm-ID: 197470 [Multi-domain] Cd Length: 23 Bit Score: 35.76 E-value: 2.69e-03
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
234-434 |
3.50e-03 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 40.77 E-value: 3.50e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720415013 234 EKKLGVKRQKKMSSALLNLTRSVQELTEENQSLKEDLDRMLSNSPTISKIKGYGDwskprLLRRIAELEkkvsssespkq 313
Cdd:COG3206 213 EAKLLLQQLSELESQLAEARAELAEAEARLAALRAQLGSGPDALPELLQSPVIQQ-----LRAQLAELE----------- 276
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720415013 314 stselvnpnplvrspSNISVQKQPKGDQSPEdlpkvapceeqehlqgtVKSLREELGALQEQLLEkdlEMKQLLQSkidL 393
Cdd:COG3206 277 ---------------AELAELSARYTPNHPD-----------------VIALRAQIAALRAQLQQ---EAQRILAS---L 318
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1720415013 394 EKELETAREGEKGRQEQEQALREEVEALTKKCQELEEAKRE 434
Cdd:COG3206 319 EAELEALQAREASLQAQLAQLEARLAELPELEAELRRLERE 359
|
|
| IQ |
pfam00612 |
IQ calmodulin-binding motif; Calmodulin-binding motif. |
510-528 |
5.14e-03 |
|
IQ calmodulin-binding motif; Calmodulin-binding motif.
Pssm-ID: 459869 Cd Length: 21 Bit Score: 34.99 E-value: 5.14e-03
|
| Adgb_C_mid-like |
cd22307 |
C-terminal middle region of Androglobins (Adgbs) and related proteins; including permuted ... |
395-537 |
6.62e-03 |
|
C-terminal middle region of Androglobins (Adgbs) and related proteins; including permuted globin domain and IQ motif; Androglobin (Adgb, also known as Calpain-7-like protein, CAPN7L) is a large multidomain protein consisting of an N-terminal peptidase C2 family calpain-like domain, an IQ calmodulin-binding motif, and an internal, circularly permuted globin domain. The canonical secondary structure of hemoglobins is an 3-over-3 alpha-helical sandwich structure, where the eight alpha-helical segments are conventionally labeled, A-H, according to their sequential order; Adgbs differ from this in having helices C-H followed by A-B. Adgbs and other phylogenetically ancient globins, such as neuroglobins and globin X, form hexacoordinated heme iron complexes. Globins contain various highly conserved residues of the heme pocket: including a Phe in the interhelical position CD1 (Phe CD1, first position in the loop between the helices C and D) that is packed against the heme, a His at the 7th position of the E-helix (His E7) that binds the heme iron distally, and a His at the 8th position of the F-helix (His F8) that binds the heme iron proximally. Unlike other hexacoordinated globins, Adgbs have an E7 Gln; their hexacoordination scheme is [Gln]-Fe-[His]. In mammals, Adgb is mainly expressed in the testes and may play an important role in spermatogenesis. Arthropod Adgbs have degenerate globin domains (DOI:10.3389/fgene.2020.00858). This model spans the permuted globin domain, the IQ motif, and a conserved region of about 200 amino acid residues located C-terminal to the globin domain; it does not include the N-terminal protease domain or the large uncharacterized C-terminal domain of approximately 500 residues.
Pssm-ID: 412094 Cd Length: 416 Bit Score: 39.46 E-value: 6.62e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720415013 395 KELETA-----REGEKGRQEQEQALREEVEALTKKCQELEEAKrEEKNSFVAVTHEahpelhaPSPCSRHSEPDSDNSAG 469
Cdd:cd22307 57 KELYRSycpplLWSKEDKKEHHKVFNEALYHLLKKALGRKETP-DELFALRALFLD-------PDIGLEYKESPSSSLRE 128
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1720415013 470 EEGSSqppaPCSEERREAAIRtlqaqwkahrrkkreaaLDEAATVLQAAFRGHLARsKLVRSKVPDSR 537
Cdd:cd22307 129 IVEPD----ECDCRTREPTIE-----------------EHEAATKIQAFFRGTLVR-KLLKAHKPGTK 174
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
353-512 |
1.60e-06 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 51.86 E-value: 1.60e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720415013 353 EEQEHLQGTVKSLREELGALQEQLLEKDLEMKQLLQSKIDLEKELETAREGEKGRQEQEQALREEVEALTKKCQELEEAK 432
Cdd:COG1196 260 AELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEEL 339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720415013 433 REEKNSFvavtHEAHPELHApspcSRHSEPDSDNSAGEEgssqppapcsEERREAAIRTLQAQWKAHRRKKREAALDEAA 512
Cdd:COG1196 340 EELEEEL----EEAEEELEE----AEAELAEAEEALLEA----------EAELAEAEEELEELAEELLEALRAAAELAAQ 401
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
149-431 |
6.92e-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: 49.67 E-value: 6.92e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720415013 149 GPDFVRTLAEKKPDTGwvITGLKQRIFRLEQQCKEKDNTINKLQTdmkttNLEEMRIAMETYYEEIHRLQTLLASSEatg 228
Cdd:TIGR02168 656 RPGGVITGGSAKTNSS--ILERRREIEELEEKIEELEEKIAELEK-----ALAELRKELEELEEELEQLRKELEELS--- 725
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720415013 229 KKPMVEKKLGVKRQKKMSSALLNLTRSVQELTEENQSLKEDLDRMLSNSPTISkikgygdwskpRLLRRIAELEKKVS-S 307
Cdd:TIGR02168 726 RQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELA-----------EAEAEIEELEAQIEqL 794
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720415013 308 SESPKQSTSELVNPNPLVRSpSNISVQKQPKGDQSPEDlpKVAPCEEQ--------EHLQGTVKSLREELGALQEQLLEK 379
Cdd:TIGR02168 795 KEELKALREALDELRAELTL-LNEEAANLRERLESLER--RIAATERRledleeqiEELSEDIESLAAEIEELEELIEEL 871
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 1720415013 380 DLEMKQLLQSKIDLEKELETAREGEKGRQEQEQALREEVEALTKKCQELEEA 431
Cdd:TIGR02168 872 ESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREK 923
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
336-434 |
1.52e-05 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 48.32 E-value: 1.52e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720415013 336 QPKGDQSPEDLPKVAPCEEQEH------LQGTVKSLREELGALQEQLLEKDLEMKqllqskiDLEKELETAR--EGEKGR 407
Cdd:COG2433 390 LPEEEPEAEREKEHEERELTEEeeeirrLEEQVERLEAEVEELEAELEEKDERIE-------RLERELSEARseERREIR 462
|
90 100
....*....|....*....|....*...
gi 1720415013 408 QEQE-QALREEVEALTKKCQELEEAKRE 434
Cdd:COG2433 463 KDREiSRLDREIERLERELEEERERIEE 490
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
104-436 |
1.68e-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: 1.68e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720415013 104 EIIELKKSLHMQKSDVDLMRTKLRRLEEENSRKDRQIEQLLDpsrgpdfvrtlaeKKPDTGWVITGLKQRIFRLEQQCKE 183
Cdd:TIGR02168 678 EIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRK-------------ELEELSRQISALRKDLARLEAEVEQ 744
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720415013 184 KDNTINKLQTdmkttNLEEMRIAMETYYEEIHRLQTLLASSEAtgkkpmvEKKLGVKRQKKMSSALLNLTRSVQELTEEN 263
Cdd:TIGR02168 745 LEERIAQLSK-----ELTELEAEIEELEERLEEAEEELAEAEA-------EIEELEAQIEQLKEELKALREALDELRAEL 812
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720415013 264 QSLKEDLDRMLSNSPTISKIKGYGDWSKPRLLRRIAELEKKVSS--------SESPKQSTSELVnpnplvrSPSNISVQK 335
Cdd:TIGR02168 813 TLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESlaaeieelEELIEELESELE-------ALLNERASL 885
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720415013 336 QPKGDQSPEDLPKVApcEEQEHLQGTVKSLREELGALQEQLLEKDLEMKQL------LQSKI--DLEKELETAREGEKGR 407
Cdd:TIGR02168 886 EEALALLRSELEELS--EELRELESKRSELRRELEELREKLAQLELRLEGLevridnLQERLseEYSLTLEEAEALENKI 963
|
330 340 350
....*....|....*....|....*....|....*..
gi 1720415013 408 QEQEQALREEVEALTKKCQEL--------EEAKREEK 436
Cdd:TIGR02168 964 EDDEEEARRRLKRLENKIKELgpvnlaaiEEYEELKE 1000
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
353-532 |
3.32e-05 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 47.24 E-value: 3.32e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720415013 353 EEQEHLQGTVKSLREELGALQEQLLEKDLEMKQLLQSKIDLEKELETAREGEKGRQEQEQALREEVEALTKKCQELEEAK 432
Cdd:COG1196 281 LELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAEL 360
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720415013 433 REEKNSFVAVTHEAHPELHApspcsRHSEPDSDNSAGEEGSSQppapcsEERREAAIRTLQAQwkAHRRKKREAALDEAA 512
Cdd:COG1196 361 AEAEEALLEAEAELAEAEEE-----LEELAEELLEALRAAAEL------AAQLEELEEAEEAL--LERLERLEEELEELE 427
|
170 180
....*....|....*....|
gi 1720415013 513 TVLQAAFRGHLARSKLVRSK 532
Cdd:COG1196 428 EALAELEEEEEEEEEALEEA 447
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
353-528 |
3.94e-05 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 47.24 E-value: 3.94e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720415013 353 EEQEHLQGTVKSLREELGALQEQLLEKDLEMKQLLQSKIDLEKELETAREGEKGRQEQEQALREEVEALTKKCQELEEAK 432
Cdd:COG1196 351 EELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEAL 430
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720415013 433 REEKNSFVAVTHEAHPELHApspcsrhsepDSDNSAGEEGSSQPPAPCSEERREAAIRTLQAQWKAHRRKKREAALDEAA 512
Cdd:COG1196 431 AELEEEEEEEEEALEEAAEE----------EAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAE 500
|
170
....*....|....*.
gi 1720415013 513 TVLQAAFRGHLARSKL 528
Cdd:COG1196 501 ADYEGFLEGVKAALLL 516
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
93-693 |
4.00e-05 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 47.04 E-value: 4.00e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720415013 93 SVYREKEDMY-DEIIELKKSLHMQKSDVDLMRTKLRRLEEENSRKDRQIEQLLDPSRGPDFVRTLAEKKPDTGW-VITGL 170
Cdd:pfam15921 331 SELREAKRMYeDKIEELEKQLVLANSELTEARTERDQFSQESGNLDDQLQKLLADLHKREKELSLEKEQNKRLWdRDTGN 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720415013 171 KQRIFRLEQQCKEKDNTINKLQTDMKTT------NLEEMRIAMETYYEEIHRLQTLLASSEATgkKPMVEKKLGVKRQKK 244
Cdd:pfam15921 411 SITIDHLRRELDDRNMEVQRLEALLKAMksecqgQMERQMAAIQGKNESLEKVSSLTAQLEST--KEMLRKVVEELTAKK 488
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720415013 245 MSsaLLNLTRSVQELT----------------------------EENQSLKEDLDRmLSNSPT----------------- 279
Cdd:pfam15921 489 MT--LESSERTVSDLTaslqekeraieatnaeitklrsrvdlklQELQHLKNEGDH-LRNVQTecealklqmaekdkvie 565
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720415013 280 --------ISKIKGYGDWSKPRLLRRIAELEKKVSSSESPKQSTSELVNPN-----PLVRSPSNISVQKQPKGDQSPEDL 346
Cdd:pfam15921 566 ilrqqienMTQLVGQHGRTAGAMQVEKAQLEKEINDRRLELQEFKILKDKKdakirELEARVSDLELEKVKLVNAGSERL 645
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720415013 347 PKVAPC-EEQEHLQGTVKSLREELGALQE--QLLEKDLEMK-------------QLLQSKIDLEKELETAREGEK----- 405
Cdd:pfam15921 646 RAVKDIkQERDQLLNEVKTSRNELNSLSEdyEVLKRNFRNKseemetttnklkmQLKSAQSELEQTRNTLKSMEGsdgha 725
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720415013 406 -----GRQEQEQALREEVEALTKKCQELEEAKREEKNsfvavtheahpelhapspcSRHSEPDSDNSAGEEGSSqppAPC 480
Cdd:pfam15921 726 mkvamGMQKQITAKRGQIDALQSKIQFLEEAMTNANK-------------------EKHFLKEEKNKLSQELST---VAT 783
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720415013 481 SEERREAAIRTLQAQWKAHRRK--KREAALDEAAtvLQAA------FRGHLARSKLVRSKVPDSRSPSLPGLLSplnQSS 552
Cdd:pfam15921 784 EKNKMAGELEVLRSQERRLKEKvaNMEVALDKAS--LQFAecqdiiQRQEQESVRLKLQHTLDVKELQGPGYTS---NSS 858
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720415013 553 PAPRVLSPISPAEENPTqeeaviviqsilrgylaqarfiasccreiaASSQRETVSLTPSGSASPPSLRASPGVIRKELC 632
Cdd:pfam15921 859 MKPRLLQPASFTRTHSN------------------------------VPSSQSTASFLSHHSRKTNALKEDPTRDLKQLL 908
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1720415013 633 asEELRETSASEPAPSVPYSAQGGHG-------DCPSSSSLEAvpSMKDAMCEERSSSPRSAGPSLAE 693
Cdd:pfam15921 909 --QELRSVINEEPTVQLSKAEDKGRApslgaldDRVRDCIIES--SLRSDICHSSSNSLQTEGSKSSE 972
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
170-520 |
6.82e-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: 46.59 E-value: 6.82e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720415013 170 LKQRIFRLEQQC------KEKDNTINKLQTDMKTTNLEEMRIAMETYYEEIHRLQTLLAssEATGKKPMVEKKLGVKRqk 243
Cdd:TIGR02168 198 LERQLKSLERQAekaeryKELKAELRELELALLVLRLEELREELEELQEELKEAEEELE--ELTAELQELEEKLEELR-- 273
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720415013 244 kmsSALLNLTRSVQELTEENQSLKEDLDRmlsnsptiskikgygdwskprLLRRIAELEKKVSSsespkqstselvnpnp 323
Cdd:TIGR02168 274 ---LEVSELEEEIEELQKELYALANEISR---------------------LEQQKQILRERLAN---------------- 313
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720415013 324 LVRSPSNISVQKQPKGDQSPEDLPKVAPCEEQehlqgtVKSLREELGALQEQLLEKDLEMKQLLQSKIDLEKELETAREG 403
Cdd:TIGR02168 314 LERQLEELEAQLEELESKLDELAEELAELEEK------LEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSK 387
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720415013 404 EKGRQEQEQALREEVEALTKKCQELEEakREEKNSFVAVTHEAHPELHAPSPCSRHSEpdsdnsagEEGSSQPPAPCSEE 483
Cdd:TIGR02168 388 VAQLELQIASLNNEIERLEARLERLED--RRERLQQEIEELLKKLEEAELKELQAELE--------ELEEELEELQEELE 457
|
330 340 350
....*....|....*....|....*....|....*..
gi 1720415013 484 RREAAIRTLQAQwkahRRKKREAALDEAATVLQAAFR 520
Cdd:TIGR02168 458 RLEEALEELREE----LEEAEQALDAAERELAQLQAR 490
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
353-518 |
8.93e-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: 8.93e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720415013 353 EEQEHLQGTVKSLREELGALQEQLLEKDLEMKQLLQSKIDLEKELETAREGEKGRQEQEQALREEVEALTKKCQELEEAK 432
Cdd:COG1196 253 AELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEEL 332
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720415013 433 REEKnsfvAVTHEAHPELHApspcsrhSEPDSDNSAGEEGSSQppapCSEERREAAIRTLQAQWKAHRRKKREAALDEAA 512
Cdd:COG1196 333 EELE----EELEELEEELEE-------AEEELEEAEAELAEAE----EALLEAEAELAEAEEELEELAEELLEALRAAAE 397
|
....*.
gi 1720415013 513 TVLQAA 518
Cdd:COG1196 398 LAAQLE 403
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
102-437 |
1.99e-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: 45.05 E-value: 1.99e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720415013 102 YDEIIELKKSLHMQKSDVDLMRTKLRRLEEENSRKDRQIEQLLDpsrgpdFVRTLAEKKPDTGWVITGLKQRIFRLEQQC 181
Cdd:TIGR02168 231 VLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRL------EVSELEEEIEELQKELYALANEISRLEQQK 304
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720415013 182 KEKDNTINKLQTDMKTTN--LEEMRIAMETYYEEIHRLQTLLASSEatgkkpmVEKKLGVKRQKKMSSALLNLTRSVQEL 259
Cdd:TIGR02168 305 QILRERLANLERQLEELEaqLEELESKLDELAEELAELEEKLEELK-------EELESLEAELEELEAELEELESRLEEL 377
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720415013 260 TEENQSLKEDLDRMLSNSPTISKikgygdwskprllrRIAELEKKVSSSESpkqstselvnpnplvrspsnisvqKQPKG 339
Cdd:TIGR02168 378 EEQLETLRSKVAQLELQIASLNN--------------EIERLEARLERLED------------------------RRERL 419
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720415013 340 DQSPEDLPKVAPCEEQEHLQGTVKSLREELGALQEQLlekdlemKQLLQSKIDLEKELETAREGEKGRQEQEQALREEVE 419
Cdd:TIGR02168 420 QQEIEELLKKLEEAELKELQAELEELEEELEELQEEL-------ERLEEALEELREELEEAEQALDAAERELAQLQARLD 492
|
330
....*....|....*...
gi 1720415013 420 ALTKKCQELEEAKREEKN 437
Cdd:TIGR02168 493 SLERLQENLEGFSEGVKA 510
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
353-439 |
2.08e-04 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 44.12 E-value: 2.08e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720415013 353 EEQEHLQGTVKSLREELGALQEQLLEKDLEMKQLLQSKIDLEKELETAREGEKGRQEQEQALREEVEALTKKCQELEEAK 432
Cdd:COG4372 59 EELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQI 138
|
....*..
gi 1720415013 433 REEKNSF 439
Cdd:COG4372 139 AELQSEI 145
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
293-442 |
2.36e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 44.37 E-value: 2.36e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720415013 293 RLLRRIAELEKKVSSSESPKQSTSELVNPNPLVRSPSNISVQKQPKGDQSPEDLPKVAP----CEEQEHLQGTVKSLREE 368
Cdd:COG4717 99 ELEEELEELEAELEELREELEKLEKLLQLLPLYQELEALEAELAELPERLEELEERLEElrelEEELEELEAELAELQEE 178
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1720415013 369 LGALQEQL-LEKDLEMKQLLQSKIDLEKELETAREGEKGRQEQEQALREEVEALTKKCQELEEAKREEKNSFVAV 442
Cdd:COG4717 179 LEELLEQLsLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERLKEARLLLL 253
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
96-421 |
2.36e-04 |
|
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: 44.43 E-value: 2.36e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720415013 96 REKEDMYDEIIELKKSLHMQKSDVDlmrTKLRRLEEENSRKDRQIEQLLDPSRGPDfvRTLAEKKPDTGWVITGLKQRIF 175
Cdd:pfam10174 411 RDKDKQLAGLKERVKSLQTDSSNTD---TALTTLEEALSEKERIIERLKEQRERED--RERLEELESLKKENKDLKEKVS 485
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720415013 176 RLEQQCKEKDNTINKLQTDM---------KTTNLEEMRIAMETYYEEIHRLQTLLASSEatgkkpmvEKKLGVKRQKKMS 246
Cdd:pfam10174 486 ALQPELTEKESSLIDLKEHAsslassglkKDSKLKSLEIAVEQKKEECSKLENQLKKAH--------NAEEAVRTNPEIN 557
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720415013 247 SALLNLTRSVQELTEENQSLKEDLDRMLSNSPTISKIKGYGDwskprllRRIAELEKKVSSSESPKQSTSELVNPNPLVR 326
Cdd:pfam10174 558 DRIRLLEQEVARYKEESGKAQAEVERLLGILREVENEKNDKD-------KKIAELESLTLRQMKEQNKKVANIKHGQQEM 630
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720415013 327 SPSNISVQKQPKgdqSPEDLPKVAPCEEQ-EHLQGTVKSLREELGAL-------QEQLLEKD-----------------L 381
Cdd:pfam10174 631 KKKGAQLLEEAR---RREDNLADNSQQLQlEELMGALEKTRQELDATkarlsstQQSLAEKDghltnlraerrkqleeiL 707
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 1720415013 382 EMKQ-LLQSKIDlEKE-----LETAREGEKGRQEQEQALREEVEAL 421
Cdd:pfam10174 708 EMKQeALLAAIS-EKDanialLELSSSKKKKTQEEVMALKREKDRL 752
|
|
| IQCD |
cd23767 |
IQ (isoleucine-glutamine) motif containing D (IQCD); IQCD, also called dynein regulatory ... |
501-532 |
3.49e-04 |
|
IQ (isoleucine-glutamine) motif containing D (IQCD); IQCD, also called dynein regulatory complex protein 10 (DRC10), belongs to the IQ motif-containing protein family which contains a C-terminal conserved IQ motif domain and two coiled-coil domains. The IQ motif ([ILV]QxxxRxxxx[RK]), where x stands for any amino-acid residue, interacts with calmodulin (CaM) in a calcium-independent manner and is present in proteins with a wide diversity of biological functions. The IQCD protein was found to primarily accumulate in the acrosome area of round and elongating spermatids of the testis during late stage of spermiogenesis and was then localized to the acrosome and tail regions of mature spermatozoa. The expression of IQCD follows the trajectory of acrosome development during spermatogenesis. IQCD is associated with neuroblastoma and neurodegenerative diseases, and is reported to interact with the nuclear retinoid X receptor in the presence of 9-cis-retinoic acid, thereby activating the transcriptional activity of the receptor.
Pssm-ID: 467745 [Multi-domain] Cd Length: 37 Bit Score: 38.29 E-value: 3.49e-04
10 20 30
....*....|....*....|....*....|..
gi 1720415013 501 RKKREAALDEAATVLQAAFRGHLARSKLVRSK 532
Cdd:cd23767 1 EEEELQRMNRAATLIQALWRGYKVRKELKKKK 32
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
89-434 |
4.07e-04 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 43.90 E-value: 4.07e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720415013 89 VSGTSVY-REKEDMYDEIIELKKSLHMQKSDVDLMRTKLRRLEEENSRKDRQIEqLLDPSRGPDFVRTLAEKK------- 160
Cdd:TIGR02169 162 IAGVAEFdRKKEKALEELEEVEENIERLDLIIDEKRQQLERLRREREKAERYQA-LLKEKREYEGYELLKEKEalerqke 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720415013 161 ------PDTGWVITGLKQRIFRLEQQCKEKDNTINKLQTDMKTTNLEEMRiameTYYEEIHRLQTLLASSEATGKKPMVE 234
Cdd:TIGR02169 241 aierqlASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQL----RVKEKIGELEAEIASLERSIAEKERE 316
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720415013 235 KKLGVKRQKKMSSALLNLTRSVQELTEENQSLKEDLDRMLSNspTISKIKGYGDwskprLLRRIAELEKK----VSSSES 310
Cdd:TIGR02169 317 LEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEE--YAELKEELED-----LRAELEEVDKEfaetRDELKD 389
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720415013 311 PKQSTSELVNP-NPLVRSPSNISVQKQPKGdqspedlpkvapcEEQEHLQGTVKSLREELGALQEQLLEKDLEMKQllqs 389
Cdd:TIGR02169 390 YREKLEKLKREiNELKRELDRLQEELQRLS-------------EELADLNAAIAGIEAKINELEEEKEDKALEIKK---- 452
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 1720415013 390 kidLEKELETAREGEKGRQEQEQALREEVEALTKkcqELEEAKRE 434
Cdd:TIGR02169 453 ---QEWKLEQLAADLSKYEQELYDLKEEYDRVEK---ELSKLQRE 491
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
167-438 |
6.37e-04 |
|
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: 43.09 E-value: 6.37e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720415013 167 ITGLKQRIFRLEQQCKEKDNTINKLQTDMKTTNLEEmriamETYYEEIHRLQTLLASSEATGKKPMVEKKLGVKRQKKMS 246
Cdd:TIGR04523 77 IKILEQQIKDLNDKLKKNKDKINKLNSDLSKINSEI-----KNDKEQKNKLEVELNKLEKQKKENKKNIDKFLTEIKKKE 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720415013 247 SALLNLTRSVQELTEENQSLKEDLDRMLSNsptISKIKGYGDWSKPRLLRriaeLEKKVSSSESPKQSTSELVNP-NPLV 325
Cdd:TIGR04523 152 KELEKLNNKYNDLKKQKEELENELNLLEKE---KLNIQKNIDKIKNKLLK----LELLLSNLKKKIQKNKSLESQiSELK 224
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720415013 326 RSPSNISVQKQPKGDQSPEDLPKVAPCEEQehlqgtVKSLREELGALQEQLLEKDLEMKQLLQSKIDLEKELETAR-EGE 404
Cdd:TIGR04523 225 KQNNQLKDNIEKKQQEINEKTTEISNTQTQ------LNQLKDEQNKIKKQLSEKQKELEQNNKKIKELEKQLNQLKsEIS 298
|
250 260 270
....*....|....*....|....*....|....*
gi 1720415013 405 KGRQEQEQALREEV-EALTKKCQELEEAKREEKNS 438
Cdd:TIGR04523 299 DLNNQKEQDWNKELkSELKNQEKKLEEIQNQISQN 333
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
353-434 |
7.22e-04 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 42.58 E-value: 7.22e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720415013 353 EEQEHLQGTVKSLREELGALQEQLLEKDLEMKQLLQSKIDLEKELETAREGEKGRQEQEQALREEVEALTKKCQELEEAK 432
Cdd:COG4372 45 EELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKER 124
|
..
gi 1720415013 433 RE 434
Cdd:COG4372 125 QD 126
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
96-436 |
8.96e-04 |
|
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: 42.70 E-value: 8.96e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720415013 96 REKEDMYDEIIELKKSLHMQKSDVDLMRTKLRRLEEENSRKDRQIEQLLDPsrgpdfVRTLAEKKPDTGWVITGLKQRIF 175
Cdd:TIGR04523 321 KKLEEIQNQISQNNKIISQLNEQISQLKKELTNSESENSEKQRELEEKQNE------IEKLKKENQSYKQEIKNLESQIN 394
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720415013 176 RLEQQCKEKDNTINKLQTDMKTTNLEEmriamETYYEEIHRLQTLLASSEATGKKpmVEKKLGVKRQKKMSsalLNLTRS 255
Cdd:TIGR04523 395 DLESKIQNQEKLNQQKDEQIKKLQQEK-----ELLEKEIERLKETIIKNNSEIKD--LTNQDSVKELIIKN---LDNTRE 464
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720415013 256 VQElteenQSLKEdldrmLSNSptISKIKGYGDWSKprllrriAELEKKVSSSESPKQSTSELVNPNPLVRSPSNISVQK 335
Cdd:TIGR04523 465 SLE-----TQLKV-----LSRS--INKIKQNLEQKQ-------KELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEK 525
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720415013 336 QpkgdqspEDLPKVAPCEEQE--HLQGTVKSLREEL--GALQEQLLEKDLEMKQLLQSKIDLEKELETAREGEKGRQEQE 411
Cdd:TIGR04523 526 I-------EKLESEKKEKESKisDLEDELNKDDFELkkENLEKEIDEKNKEIEELKQTQKSLKKKQEEKQELIDQKEKEK 598
|
330 340
....*....|....*....|....*....
gi 1720415013 412 QALREEVEALTKKC----QELEEAKREEK 436
Cdd:TIGR04523 599 KDLIKEIEEKEKKIssleKELEKAKKENE 627
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
96-434 |
1.20e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 42.33 E-value: 1.20e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720415013 96 REKEDMYDEIIELKKSLHMQKSDVDLMRTKLRRLEEENSRKDRQIEQLLDpsRGPDFVRTLAEKKPDTGWV---ITGLKQ 172
Cdd:PRK02224 272 REREELAEEVRDLRERLEELEEERDDLLAEAGLDDADAEAVEARREELED--RDEELRDRLEECRVAAQAHneeAESLRE 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720415013 173 RIFRLEQQCKEKDNTINKLQTDmkttnLEEMRIAMETYYEEIHRLQTLLASSEAtgkkpmvekklgvkrqkkmssALLNL 252
Cdd:PRK02224 350 DADDLEERAEELREEAAELESE-----LEEAREAVEDRREEIEELEEEIEELRE---------------------RFGDA 403
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720415013 253 TRSVQELTEENQSLKEDLDRmlsnsptiskikgygdwskprLLRRIAELEKKVSSSESPKQSTSELVNPNplvrspsnis 332
Cdd:PRK02224 404 PVDLGNAEDFLEELREERDE---------------------LREREAELEATLRTARERVEEAEALLEAG---------- 452
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720415013 333 vqKQPKGDQSPEDLPKVAPCEEQEhlqGTVKSLREELGALQEQL--LEKDLE-----------MKQLLQSKIDLEKELET 399
Cdd:PRK02224 453 --KCPECGQPVEGSPHVETIEEDR---ERVEELEAELEDLEEEVeeVEERLEraedlveaedrIERLEERREDLEELIAE 527
|
330 340 350
....*....|....*....|....*....|....*
gi 1720415013 400 AREGEKGRQEQEQALREEVEALTKKCQELEEAKRE 434
Cdd:PRK02224 528 RRETIEEKRERAEELRERAAELEAEAEEKREAAAE 562
|
|
| PHA03307 |
PHA03307 |
transcriptional regulator ICP4; Provisional |
433-706 |
1.25e-03 |
|
transcriptional regulator ICP4; Provisional
Pssm-ID: 223039 [Multi-domain] Cd Length: 1352 Bit Score: 42.47 E-value: 1.25e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720415013 433 REEKNSFVAVTHEAHPELHAPSPCSRHSEPDSDNSAGEEGSSQP--PAPCSEERREAAIRTLQAQWKAHRRKKREAALDE 510
Cdd:PHA03307 80 PANESRSTPTWSLSTLAPASPAREGSPTPPGPSSPDPPPPTPPPasPPPSPAPDLSEMLRPVGSPGPPPAASPPAAGASP 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720415013 511 AATVLQAAFRGHLAR-SKLVRSKV--PDSRSPSLPGLLSPLNQSSPAPRVLSPISPAEENPTQEEAVIVIQSILRGYLAQ 587
Cdd:PHA03307 160 AAVASDAASSRQAALpLSSPEETAraPSSPPAEPPPSTPPAAASPRPPRRSSPISASASSPAPAPGRSAADDAGASSSDS 239
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720415013 588 ArfiASCCREIAASSQRETVSLTPSGSASPPSLRASPGVIRKELCASEELRETSASEPAPSV-PYSAQGGHGDCPSSSSL 666
Cdd:PHA03307 240 S---SSESSGCGWGPENECPLPRPAPITLPTRIWEASGWNGPSSRPGPASSSSSPRERSPSPsPSSPGSGPAPSSPRASS 316
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 1720415013 667 EAVPSMKDAMCEERSSSPRSAGPSLAEPSPPELQPLSPPP 706
Cdd:PHA03307 317 SSSSSRESSSSSTSSSSESSRGAAVSPGPSPSRSPSPSRP 356
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
448-732 |
1.51e-03 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 42.23 E-value: 1.51e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720415013 448 PELHAPSPCSRHSEPDSDNSAGEEGSSQPPAPcsEERREAAIRTLqaqwKAHRRKKREAALDEAATVLQAaFRGHLARSK 527
Cdd:PHA03247 2619 PDTHAPDPPPPSPSPAANEPDPHPPPTVPPPE--RPRDDPAPGRV----SRPRRARRLGRAAQASSPPQR-PRRRAARPT 2691
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720415013 528 LvrSKVPDSRSPSLPGllsplNQSSPAPRVLSPISPAEENPTQEEaviviQSILRGYLAQARFIASCCREIAASSQRETV 607
Cdd:PHA03247 2692 V--GSLTSLADPPPPP-----PTPEPAPHALVSATPLPPGPAAAR-----QASPALPAAPAPPAVPAGPATPGGPARPAR 2759
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720415013 608 SLTPSG--SASPPSLRASPGVIRKELCASEELRETSASEPAPSVPysaqgghgdcpsSSSLEAVPSMKDAMCEERSSSPR 685
Cdd:PHA03247 2760 PPTTAGppAPAPPAAPAAGPPRRLTRPAVASLSESRESLPSPWDP------------ADPPAAVLAPAAALPPAASPAGP 2827
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 1720415013 686 SAGPSLAEPSPPelqPLSPPPVEDICSDDSDDIIFSPFLPRKKSPSP 732
Cdd:PHA03247 2828 LPPPTSAQPTAP---PPPPGPPPPSLPLGGSVAPGGDVRRRPPSRSP 2871
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
362-525 |
2.07e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 41.44 E-value: 2.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720415013 362 VKSLREELGALQEQL--LEK-DLEMKQLLQSKIDLEKELETAREGEKGRQEQEQALREEVEALTKKCQELEEAKreekns 438
Cdd:COG4913 663 VASAEREIAELEAELerLDAsSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRL------ 736
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720415013 439 fvavtheahpelhapspcsrhsepdsdnSAGEEGSSQPPAPCSEERREAAIRTLQ----AQWKAHRRKKREAALDEAATV 514
Cdd:COG4913 737 ----------------------------EAAEDLARLELRALLEERFAAALGDAVerelRENLEERIDALRARLNRAEEE 788
|
170
....*....|.
gi 1720415013 515 LQAAFRGHLAR 525
Cdd:COG4913 789 LERAMRAFNRE 799
|
|
| IQ |
smart00015 |
Calmodulin-binding motif; Short calmodulin-binding motif containing conserved Ile and Gln ... |
508-528 |
2.69e-03 |
|
Calmodulin-binding motif; Short calmodulin-binding motif containing conserved Ile and Gln residues.
Pssm-ID: 197470 [Multi-domain] Cd Length: 23 Bit Score: 35.76 E-value: 2.69e-03
|
| PHA03378 |
PHA03378 |
EBNA-3B; Provisional |
460-733 |
3.20e-03 |
|
EBNA-3B; Provisional
Pssm-ID: 223065 [Multi-domain] Cd Length: 991 Bit Score: 40.82 E-value: 3.20e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720415013 460 SEPDSDNSAGEEGSSQP---PAPCSEERREAAIRTLQAqwkAHRRKKREAALDEAATVlqAAFRGHLARSKLVRSK---- 532
Cdd:PHA03378 369 CDPDEDKSGAEALASIPqtlPDPPTVYGRPKVFARKAD---LKSTKKCRAIVTDPSVI--KAIEEEHRKKKAARTEqpra 443
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720415013 533 VPDSRSPSLPgLLSPLNQSSPAP----RVLSPISPAEENP-TQEEAVIVIQSILRGYLAQARFIASCCREIAASSQRETV 607
Cdd:PHA03378 444 TPHSQAPTVV-LHRPPTQPLEGPtgplSVQAPLEPWQPLPhPQVTPVILHQPPAQGVQAHGSMLDLLEKDDEDMEQRVMA 522
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720415013 608 SLTPSGSASPPSLRASPGVIRKELCASEElretsasEPAPSVPYSAQggHGDCPSSSSLEAVPSMKDAMCEERSSSPRSA 687
Cdd:PHA03378 523 TLLPPSPPQPRAGRRAPCVYTEDLDIESD-------EPASTEPVHDQ--LLPAPGLGPLQIQPLTSPTTSQLASSAPSYA 593
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 1720415013 688 GPSL------AEPSPPELQplSPPPVEDICSDDSDDIIFSPFLPRKKSPSPF 733
Cdd:PHA03378 594 QTPWpvphpsQTPEPPTTQ--SHIPETSAPRQWPMPLRPIPMRPLRMQPITF 643
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
98-434 |
3.34e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 40.82 E-value: 3.34e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720415013 98 KEDMYDEIIELKKSLHMQKSDVDLMRTKLRRLEEENSRKDRQIEQL-----------LDPSRGPDFVRTLAEKKPDTGWV 166
Cdd:PRK03918 188 TENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELeelkeeieeleKELESLEGSKRKLEEKIRELEER 267
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720415013 167 ITGLKQRIFRLEQQCKEkdntINKLQTDMKTtnLEEMRIAMETYYEEIHRLQTLLA--SSEATG-KKPMVEKKLGVKRQK 243
Cdd:PRK03918 268 IEELKKEIEELEEKVKE----LKELKEKAEE--YIKLSEFYEEYLDELREIEKRLSrlEEEINGiEERIKELEEKEERLE 341
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720415013 244 KMSSALLNLTRSVQELtEENQSLKEDLDRMLSNSPTISKIKgyGDWSKPRLLRRIAELEK-KVSSSESPKQSTSELVNPN 322
Cdd:PRK03918 342 ELKKKLKELEKRLEEL-EERHELYEEAKAKKEELERLKKRL--TGLTPEKLEKELEELEKaKEEIEEEISKITARIGELK 418
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720415013 323 PLVRS-PSNISVQKQPKGdqspedlpKVAPCE---EQEHLQGTVKSLREELGALQEQLLEKDLEMKQLLQSKIDLEKELE 398
Cdd:PRK03918 419 KEIKElKKAIEELKKAKG--------KCPVCGrelTEEHRKELLEEYTAELKRIEKELKEIEEKERKLRKELRELEKVLK 490
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 1720415013 399 TAREGEKGRQ--EQEQALREE-----VEALTKKCQELEEAKRE 434
Cdd:PRK03918 491 KESELIKLKElaEQLKELEEKlkkynLEELEKKAEEYEKLKEK 533
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
234-434 |
3.50e-03 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 40.77 E-value: 3.50e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720415013 234 EKKLGVKRQKKMSSALLNLTRSVQELTEENQSLKEDLDRMLSNSPTISKIKGYGDwskprLLRRIAELEkkvsssespkq 313
Cdd:COG3206 213 EAKLLLQQLSELESQLAEARAELAEAEARLAALRAQLGSGPDALPELLQSPVIQQ-----LRAQLAELE----------- 276
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720415013 314 stselvnpnplvrspSNISVQKQPKGDQSPEdlpkvapceeqehlqgtVKSLREELGALQEQLLEkdlEMKQLLQSkidL 393
Cdd:COG3206 277 ---------------AELAELSARYTPNHPD-----------------VIALRAQIAALRAQLQQ---EAQRILAS---L 318
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1720415013 394 EKELETAREGEKGRQEQEQALREEVEALTKKCQELEEAKRE 434
Cdd:COG3206 319 EAELEALQAREASLQAQLAQLEARLAELPELEAELRRLERE 359
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
96-439 |
3.73e-03 |
|
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: 40.77 E-value: 3.73e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720415013 96 REKEDMYDEIielkKSLHMQKSDvdlMRTKLRRLEEENSRKDRQIEQLLDPSRgpdfvrtLAEKKpdtgwvITGLKQRIF 175
Cdd:TIGR04523 377 KENQSYKQEI----KNLESQIND---LESKIQNQEKLNQQKDEQIKKLQQEKE-------LLEKE------IERLKETII 436
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720415013 176 RLEQQCKEKDNTINKLQTDMKttNLEEMRIAMETYYEEIHRLQTLLASSEATGKKPMVEKKlgvkrqkkmsSALLNLTRS 255
Cdd:TIGR04523 437 KNNSEIKDLTNQDSVKELIIK--NLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKE----------KELKKLNEE 504
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720415013 256 VQELTEENQSLKEDldrmlsNSPTISKIKgygdwskpRLLRRIAELEKKVSSSESPKQSTSELVNPNPLVRSPSNISvQK 335
Cdd:TIGR04523 505 KKELEEKVKDLTKK------ISSLKEKIE--------KLESEKKEKESKISDLEDELNKDDFELKKENLEKEIDEKN-KE 569
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720415013 336 QPKGDQSPEDLPKvapceEQEHLQGTVKSLREELGALQEQLLEKDlemkqllQSKIDLEKELETAREGEKGRQEQEQALR 415
Cdd:TIGR04523 570 IEELKQTQKSLKK-----KQEEKQELIDQKEKEKKDLIKEIEEKE-------KKISSLEKELEKAKKENEKLSSIIKNIK 637
|
330 340
....*....|....*....|....
gi 1720415013 416 EEVEALTKKCQELEEAKREEKNSF 439
Cdd:TIGR04523 638 SKKNKLKQEVKQIKETIKEIRNKW 661
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
353-436 |
3.79e-03 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 40.69 E-value: 3.79e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720415013 353 EEQEHLQGTVKSLREELGALQEQLLEKDLEMKQLLQSKIDLEKELETAREGEKGRQEQEQALREEVEALTKKCQELEEAK 432
Cdd:COG1196 239 AELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERL 318
|
....
gi 1720415013 433 REEK 436
Cdd:COG1196 319 EELE 322
|
|
| EzrA |
pfam06160 |
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ... |
175-383 |
3.86e-03 |
|
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like cell-division protein FtsZ polymerizes into a ring structure that establishes the location of the nascent division site. EzrA modulates the frequency and position of FtsZ ring formation. The structure contains 5 spectrin like alpha helical repeats.
Pssm-ID: 428797 [Multi-domain] Cd Length: 542 Bit Score: 40.61 E-value: 3.86e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720415013 175 FRLEQQCKEKDNTINKLQTDMKTTNLEEMRIAMETYYEEIHRLQTLL-ASSEAtgkKPMVEKKLGvkrqkkmssallNLT 253
Cdd:pfam06160 233 LNVDKEIQQLEEQLEENLALLENLELDEAEEALEEIEERIDQLYDLLeKEVDA---KKYVEKNLP------------EIE 297
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720415013 254 RSVQELTEENQSLKEDLDRM-----LSNSpTISKIKGYGDWSKpRLLRRIAELEKKVsssESPKQSTSELvnpnplvrsp 328
Cdd:pfam06160 298 DYLEHAEEQNKELKEELERVqqsytLNEN-ELERVRGLEKQLE-ELEKRYDEIVERL---EEKEVAYSEL---------- 362
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1720415013 329 snISVQKQPKgdqspEDLPKVApcEEQEHLQGTVKSLREELGALQEQLLEKDLEM 383
Cdd:pfam06160 363 --QEELEEIL-----EQLEEIE--EEQEEFKESLQSLRKDELEAREKLDEFKLEL 408
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
96-451 |
4.42e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 40.41 E-value: 4.42e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720415013 96 REKEDMYDEIIELKKsLHMQKSDVDLMRTKLRRLEEENSRKDRQIEQlldpsrgpdfvrTLAEKKPdtgwviTGLKQRIF 175
Cdd:PRK02224 149 SDRQDMIDDLLQLGK-LEEYRERASDARLGVERVLSDQRGSLDQLKA------------QIEEKEE------KDLHERLN 209
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720415013 176 RLEQQCKEKDNTINKL--QTDMKTTNLEEMRIAMETYYEEIHRLQTLLASSEATgkkpmVEKKLGVKRQKKmssallNLT 253
Cdd:PRK02224 210 GLESELAELDEEIERYeeQREQARETRDEADEVLEEHEERREELETLEAEIEDL-----RETIAETERERE------ELA 278
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720415013 254 RSVQELTEENQSLKEDLDRMLSNSptiskikGYGDWSKPRLLRRIAELEKKVSSSEspkqstselvnpnplvrspsnisv 333
Cdd:PRK02224 279 EEVRDLRERLEELEEERDDLLAEA-------GLDDADAEAVEARREELEDRDEELR------------------------ 327
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720415013 334 qkqpkgdqspEDLPKVAPceEQEHLQGTVKSLREELGALQEQLLEKDLEMKqllqskiDLEKELETAREGEKGRQEQEQA 413
Cdd:PRK02224 328 ----------DRLEECRV--AAQAHNEEAESLREDADDLEERAEELREEAA-------ELESELEEAREAVEDRREEIEE 388
|
330 340 350
....*....|....*....|....*....|....*...
gi 1720415013 414 LREEVEALTKKCQELEEAkREEKNSFVAVTHEAHPELH 451
Cdd:PRK02224 389 LEEEIEELRERFGDAPVD-LGNAEDFLEELREERDELR 425
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
353-436 |
4.61e-03 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 40.31 E-value: 4.61e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720415013 353 EEQEHLQGTV-----KSLREELGALQEQLLEKDLEMKQLLQSKIDLEKELETAREGEKGRQEQEQALREEVEALTKKCQE 427
Cdd:COG1196 220 EELKELEAELlllklRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELAR 299
|
....*....
gi 1720415013 428 LEEAKREEK 436
Cdd:COG1196 300 LEQDIARLE 308
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
353-443 |
4.97e-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: 39.14 E-value: 4.97e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720415013 353 EEQEHLQGTVKSLREELGALQEQLLEKDLEMKQL------LQSKID-----------------LEKELETAREGEKGRQE 409
Cdd:COG1579 31 AELAELEDELAALEARLEAAKTELEDLEKEIKRLeleieeVEARIKkyeeqlgnvrnnkeyeaLQKEIESLKRRISDLED 110
|
90 100 110
....*....|....*....|....*....|....
gi 1720415013 410 QEQALREEVEALTKKCQELEEAKREEKNSFVAVT 443
Cdd:COG1579 111 EILELMERIEELEEELAELEAELAELEAELEEKK 144
|
|
| IQ |
pfam00612 |
IQ calmodulin-binding motif; Calmodulin-binding motif. |
510-528 |
5.14e-03 |
|
IQ calmodulin-binding motif; Calmodulin-binding motif.
Pssm-ID: 459869 Cd Length: 21 Bit Score: 34.99 E-value: 5.14e-03
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
353-434 |
5.84e-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: 39.14 E-value: 5.84e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720415013 353 EEQEHLQGTVKSLREELGALQEQLLEKDLEMKQLLQSKIDLEKELETAREGEKGRQEQ--------E-QALREEVEALTK 423
Cdd:COG1579 24 HRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQlgnvrnnkEyEALQKEIESLKR 103
|
90
....*....|.
gi 1720415013 424 KCQELEEAKRE 434
Cdd:COG1579 104 RISDLEDEILE 114
|
|
| Adgb_C_mid-like |
cd22307 |
C-terminal middle region of Androglobins (Adgbs) and related proteins; including permuted ... |
395-537 |
6.62e-03 |
|
C-terminal middle region of Androglobins (Adgbs) and related proteins; including permuted globin domain and IQ motif; Androglobin (Adgb, also known as Calpain-7-like protein, CAPN7L) is a large multidomain protein consisting of an N-terminal peptidase C2 family calpain-like domain, an IQ calmodulin-binding motif, and an internal, circularly permuted globin domain. The canonical secondary structure of hemoglobins is an 3-over-3 alpha-helical sandwich structure, where the eight alpha-helical segments are conventionally labeled, A-H, according to their sequential order; Adgbs differ from this in having helices C-H followed by A-B. Adgbs and other phylogenetically ancient globins, such as neuroglobins and globin X, form hexacoordinated heme iron complexes. Globins contain various highly conserved residues of the heme pocket: including a Phe in the interhelical position CD1 (Phe CD1, first position in the loop between the helices C and D) that is packed against the heme, a His at the 7th position of the E-helix (His E7) that binds the heme iron distally, and a His at the 8th position of the F-helix (His F8) that binds the heme iron proximally. Unlike other hexacoordinated globins, Adgbs have an E7 Gln; their hexacoordination scheme is [Gln]-Fe-[His]. In mammals, Adgb is mainly expressed in the testes and may play an important role in spermatogenesis. Arthropod Adgbs have degenerate globin domains (DOI:10.3389/fgene.2020.00858). This model spans the permuted globin domain, the IQ motif, and a conserved region of about 200 amino acid residues located C-terminal to the globin domain; it does not include the N-terminal protease domain or the large uncharacterized C-terminal domain of approximately 500 residues.
Pssm-ID: 412094 Cd Length: 416 Bit Score: 39.46 E-value: 6.62e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720415013 395 KELETA-----REGEKGRQEQEQALREEVEALTKKCQELEEAKrEEKNSFVAVTHEahpelhaPSPCSRHSEPDSDNSAG 469
Cdd:cd22307 57 KELYRSycpplLWSKEDKKEHHKVFNEALYHLLKKALGRKETP-DELFALRALFLD-------PDIGLEYKESPSSSLRE 128
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1720415013 470 EEGSSqppaPCSEERREAAIRtlqaqwkahrrkkreaaLDEAATVLQAAFRGHLARsKLVRSKVPDSR 537
Cdd:cd22307 129 IVEPD----ECDCRTREPTIE-----------------EHEAATKIQAFFRGTLVR-KLLKAHKPGTK 174
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
291-436 |
9.27e-03 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 39.34 E-value: 9.27e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720415013 291 KPRLLRRIAELEKKvssSESPKQSTSELVNPNPLVRSPSNISVQKQPKGDQSPEDL--PKVAPCEEQEHLQGTVKSLREE 368
Cdd:pfam17380 346 RERELERIRQEERK---RELERIRQEEIAMEISRMRELERLQMERQQKNERVRQELeaARKVKILEEERQRKIQQQKVEM 422
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1720415013 369 LGALQEQLLEKDLEMKQLLQSKidlEKELETAREGEKGRQEQEQALREEVEALTKKCQELEEAKREEK 436
Cdd:pfam17380 423 EQIRAEQEEARQREVRRLEEER---AREMERVRLEEQERQQQVERLRQQEEERKRKKLELEKEKRDRK 487
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
354-431 |
9.43e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 39.04 E-value: 9.43e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1720415013 354 EQEHLQGTVKSLREELGALQEQLLEKDLEMKQLLQSKIDLEKELETAregekgrQEQEQALREEVEALTKKCQELEEA 431
Cdd:COG3883 17 QIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEAL-------QAEIDKLQAEIAEAEAEIEERREE 87
|
|
| |
